CYANONEWS
Volume 9 Number 2 July 1993
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CYANONEWS - a newsletter intended to provide cyanobacteriologists with a
forum for rapid informal communication, unavailable through journals.
Everything you read in this newsletter is contributed by readers like
yourself. Published occasionally, about three times per year.
SUBSCRIPTIONS - $10 or equivalent/year for a hard copy. Free by E-Mail.
CONTRIBUTIONS - Expected every couple of years: a new result, an upcoming
meeting or a summary of a past meeting, a post-doctoral opening, a new
publication, a request for strains, a change of life... something. See
last page for addresses you can send news to.
HOW TO FIND OUT MORE ABOUT SOMETHING YOU READ HERE -Contact the person whose
name is capitalized in the news item. Addresses are given at the end of
the issue. Also, a Directory of Cyanobacteriologists is distributed every
two years.
INSTRUCTIONS TO AUTHORS - Send news.
COPYRIGHT - This newsletter is not copyrighted and no rights are reserved.
You are encouraged to reproduce or to transmit any part of this
publication by whatever means at your disposal, no permission required.
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CONTENTS
BULLETIN BOARD:
* Meetings
* Announcements
* Positions available
TRANSITIONS:
* Shanghao Li
NEWS:
* Fremyella,Nostoc plasmids share common features
* Dune cyanobacteria described, available
* Spirulina grown on citrus industry effluent
* Unique rubisco activase in heterocystous cyanos
* Red cyanobacteria infest coral reefs
* Genes encoding eukaryotic-type RNA-binding proteins
found in cyanobacteria
* Novel method to separate enantiomers: Application to homoanatoxin-a
COMMENTARY:
* AT-bias and phylogeny of prochlorophytes
MEETING REPORT:
* 1993 Cyanobacterial Workshop
REFERENCES
ADDRESSES
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BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD
The 10th AUSTRALIAN NITROGEN FIXATION CONFERENCE, to be held 7-10 Sep 1993
in Brisbane, will include symposia centered around several themes, some of
which may be: non-symbiotic N2 fixation, microbe-plant genetic interactions,
the role of molecular genetics in microbial ecology, nitrogen fixation in
agricultural production systems, and metabolic pathways associated with
nitrogen fixation.
Contact: H. Van Bushby, CSIRO Div of Tropical Crops & Pastures,
306 Carmody Road, Santa Lucia Qld 4067, Australia. (Fax) 61-7-3713946.
Or phone P. Dart (61-7-3652867) or Lex Diatloff (61-7-8779311).
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Umea, Sweden, will be the site of the EUCHEM-conference on ULTRAFAST
PROCESSES IN CHEMISTRY AND BIOLOGY, 13-16 June, 1994. Amongst the topics to
be addressed are energy transfer and electron transfer in photosynthesis.
Contact: The Swedish National Committee for Chemistry, Wallingatan 26
B, S-111 24 Stockholm. (Tel) 46-8-115280, (Fax) 46-8-106678.
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The 8th INTERNATIONAL SYMPOSIUM ON PHOTOTROPHIC PROKARYOTES is scheduled for
10-15 Sep 1994 in Urbino, Italy. In addition to themes common to previous
symposia, e.g., biogenesis, regulation, structure, and function of the
photosynthetic apparatus, metabolism, ecology, and taxonomy, the organizers
have added a new theme: basic and applied biotechnological processes
Contact: Stefano Ventura, CNR - Centro di Studio dei Microrganismi
Autotrofi, piazzale delle Cascine 27, I-50144 Firenze Italy.
(Tel) 39-55-350542, (Fax) 39-55-330431, (E-mail) Ventura@csma.fi.cnr.it
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The 6th AFRICAN ASSOCIATION FOR BIOLOGICAL NITROGEN FIXATION (AABNF)
CONFERENCE will be held in Harare, Zimbabwe, 12-17 September 1994, focusing
on the agronomic, socio-economic and environmental benefits of biological
nitrogen-fixing systems in Africa.
Contact: The Secretary, AABNF, Department of Soil Science, University
of Zimbabwe, Box MP 167, Mount Pleasant, Harare, Zimbabwe.
(Tel) 263-4-303211 ext 1412. (Fax) 263-4-732828. (Telex) 26580 UNIVZ
ZW. (Email) rcrust@zimbix.uz.zw (or) smoyo@zimbix.uz.zw
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The 8th EUROPEAN BIOENERGETICS CONFERENCE will be held in Valencia, Spain,
12-17 Sep 1994 and will emphasize several topics, including the structure of
energy-transfer proteins, electron-transport systems, light-harvesting
systems, reaction centers, and sodium bioenergetics and salt tolerance. Those
wishing to receive the second announcement should send their complete postal
address, telefax number and areas of interest.
Contact: Eduardo Rial, EBEC 94, Centro de Investigaciones Biologicas,
Velazquez 144, 28006 Madrid, Spain. (Fax) 34-1-5627518,
(Email) ciber12@cc.Csic.Es
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Next year's Gordon Conference on BIOPHYSICAL ASPECTS OF PHOTOSYNTHESIS is
tentatively scheduled for August 7-12, 1994. Suggestions regarding the
program (topics, speakers, format, etc.) are welcome. Also, alternative dates
for the meeting will be considered. Send your comments within the next two
months.
Contact: Marion Thurnauer, Argonne National Laboratory, 9700 S. Cass
Avenue, Argonne IL 60439 U.S.A. (Tel) 708-252-3545, (Fax) 708-252-9289,
(E-Mail) thurnauer@anlchm.chm.anl.gov or thurnaue@anlchm.bitnet
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There will be a TRAINING COURSE on FIELD AND LABORATORY TECHNIQUES FOR
SOUTH-EAST ASIA AND THE PACIFIC, entitled "Photosynthesis and Productivity
in a Changing Environment", 5-26 Jan 1994 in Bangkok, Thailand. The course
will cover a wide range of topics, including field photosynthesis
measurements, carbon and nitrogen assimilation, algal systems, and biofuels
and energy balance. Applications must arrive by 31st August, 1993 and should
include: (a) a detailed curriculum vitae, (b) a brief description of present
or proposed work and its relevance to the course program, and (c) a letter
of support from an employer or supervisor.
Contact (applicants from Thailand): Morakot Tanticharoen, School of
Bioresources and Technology, King Mongkut's Institute of Technology
Thonburi, Bangmod, Rasburana, Bangkok 10140. (Tel) 66-2-4270039
ext. 7000, (Fax) 66-2-4279062, 4278077, (Telex) 72383 KMITT TH.
Contact (applicants from other south-east Asian and Pacific countries:
David O. Hall, Division of Life Sciences, King's College London,
University of London, Campden Hill Road, London W8 7AH, UK.
(Tel) 44-71-3334317, (Fax) 44-71-9377783, (Telex) 8954102 BBSLON G.
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JIRI KIVIRANTA has completed and published his Ph.D. dissertation, entitled
Toxins of Cyanobacteria (Blue-Green Algae) -- a Biological and Chemical
Study. One main focus of his work was screening for cyanobacteria toxic to
mosquito larvae. The toxin most effective against mosquitos came from a
hepatotoxic fraction extracted from Microcystis aeruginosa strain 205. It was
analyzed and determined to be [Dha7]microcystin-RR.
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Judy Acreman has sent in a description of the UNIVERSITY OF TORONTO
CULTURE COLLECTION (UTCC), of which she is curator. The UTCC, officially
opened in 1987, makes available cyanobacterial cultures from a collection of
about 250 isolates of freshwater algae and cyanobacteria. One of the main
goals of the UTCC is to develop a collection of these organisms that is
representative of species native to Canada. Of particular interest are
isolates from areas under environmental stress, for example, acid-stressed
lakes, metal-polluted sites and organically polluted sites. There are
currently 40 isolates of 24 species of cyanobacteria in the collection, and
more will be added as new isolations proceed. Deposits of research cultures
are welcome, particularly those isolated from locations in Canada. To be
considered for deposit, the cultures should be positively identified at least
to genus and if not axenic, at least have only bacteria present as
contaminants.
In addition to distributing cultures, the UTCC also offers the following
services: a) custom-isolation of algae and cyanobacteria, b) training in
methods of isolation and culture of these organisms, c) safe-deposit of
cultures on a confidential basis, d) preparation of media.
To obtain a catalogue of species in culture or for further information
contact:
Judy Acreman, UTCC, Botany Department, University of Toronto, Toronto,
Ontario, Canada M5S 3B2. (Tel) 416-978-3641, (Fax) 416-978-5878,
(E-mail) JAcreman@botany.Utoronto.Ca
POSITIONS AVAILABLE
POSITION: Postdoc
CONTACT: Steve Theg, Section of Plant Biology, University of California,
Davis CA 95616 U.S.A. (Tel) 916-752-0624, (E-mail) SMTheg@UCDavis.Edu
START: After July 1, 1993
RESEARCH: Study the assembly and function of the three extrinsic subunits of
the photosynthetic oxygen evolving complex in chloroplasts. The long range
goals of the project are to identify specific amino acids involved in
holding the complex together and in imparting its biological activity.
The experimental approaches will lean heavily on techniques for random and
site-directed mutagenesis, in vitro chloroplast protein import, in vitro
protein reconstitution, and analysis of photosynthetic capacities by
various biophysical means.
REQUIREMENTS: Ideally, an intimate understanding of photosystem II reactions,
both theoretical and practical knowledge of molecular biology (cloning,
sequencing, etc.), experience in biophysical techniques applied to
chloroplast bioenergetics (i.e., fluorescence, spectroscopy, etc.), and
familiarity with the field of protein trafficking. Persons meeting some,
but not all, of these criteria are still encouraged to apply; clear
thinking, desire, and solid scientific training will go a long way in
filling in the gaps.
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POSITION: Post-doc
CONTACT: Peter Brzezinski, Department of Biochemistry and Biophysics,
Chalmers University of Technology, S-412 96 Goteborg, Sweden.
(Tel) 46-31-7722807, (Fax) 46-31-7722813,
(E-mail) Peter@Biofy2.Bcbp.Chalmers.Se
RESEARCH: Use various biophysical and genetic techniques to study bacterial
and plant photosynthesis. Current work in the project associated with the
position focuses on reconstitution of PSII in phospholipid vesicles and
time-resolved measurements of light-induced electrogenic events associated
with electron and proton transfer. There is great flexibility in the
design of the project.
SEND: A brief description of research interests, CV, and the names and
addresses of at least two references.
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POSITION: Post-doc
CONTACT: Terry Bricker, Dept. of Botany, Louisiana State University, Baton
Rouge LA 70803 U.S.A.
RESEARCH: Molecular biochemistry of photosynthesis. One position involves the
production and characterization of mutants in the CPa-1 protein of PS II
[Putnam-Evans & Bricker (92) Biochem 31:11482]. Another involves the study
of protein-protein interactions in PS II [Frankel & Bricker (92) Biochem
31:11059].
SUPPORT: Initially for 1 year.
START: Anticipated starting date Sept. 1 1993.
SEND: CV
TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TR
Shanghao Li (1917-1993)
Shanghao Li passed away suddenly on February 24, 1993 at the Institute of
Hydrobiology of the Chinese Academy of Science in Wuhan. He will be missed
in the scientific communities both in China and abroad as well as by those
of us who knew him directly or indirectly.
Shanghao Li was born in the Guangzou Province in China. He went to
Zhongshan University to study biology and joined the Institute of
Hydrobiology in the early 1950's. His early research focused on limnology and
the systematics of algae, especially diatoms and green algae. From the mid-
1970's, he studied the physiological ecology of cyanobacteria. He introduced
the method of applying on a grand scale Anabaena as a fertilizer in rice
fields, the success of which was immediately recognized by his colleagues and
by local farmers. The culture collection of algae at the Institute, including
cyanobacteria in his own laboratory, is among the best in Asia.
Shanghao Li was the author of numerous research papers and reviews and was
the editor of a number of books. He was often an invited speaker at
international conferences and also hosted many foreign colleagues in China.
He was elected a member of the Chinese Academy of Science in 1980, and in
1981 he was appointed Director of the Institute of Hydrobiology. He served
on several editorial boards of journals and publications (including
CyanoNews) and on organizing committees of conferences.
To those of us who knew him personally, Professor Li was an outstanding
scientist, a patient teacher, a giving friend, and a man of family. He always
found time for his students, his friends, and his family. We students learned
from his teaching to appreciate the good things in science and to gain
confidence in our research. He was ready to help but seldom mentioned any
unfairness to himself.
There were quite a few political movements in China against the educated,
and Professor Li survived each of them, as a cyanobacterium resists adverse
conditions. After 10 years of the Cultural Revolution, he was among the first
to remake contact with the world. He even participated in some political
processes to persuade the government to maintain an open door policy. Many
of his students went abroad to study various aspects of cyanobacteria. While
respecting their opinions, Professor Li always reminded his students that
there were opportunities in China and that China needed well-trained
scientists, not only for its scientific progress but also for its political
progress.
Shanghao Li was also talented in music and Chinese art and literature. He
enjoyed playing piano with his wife and loved walking with his grandson at
sunset along the coast of the beautiful East Lake, where the Institute of
Hydrobiology is located. His life exemplified all that is good in science and
in human beings, an he will be remembered that way.
Professor Li, we all miss you!
-- Jindong Zhao
NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NE
FREMYELLA,NOSTOC PLASMIDS SHARE COMMON FEATURES
MIKE SCHAEFER, recently arrived in his new position in Missouri, reports
a curious finding. He sequenced the origin of replication from pFdAI (a
shuttle vector used in Fremyella) and found it to be very similar to that of
plasmid pDU1, the plasmid from Nostoc PCC 7524 that is the basis for many
shuttle vectors used in Anabaena PCC 7120 and other strains. The similarity
includes an open reading frame of unknown function and regions of dyad
symmetry. Conceivably, the shuttle vectors developed for Anabaena may work
in Fremyella, and Fremyella vectors may work in Anabaenas and Nostocs. Has
anyone ever tried?
DUNE CYANOBACTERIA DESCRIBED, AVAILABLE
BOB WEBB, another recent arrivee at a new job, this one in Texas, has
isolated some new cyanobacteria from the gypsum dunes at White Sands, New
Mexico. He has two unicellular strains, three filamentous strains, and one
that grows in very short filaments, about four cells within a sheath. The
unicellular strains and two of the filamentous strains grow fairly well on
plates without nitrate. He invites anyone with a possible interest in these
strains to let him know: they are available.
SPIRULINA GROWN ON CITRUS INDUSTRY EFFLUENT
ROGERIO LACAZ-RUIZ has given us a progress report on how he, M.E. Kornfeld,
and M.A. Zanetti in Sao Paulo, Brazil, have used waste water from the citrus
industry to grow Spirulina platensis. The waste water was supplemented with
a wood ash alkaline solution, nitrogen, and phosphorus. They have received
a patent for this growth medium. Spirulina accumulated in this growth medium
at the rate of 0.5 mg/ml during a five day growth period, with little
contamination by green algae. The crude protein content of the biomass was
52% by dry weight. The medium costs US$1.37/liter, 4.2% less than CFTRI, an
alternative synthetic medium.
UNIQUE RUBISCO ACTIVASE IN HETEROCYSTOUS CYANOS
BOB TABITA let us know that his laboratory has identified in Anabaena sp.
strain CA three open reading frames downstream from rbcS, encoding the small
subunit of Rubisco. One, labeled rca, encodes Rubisco activase and lies about
2 kb downstream from rbcS. The other two have no recognizable function and
lie between rbcS and rca. Interestingly, rca from Anabaena CA does not show
clear hybridization to DNA from unicellular or nonheterocystous filamentous
cyanobacteria. There is very strong hybridization, however, to DNA from other
strains of Anabaena and Nostoc. The work has recently been published [Plant
Mol Biol 21:753-764].
RED CYANOBACTERIA INFEST CORAL REEFS
Recent times have seen a steady decline in the health of coral reef
ecosystems, and much of this decline may be attributable to coral diseases
associated with cyanobacteria. Two of the most common of the known diseases
affecting coral are black band disease and white band disease. In both cases,
a band of activity sweeps across the coral surface, destroying coral tissue.
Black band consists of a consortium of bacteria, in many ways analogous to
a microbial mat community. The color is due to phycoerythrin from the
dominant species, Phormidium corallyticum. Much less is known about white
band disease.
First black, then white... now LAURIE RICHARDSON tells us she has found
a new plague on corals: red band disease. In many ways red band is similar
to black band. The most obvious differences are that the band is brick red
in color and is dominated by a species of the genus Oscillatoria. Unlike
black band, however, red band progresses only in the light and at a much
slower rate of 1 mm per daylight period. It is not clear what controls
movement of the band. In the case of black band, control by light has been
excluded, raising the possibility that chemotaxis is involved.
In passing, it should be noted that red band disease has never been
observed outside the Bahamas. Scientists wishing to study the disease must
therefore be willing to spend a significant period in these tropical islands,
a point to consider when choosing an experimental system.
GENES ENCODING EUKARYOTIC-TYPE RNA-BINDING PROTEINS, FOUND IN CYANOBACTERIA
Those of us who study cyanobacteria often have an interest in eukaryotes
greater than that of your average bacteriologist. This situation arises in
part because at least one ancient member of our chosen class of organisms
snuck into a eukaryote a billion or so years ago, forcing us to comprehend
the behavior of the nucleus in order to appreciate the condition of these
chloroplast descendants. It was ironic, then, to hear two years ago [Kathe
et al (1990) Science 250:1566-1570; Kuhsel et al (1990) Science 250:1570-
1573] that cyanobacteria possess a gene with an intron, that eukaryotic
device previously unknown to bacterial genomes. MARTIN MULLIGAN now comes
with the news that the connection with eukaryotes appears stronger than we
thought. He tells us that heterocyst-forming cyanobacteria have multiple
genes encoding proteins that are similar to the RNP family of eukaryotic RNA-
binding proteins, a family that includes snRNP proteins (responsible for the
excision of introns) and certain regulatory proteins. Previous to this
account, such genes had not been discovered outside of the eukaryotes, unless
one counts chloroplasts as exceptions.
Three genes from two strains of cyanobacteria (Anabaena and
Chlorogloeopsis) have been sequenced. All three putative gene products
contain a single RNA Recognition Motif (RRM) that includes the highly
conserved RNP1 and RNP2 regions and all three have a short glycine-rich
carboxy-terminal tail. RNA-binding protein genes are abundant in heterocyst-
forming filamentous cyanobacteria but are not abundant in non-heterocyst-
forming filamentous or unicellular cyanobacteria, raising the possibility
that the cyanobacterial proteins may play a role in gene expression during
heterocyst differentiation. Although the exact function of the
cyanobacterial gene products is not yet known, their similarity to eukaryotic
proteins suggests that they may play a role in RNA processing - either in
splicing reactions or in processing the 3' end of nascent cyanobacterial
mRNA. The unexpected presence of these genes in cyanobacteria has some
intriguing implications for the evolution of RNA binding proteins and RNA
processing.
NOVEL METHOD TO SEPARATE ENANTIOMERS: APPLICATION TO HOMOANATOXIN-A
Homoanatoxin-a is the neurotoxic compound produced by Oscillatoria
formosa. A new gas chromatographic technique allows the enantiomer-specific
separation of the bicyclic secondary amine, reports OLAV SKULBERG, who
recently developed the procedure in collaboration with John-Erik Haugen and
Michael Oehme (Norwegian Institute for Air Research), Markus Mueller (Swiss
Federal Research Station), and Timothy Gallagher (University of Bristol).
Separation of cyanophyte neurotoxins into their enantiomers is of
considerable interest. The chemical synthesis of enantiomeric substances
gives a racemate (a precise 1:1 mixture of both enantiomers), while biogenic
formation normally results in a single enantiomer. In many cases, only one
of the enantiomers shows relevant bioactivity. The other is inactive or even
antagonistic. A simple technique to separate enantiomeric neurotoxins
permits:
1. confirmation of the enantiomeric purity of synthetically produced
neurotoxins that have been separated into single enantiomers by classical
techniques, such as the formation of diasteriomers.
2. Identification of the enantiomers formed by cyanophytes, and evaluation
of the enantiomer-specificity of the biosynthesis.
Recently, new routine gas chromatographic methods have been developed that
allow the trace level separation of enantiomers on special tailor-made
enantiomeric stationary phases. Such phases consist of a chiral modifier, for
example, a modified cyclodextrin dissolved in a methyl-phenyl-polysiloxane.
This technique permits the separation of the chiral neurotoxin homoanatoxin-a
into its enantiomers.
Homoanatoxin-a, from extracts of Oscillatoria formosa (NIVA-CYA 92) and
as a synthetic racemic mixture, was transformed into the heptafluorobutyryl
derivative by acylation to obtain a thermally more stable and less polar
compound suitable for gas chromatography. Compounds were detected by negative
ion chemical ionization mass spectrometry (NICI). Mass m/z 315 [M-3HF]- was
used to monitor the compounds in the NICI mode. Figure 1 shows that the
racemic mixture can be completely separated on a glass capillary column as
short as 12 m (0.32 mm i.d.) coated with 20% of a modified beta-cyclodextrin
dissolved in 85% methyl- 15% phenylpolysiloxane. It is evident that the water
extract from the culture of NIVA-CYA 92 contained only one enantiomer. At the
moment, the exact enantiomer conformation of each signal is unknown.
The method presented has the following advantages:
* Complete separation of enantiomers within 15 minutes
* Stationary phase is compatible with selective detection using an electron
capture detector or NICI mass spectrometry
* Selectivity and detection limits allow the quantification and enantiomeric
separation of subpicogram amounts, corresponding to sub-parts per billion
in water samples
[Figure 1 omitted in electronic version]
COMMENTARY: AT-BIAS AND PHYLOGENY OF PROCHLOROPHYTES
In Cyanonews Vol. 8, No. 1, Sean Turner outlined current evidence that no
known prochlorophyte is specifically related to the ancestor of the green
chloroplast and that none of the known prochlorophytes are related to each
other. These conclusions are supported by sequence data from 16S rRNA and
genes encoding RuBp carboxylase, ATP synthase, and DNA-dependent RNA
polymerase [for references see Cyanonews Vol. 8, No. 1, and Origins of
Plastids, R.A. Lewin editor, Chapman & Hall, 1993]. In Cyanonews Vol. 9,
No. 1, Chris Howe questioned these results. His argument was that the high
AT-bias of the chloroplast may artificially group it farther apart from
prochlorophytes with less AT-biased genomes or that unrelated organisms with
convergent %GC content may be grouped together.
This criticism ignores two points. The first is that most of the AT-bias
in genes is found in the third position of the codon. The analyses of RNA
polymerase sequence data, for example, did not use the third codon position
for this reason and for the reason that the organisms are too diverged for
this position to contain useful phylogenetic information. The %GC of the
first two codon positions alone of the RNA polymerase fragments of
Prochloron, Prochlorothrix, Prochlorococcus, and maize are quite similar so
that we expect much of the %GC-bias to have been removed.
As to the second point: What is the %GC of the genomes of different
prochlorophytes? The work of Herdman suggests that the genome of Prochloron
is 40.5% GC [Arch Microbiol (1981) 129:314-6]. The work of Burger-Wiersma,
et al. suggests that the genome of Prochlorothrix is 53% GC [Int J Systematic
Bacteriol (1989) 39:250-257]. We don't know the %GC of Prochlorococcus. Since
RNA polymerase is a highly expressed protein we would expect its codon usage
and %GC to reflect that of the organism. The %GC based on RNA polymerase
sequences does seem to match that of whole cyanobacterial genomes where each
are known (data not shown). Based on RNA polymerase gene sequences, the %GC
of Prochloron, Prochlorothrix, Prochlorococcus, and maize chloroplast can be
estimated as 42%, 56%, 41-35% (two strains), and 38%, respectively.
Prochlorococcus, in particular, clearly has a high AT-bias -- low %GC. The
third codon position alone is 32% GC and 20% GC, respectively, for two
strains of Prochlorococcus in culture, compared to 27% GC for maize
chloroplast (known to be low %GC) and 79% GC for WH8103, a marine Group A
Synechococcus (known to be high %GC).
Despite the apparent high AT-bias of Prochlorococcus, it still groups
closely with marine Group A Synechococcus and shares with them an amino acid
insertion in RNA polymerase found in no other known cyanobacteria. Even with
an AT-bias similar to that of the maize chloroplast, Prochlorococcus does not
group with the green chloroplast lineage. This result suggests that AT-bias
in RNA polymerase gene sequences in general has not been strong enough to
affect the major features of trees derived from those sequences.
Although one should always exercise caution in phylogenetic inferences,
sequence data from several molecules providing similar phylogenetic trees
supports the conclusion that the prochlorophytes are a polyphyletic group and
that none of the known prochlorophytes is related to the chloroplast lineage
(though one so related could still be discovered). Chlorophyll b synthesis
thus seems to be an ability either: (1) of ancient origin that has been lost
or has become cryptic in multiple cyanobacterial lineages, (2) that has
migrated by horizontal gene transfer, (3) that has arisen on multiple
occasions by independent mutations, or (4) any combination of the above.
- Brian Palenik
MEETING REPORT*MEETING REPORT*MEETING REPORT*MEETING REPORT*MEETING REPORT
The 1993 Cyanobacterial Workshop was held May 30 - June 2 at Asilomar
Conference Center, Pacific Grove California. The summaries below represent
only a slice of the hundred or so talks and posters contributed, not to
mention the scientific exchanges that took place against the roar of the
Pacific Ocean. The meeting was organized by Arthur Grossman (Stanford
University) and Mike Schaefer (University of Missouri-Kansas City) who
somehow managed to coordinate matters despite their separation by a couple
of thousand miles. As evidence that the coordination succeeded and was
appreciated by those in attendance, it was decided to model the next meeting
after this last (imitation being the sincerest form of flattery). The next
workshop will be held in 1995, also at Asilomar, organized by Don Bryant
(Pennsylvania State University) and Neil Straus (University of Toronto), who
have no excuses, since they're only about 400 miles apart.
Photosynthesis
Photosystem I (PS I): Don Bryant (Pennsylvania State University) reported
progress in studying the PS I complex from Synechococcus PCC 7002. In this
cyanobacterium, PS I is comprised of eleven polypeptides namely, PsaA, PsaB,
PsaC, PsaD, PsaE, PsaF, PsaI, PsaJ, PsaK, PsaL and PsaM. The genes encoding
all these polypeptides except PsaI, PsaM and PsaN have been cloned and
characterized. A combination of interposon mutagenesis and overproduction of
some of the above polypeptides in Escherichia coli was used to reveal
information about PS I. PsaD is required for stabilization and correct
orientation of PsaC on the PS I complex, and PsaE polypeptide is required for
cyclic electron transport. Wendy Schluchter (Pennsylvania State University)
told us that PsaK and PsaL mutants grow in DCMU but their growth rates are
slower in low light. PsaL- mutant do not form trimeric PS I complexes.
Furthermore, this mutant exhibits altered state transitions: energy transfer
from the phycobilisome to PS I is impaired. Vim Vermaas (Arizona State
University) reported that a PS I- mutant of Synechocystis PCC 6803 grows at
5 uE/m2תs of light if adapted properly and supplied with sugar. PS II in this
strain shows normal function, and electrons from plastoquinone go to
cytochrome oxidase instead.
Photosystem II (PS II): Himadri Pakrasi (Washington University, St. Louis)
reported complementation of SK18, a mutant of Synechocystis PCC 6803 that
does not have a functional PS II. The open reading frame (ORF) that was
complemented in the mutant shows similarity to a gene from E. coli, prcA,
that encodes a carboxy-terminal processing protease. Interposon mutagenesis
of this ORF in Synechocystis results in a larger D1 protein. Therefore, he
and his colleagues propose that this ORF (designated ctpA) encodes the
carboxy-terminal processing protease for the D1 protein.
Herbicide resistance: Sergei Shestakov (Moscow State University) reported
complementation of Synechocystis mutants that are resistant to the phenolic
herbicide, dinoseb, and the carotenoid biosynthesis inhibitor, difunone. Gene
inactivation experiments showed that the molecular basis of dinoseb
resistance is associated with the absence of the product of a gene designated
drgA. DrgA does not show homology with any known proteins. It was proposed
that drgA encodes a protein that is involved in the conversion of dinoseb and
metronidazole to highly toxic agents, perhaps through a ferredoxin-dependent
pathway. Difunone resistance results from either a 3 base pair deletion or
a duplication within the dfrA gene. dfrA encodes a product of 74.5 kDa. The
carboxy-terminus shows a helix-turn-helix domain and is homologous to phoR
from B. subtilis, which acts as transcriptional regulator.
Light regulation of psbA gene expression: Susan Golden (Texas A&M University)
gave an update on the differential expression of the psbA gene family in
Synechococcus PCC 7942. Genes psbAII and psbAIII are expressed at very low
levels when cells are grown at low light, but rapidly increase their
expression upon a shift to high light. The levels of psbAI message are high
in low light, but they drop dramatically within a few minutes upon a shift
to high light. After prolonged incubation in high light, the expression of
the psbAI message increased again to the same levels as is in low light.
After six hours in high light, the total psbA message is four times higher
than before the increase in light intensity. Systematic analysis of the
control regions of psbAII and psbAIII genes showed that three elements are
present upstream of the of each gene: a basal constitutive promoter, a
negative element upstream of the promoter, and a light-responsive element
downstream of the transcription site. The light-responsive elements increase
expression from the native promoter or a heterologous promoter in a position-
and orientation-independent manner indicating enhancer activity. However, the
ability to confer light-responsive expression is orientation-dependent. In
addition, low fluence blue light was shown to elicit the same changes in psbA
expression that are induced by exposure to high light. A pulse of red light
after exposure to blue light significantly attenuates the blue-light-mediated
increase in psbAII and psbAIII messages.
(Contributed by Nikos Tsinoremas)
Phycobilisomes
Walter Sidler (E.T.H., Zuerich) described how he and coworkers have
successfully reconstituted the rod core complex, (alpha-beta)6PCתLRC29.5ת
(alpha-beta)3APתLC8.9 from Mastigocladus laminosus. This reconstitution
required using linker polypeptide LRC29.5 which had been overexpressed in E.
coli. The authors suggested that this requirement might result from
proteolysis of LRC29.5 in preparations from M. laminosus. Hopefully this
reconstituted complex will form beautiful crystals suitable for X-ray
crystallography! The core-membrane linker (LCM) functions to organize the
allophycocyanin trimers within the core complex and thus determines the
overall shape of the phycobilisome. Core complexes with two cylinders
(Synechococcus PCC 6301) and three cylinders (Synechococcus PCC 7002) have
been previously characterized.
Axel Ducret (E.T.H., Zuerich) showed electron micrographs of core
complexes reconstituted from Anabaena PCC 7120. In his interpretation of the
data, a core complex consists of three cylinders plus an additional
allophycocyanin (AP) complex attached to each side of the top cylinder (i.e.
a three-and-two-halves-cylinder core complex). I wonder if a five cylinder
phycobilisome might occur in another species.
Samuel Beale (Brown University) reported evidence, derived from work on
Cyanidium caldarium ("cyanobacterium", honoris causa?), that supports an
interesting pathway of phycobilin synthesis. If this pathway is present
generally in cyanobacteria, then it should be possible to find
phycoerythrobilin in all cyanobacteria regardless of whether phycoerythrin
is synthesized. The pathway begins with the conversion of protoheme to
biliverdin IXalpha by heme oxygenase. Two enzymes are required to convert
biliverdin IXalpha to (3Z)-phycoerythrobilin. 15,16-dihydrobiliverdin IXalpha
is the intermediate in this conversion. The two enzymes each catalyse a
two-electron reduction, and require NADPH and ferredoxin. The isomerization
of (3Z)-phycoerythrobilin to (3Z)-phycocyanobilin requires a specific
isomerase. Z-to-E isomerizations of these latter two bilins is enzymatic and
requires glutathione.
Craig Fairchild (U.C. Berkeley) described his work two proteins, CpcE and
CpcF, required for the proper attachment of phycocyanobilin attachment to the
alpha subunit of phycocyanin (PC). These polypeptides were purified from
overexpressing E. coli and shown to associate with each other. The complex
(CpcEF) catalyses not only bilin attachment but also the transfer of bilin
from one alpha subunit to another. CpcEF also associates with PC and quenches
fluorescence emission.
The last three speakers described work on chromatic adaptation in
Fremyella diplosiphon. Michael Schaefer (University of Missouri, Kansas City)
described two mutants which fail to respond to red light. He and coworkers
at the Carnegie Institution, Stanford have complemented these mutants using
a mobilizable plasmid library. The complementing gene, designated rcaC, shows
strong identity to phoP, a regulatory protein involved in phosphate
metabolism in Bacillus subtilis. The exact role of rcaC in chromatic
adaptation is presently unknown.
Nancy Federspiel and colleagues (University of Idaho, Moscow) reported
progress on in vivo and in vitro footprinting of the promoter of the cpeBA
operon (cpeBA encodes the beta and alpha subunits of phycoerythrin). Using
dimethyl sulfate, they identified two G residues within the promoter that are
protected in DNA isolated from cultures grown in either red or green light.
They concluded, therefore, that the protecting factor is bound to the
promoter, independent of light quality. This conclusion differs from that
drawn by Nicole Tandeau de Marsac (Institut Pasteur) and coworkers, working
with the similar strain, Calothrix PCC 7601. They found that the same
residues were protected only in green light.
John Cobley (University of San Francisco) presented the recent work from
his laboratory concerning a mutant, F. diplosiphon SF48, that fails in green
light to assemble phycoerythrin into the phycobilisome. Using a mobilizable
cosmid library it was possible to complement this mutant and thereby clone
the complementing gene, which has been named cpeF. cpeF has more than 30%
sequence identity to both mpeV and mpeU, genes from Synechococcus WH8020.
CpeF most probably attaches a phycoerythrobilin to a specific cysteine in
phycoerythrin. It will be particularly interesting to see if the expression
of cpeF in F. diplosiphon is dependent on green light.
(Contributed by John Cobley)
Nitrogen Metabolism and Heterocyst Differentiation
Nitrogen Metabolism:
In Synechococcus PCC 7942, the genes involved in nitrate assimilation are
organized into a cluster, nirA-nrtABCD-narB, and expressed as an operon.
Tetsuo Omata (Nagoya University) reported the presence of two
ammonium-repressible genes in the region upstream of nirA. One open reading
frame (orf349) is required for the expression of maximal activity of nirA.
A mutant affected in the other (orf309) exhibits normal levels of nitrate
reductase and nitrite reductase activities but nonetheless grows slowly with
nitrate or nitrite as the nitrogen source. The predicted protein sequence
encoded by orf309 is similar to that of transcriptional regulators of the
LysR family.
Enrique Flores (Universidad de Sevilla) talked about a second regulatory
protein, NtcA, which is involved in transcriptional activation of ammonium
repressible genes. NtcA is found in a variety of unicellular, filamentous,
and heterocystous cyanobacteria. There is considerable sequence similarity
in the three ntcA genes that have been sequenced (from Synechococcus
PCC 7942, Synechocystis PCC 6803 and Anabaena PCC 7120), particularly in a
conserved helix-turn-helix motif. Footprinting studies indicate a consensus
binding sequence of GTA..N8..TACA, found with only minor variations upstream
from a number of nitrogen-regulated genes from different cyanobacteria. These
genes include nirA, glnA, hetA, hetR, patA, and ntcA itself.
T.S. Ramasubramanian (Texas A&M University) reported on the
characterization of a gene (bifA) of Anabaena PCC 7120 that is evidently
identical to ntcA (although the identification of the two genes were by
wholly different approaches). Analysis of the binding of BifA to glnA, xisA,
and rbcL upstream sequences yielded a consensus recognition sequence of
TGT..N9-10..ACA, very close to the sequence obtained by the Seville group.
BifA is present in both vegetative cells and heterocysts. A mutant in which
bifA had been insertionally inactivated failed to grow on N2 or nitrate.
Cyanothece BH68, a unicellular cyanobacterium showcased by Milagros Colon-
Lopez (Purdue University), exhibits the ability to fix nitrogen in the
presence of oxygen. When grown with an alternating light/dark cycle, N2-
fixation is restricted to the dark period and reaches peak activity at a time
coinciding with maximal respiratory activity. In a like fashion,
photosynthetic O2 evolution is confined to the light period, peaking 4-6 h
after the dark/light transition. The periodicity of N2-fixation is retained
when growth is shifted to continuous light. Richard Bradley (State University
of New York, Binghamton) suggested that Cyanothece may employ covalent
modification of nitrogenase as a form of post-translational control to
regulate nitrogenase activity. Western blot experiments using antibodies
directed against the Fe-subunit of nitrogenase revealed a band migrating at
38-kDa under conditions of aerobic nitrogenase activity and one at 40 Kda
under conditions in which nitrogenase activity was absent.
Heterocyst differentiation:
A number of talks and posters addressed the question of heterocyst
differentiation and patterned development. Francisco Leganes (Michigan State
University) sought a connection between the two developmental processes of
heterocyst and akinete differentiation. He isolated a number of mutants of
Nostoc ellipsosporum that are defective in the differentiation of both cell
types (and hence cannot fix nitrogen in the presence of air). The two
processes appear therefore to be related by a common mechanism.
Several groups have found genes turned on early in the response of
Anabaena PCC 7120 to nitrogen deprivation. Genes involved in nitrate
assimilation seem to be among the earliest induced, reported Yuping Cai
(Michigan State University). Bill Buikema (University of Chicago) passed on
news of a gene (pknA) encoding a eukaryotic-type serine/threonine protein
kinase, isolated from Anabaena by PCR. Transcripts of pknA begin to
accumulate 2.5 hr after nitrogen stepdown. Stephanie Curtis (North Carolina
State University) described the isolation of gnd, encoding 6-phosphogluconate
dehydrogenase. The gene has multiple transcripts, at least one of which
becomes more abundant at about 6 h after removal of fixed nitrogen from the
medium.
HetR is a gene required for heterocyst formation, which, we were told by
Yuping Cai, is essential for the expression of several genes induced during
the course of differentiation. Most remarkably, extra copies of hetR in wild
type Anabaena produces multiple heterocysts. Francisca Fernandez-Pinas
(Michigan State University) showed that extra copies of a newly discovered
gene, hetP, also produces multiple heterocysts. Mutation in hetP appears like
hetR- strains: no fragmentation and little if any sign of differentiation.
Other genes were described that are involved in unusual patterns of
heterocysts. Bill Buikema described patB, a gene induced 3 h after nitrogen
stepdown and whose predicted product has a DNA-binding motif in its carboxy
terminus. A mutation in patB shows increased heterocyst frequency. Jim Golden
(Texas A&M University) told us about a mutant strain PFM1 that has a patB--
like phenotype. A cosmid clone 8E11 that suppresses this phenotype was
identified and was found to suppress heterocyst development in wild type
Anabaena. A small fragment from 8E11 containing a 1200-bp ORF was sufficient
in multicopy to mimic the effect of the entire cosmid, but weirdly enough,
fragments containing sequences adjacent to the 1200 bp ORF on a high copy
shuttle vector had the opposite effect: it induced the formation of
heterocysts, even in nitrate-containing medium.
Todd Black (Michigan State University) showed work that support the idea
that lipid biosynthesis may be involved in heterocyst differentiation. A Het-
mutant was obtained by transposon mutagenesis, and sequences flanking the
transposon insertion were found to define an ORF that resembles beta-ketoacyl
reductases, involved in the synthesis of fatty acids, polyketides, and
several other compounds. Upstream from the first ORF was a second, whose
predicted product has domains also found in polyketide synthetases.
Downstream, and on the opposite strand, is an ORF that shows homology to a
gene from Bacillus subtilis encoding a regulatory gene. Reminiscent of the
Texas A&M group's results with PFM1 (above), extra copies of the first ORF
in Anabaena results in a Het- phenotype, and extra copies of the 3' ORF
stimulates double heterocyst formation. Extra copies of both ORFs together
yielded a normal phenotype.
Two DNA rearrangements are known to occur during heterocyst
differentiation in Anabaena PCC 7120. A third DNA rearrangement, which
involves the excision of about 11.5 kb of DNA, was reported by two groups.
Andrey Matveyev (Stockholm University) analyzed restriction patterns of
vegetative cell and heterocyst DNA by pulsed-field gel electrophoresis. Jim
Golden told how the same rearrangement was found in his laboratory during the
mapping of a cosmid isolated through the complementation of PFM1 (above).
(Contributed by TS Ramasubramanian and Nick Mann)
Redundancy and Response to Environmental Stress
One major theme of the 1993 Cyanobacterial Workshop was how cyanobacteria
respond to environmental stresses. It was clear from the workshop that we are
reaching a better appreciation of the cyanobacterial machinery for sensing
and responding to particular stresses. For example, Jackie Collier (Stanford
University) described a genetic approach to understanding how cyanobacteria
break down phycobilisomes in response to nitrogen- or sulfur-deprivation and
described a newly isolated gene, designated nblA, which is required for this
process.
Within the general theme of stress responses, however, it kept coming up
that many cyanobacteria are not necessarily optimized for maximum growth
under optimal conditions. Many have instead opted for "redundancy" as a way
of insuring survival under many conditions. This was demonstrated at the
meeting by the reports of many proteins which apparently duplicate the
functions of other proteins for reasons that are not clear. For example,
Javier Florencio (Universidad de Sevilla) described how Synechocystis
PCC 6803 has not one, but two genes encoding glutamine synthetase (GS). The
second one, referred to as glnT, exhibits low homologies (about 10%) with
other cyanobacterial GS's and instead is more similar to the GS of
Bacteroides fragilis. Filamentous nitrogen-fixing cyanobacteria appear to
lack a homolog of the gene. Unlike glnA (encoding the conventional GS) glnT
is induced by removal of nitrate from the medium. Although this finding may
provide a clue as to the function of the second GS, the question remains: Why
have two GS proteins?
Several other examples of redundancy were presented. Lou Sherman (Purdue
University) demonstrated the presence of a gene (isiA) encoding an
alternative to the PS II protein CP43. The gene is induced under iron
limitation and expresses a protein with a shorter hydrophilic loop relative
to CP43. Golden (S) described the regulation of the three copies of psbA in
Synechococcus PCC 7942 under different light intensities and qualities. Georg
Schmetterer (Universitaet Wien) provided evidence for an alternative oxidase
pathway in Synechocystis PCC 6803. Terry Thiel (University of Missouri, St.
Louis) offered one of the best examples of "redundancy" in showing that
Anabaena variabilis ATCC 29413 has not only the canonical nif cluster of
nitrogen fixation genes, but also a set, nif2, for molybdenum-dependent
nitrogen fixation under anaerobic conditions, and a set, vnf, for
vanadium-dependent nitrogen fixation when molybdenum is not available. The
presentation of Martin Mulligan (Memorial University of Newfoundland) on the
recently discovered RNA binding proteins suggests that they are also found
in multiple copies.
Bianca Brahamsha (Scripps Institution of Oceanography) and Laurie Caslake
(Pennsylvania State University) presented evidence showing that Anabaena
PCC 7120 and Synechococcus PCC 7002 both have multiple RNA polymerase sigma
factors in addition to the housekeeping sigma factor, SigA. The known
alternative sigma factors of PCC 7120 (SigB and SigC) are induced under
nitrogen stress, and removal of nitrogen also appears to differentially
regulate the genes for alternative sigma factors from PCC 7002.
Aside from the obvious case of a vanadium-nitrogenase and some suggestions
of the importance of relative protein stability, we really don't know much
about the selective advantage of having these protein families. Perhaps
redundancy itself is of value or perhaps more of the reasons for these
duplicated functions will be presented at the next Cyanobacterial workshop.
(Contributed by Brian Palenik)
Protein Phosphorylation (and other matters)
Several presentations included evidence for the role of two component
sensory systems and protein phosphorylation in modulating the metabolism of
cells in response to a range of environmental transients.
Shivanthi Anandan (Texas A&M University) described a cloning strategy that
was aimed at isolating genes involved in a signal transduction pathway that
might regulate light responsive gene expression in Synechococcus sp.
PCC 7942. Regions conserved amongst response regulator sequences were used
to pull out two genes, which exhibited limited similarity to the bacterial
response regulators OmpR and PhoB. Experiments with a mutant carrying an
inactivated form of one of these genes suggested that it might be involved
in the sensing of low- to high-light transitions. David Laudenbach
(University of Western Ontario) reported, as part of a talk on the
acclimation of Synechococcus sp. PCC 7942 to sulfur stress, that genes
encoding a two component sensory system resided on the large 50-kb endogenous
plasmid. [Bianca Brahamsha, below, discusses N.M.'s own presentation, which
is certainly pertinent to the discussion here -- ed.]
Sergey Shestakov (Moscow State University) described the characterization
of a herbicide (difunon) resistance gene from Synechocystis sp. PCC 6803,
which on sequence analysis turned out to be homologous to the phoR (histidine
protein kinase) gene of Bacillus subtilis. Michael Schaefer (University of
Missouri, Kansas City) related how a genomic fragment from Fremyella
diplosiphon encodes two histidine protein kinase genes as well as a
eukaryotic-type serine/threonine kinase. This genomic fragment complemented
a mutant of the blue mutant class that is defective in chromatic adaptation.
In keeping with this theme of protein phosphorylation, Martin Hagemann
(Universitaet Rostock) has found that this form of covalent modification
occurs during the response of Synechocystis sp. PCC 6803 to salt stress.
Not in keeping with this theme, but a very interesting talk nonetheless,
Georg Schmetterer (Universitaet Wien) presented evidence for a branched
pathway of terminal respiratory electron transport. Having cloned and
sequenced the genes coxABC coding for the three subunits of cytochrome c
oxidase from Synechocystis sp. PCC 6803, a mutant carrying an interrupted
coxA gene was constructed. No trace of cytochrome c oxidase activity could
be detected in either thylakoid or cytoplasmic membranes from the mutant, but
when O2 uptake was measured in the dark, the mutant was found to respire
almost normally, suggesting that Synechocystis sp PCC 6803 contains one or
more additional respiratory terminal oxidases that are cyanide-sensitive. An
interesting phenotype of the mutant is that it cannot grow chemohetero-
trophically, even with the brief pulses of light that permits such growth in
the wild-type strain.
(Contributed by Nick Mann)
Miscellaneous Topics
Carl Johnson (University of Tennessee) reported on work he and several
colleagues have done on circadian rhythms in Synechococcus PCC 7942. Using
lux fusions to the psbAI promoter, they monitored bioluminescence following
entrainment of the culture to light and dark cycles and found that expression
of the psbAI-lux fusion exhibited the criteria of circadian rhythms, namely,
persistence in constant conditions, phase resetting by light/dark signals,
and temperature compensation of the period. Furthermore, he described an
amazing apparatus that is capable of monitoring the bioluminescence of
isolated colonies on plates. Using this device to screen mutagenized
colonies, they have isolated three mutants: one that is completely
arrhythmic, a long period mutant, and a short period mutant. Once again,
prokaryotes provide a genetically manipulatable system to model a behavior
more associated with eukaryotes, and we look forward to future developments
in the molecular and genetic characterization of the clock.
For those of you who have marvelled at how a dried-out colony of Anabaena
PCC 7120 forgotten on an old dried out BG11 plate comes back to life when
placed in liquid, Pete Lammers (New Mexico State University) may have part
of the answer. Using antibodies against a consensus peptide found in
dehydrins, a family of desiccation proteins that accumulate in plants in
response to dehydration stress, his laboratory identified a 40-kd polypeptide
in Anabaena PCC 7120. This 40-kd polypeptide, which they call cyanodehydrin,
is induced by osmotic stress (sucrose, sorbitol, PEG). They have also found
putative cyanodehydrins in two other filamentous cyanobacteria: Calothrix
PCC 7601 and Nostoc PCC 7911. Although plant dehydrins accumulate in response
to dehydration caused by a variety of stresses, their function has not been
determined. It will now be possible to address such functional questions in
the genetically manipulatable Anabaena PCC 7120.
Marine group A Synechococcus were represented in two posters and a talk.
These phycoerythrin-containing unicellular cyanobacteria are abundant in the
oligotrophic open ocean and are thought to be responsible for 5 to 25% of
primary production. Their adaptive responses to nutrient limitation and other
stresses are of interest. John Rueter and others at Portland State University
are studying the interrelationship of iron-, light-, and nitrogen-limitation
in Synechococcus WH7803 grown in continuous culture. Nicholas Mann
(University of Warwick) described the response of Synechococcus WH7803 to
phosphate limitation. He and coworkers have isolated a gene, pstS, which is
induced by phosphate limitation. Its product is localized to the cell
envelope, and it shows 35% identity to the inducible periplasmic phosphate
binding protein of E. coli. The have also cloned from WH7803 genes encoding
homologs to proteins, PhoR and PhoB, that regulate the response of E. coli
to phosphate deprivation by means of a two component sensory system.
Brian Palenik described the use of RNA polymerase sequence data (that
derived from a conserved portion of the cyanobacterial rpoC1 gene) to study
the evolution and ecology of marine Synechococcus and Prochlorococcus sp. He
also urged anyone interested in the evolution of cyanobacteria to include
Gloeobacter in her/his analyses, as members of the genus appear by both RNA
polymerase and 16S rRNA sequence data to be representatives of the oldest
known cyanobacterial lineage.
(Contributed by Bianca Brahamsha)
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Laurinavichene TV, Yakunin AF, Gogotov IN (1992). Nitrogenase Activity and
Growth of Nitrogen-Fixing Symbiotic Association of Azolla Caroliniana with
a Shortage of Certain Elements in the Medium. Microbiology-Engl Tr
61(5):597-601.
Samal KC, Kannaiyan S (1992). Isolation of the Algal Symbiont Anabaena
azollae and the Role of Vitamins in Growth, Heterocyst Development and
Nitrogen-Fixing Activity. Folia Microbiol Prague 37(6):421-426.
Zimmerman WJ, Rosen BH (1992). Cyanobiont Diversity Within and Among Cycads
of One Field Site. Can J Microbiol 38(12):1324-1328.
TOXINS and NATURAL SUBSTANCES
Abdelrahman S, Elayouty YM, Kamael HA (1993). Characterization of
Heptapeptide Toxins Extracted from Microcystis aeruginosa (Egyptian
Isolate) - Comparison with Some Synthesized Analogs. Int J Pept Protein
Res 41(1):1-7.
Feuillade J (1992). Les toxines des cyanobacteries: revue de synthese
[French]. Rev Sc Eau 5:489-508.
Lukac M, Aegerter R (1993). Influence of Trace Metals on Growth and Toxin
Production of Microcystis aeruginosa. Toxicon 31(3):293-305.
Luu HA, Chen DZX, Magoon J, Worms J, Smith J, Holmes CFB (1993).
Quantification of Diarrhetic Shellfish Toxins and Identification of Novel
Protein Phosphatase Inhibitors in Marine Phytoplankton and Mussels.
Toxicon 31(1):75-83.
Namikoshi M, Carmichael WW, Sakai R, Jareserijman EA, Kaup AM, Rinehart KL
(1993). 9-Deazaadenosine and Its 5'-alpha-D-Glucopyranoside Isolated from
the Cyanobacterium Anabaena Affinis Strain VS-1. J Am Chem Soc
115(6):2504-2505.
Namikoshi M, Choi BW, Sun FR, Rinehart KL, Evans WR, Carmichael WW (1993).
Chemical Characterization and Toxicity of Dihydro Derivatives of Nodularin
and Microcystin-LR, Potent Cyanobacterial Cyclic Peptide Hepatotoxins.
Chem Res Toxicol 6(2):151-158.
Okino T, Matsuda H, Murakami M, Yamaguchi K (1993). Microginin, an
Angiotensin-Converting Enzyme Inhibitor from the Blue-Green Alga
Microcystis aeruginosa. Tetrahedron Lett 15;34(3):501-504.
Poon GK, Griggs LJ, Edwards C, Beattie KA, Codd GA (1993). Liquid
Chromatography-Electrospray Ionization Mass Spectrometry of Cyanobacterial
Toxins. J Chromatogr 628(2):215-233.
Semmelhack MF, Rhee H (1993). Formal Synthesis of Teleocidin-A via
Indole-Cr(CO)3 Complexes. Tetrahedron Lett 34(9):1399-1402.
Singh V, Goyle MR, Srivastava A, Mishra L (1992). New Bistriazole Derivatives
and the Biological Activity of the Thermophilic Cyanobacterium
Mastigocladus laminosus Cohn. Biosci Biotechnol Biochem 56(12):2052-2053.
Unson MD, Faulkner DJ (1993). Cyanobacterial Symbiont Biosynthesis of
Chlorinated Metabolites from Dysidea Herbacea (Porifera). Experientia
49(4):349-353.
Williams DE, Burgoyne DL, Rettig SJ, Andersen RJ, Fathiafshar ZR, Allen TM
(1993). The Isolation of Majusculamide-C from the Sponge Ptilocaulis
trachys Collected in Enewetak and Determination of the Absolute
Configuration of the 2-Methyl-3-Aminopentanoic Acid Residue. J Nat
Prod-Lloydia 56(4):545-551.
Yang XM, Shimizu YZ, Steiner JR, Clardy J (1993). Nostoclide I and II,
Extracellular Metabolites from a Symbiotic Cyanobacterium, Nostoc sp, from
the Lichen Peltigera Canina. Tetrahedron Lett 34(5):761-764.
TOXINS and NATURAL SUBSTANCES (Physiological Effects)
Bagchi SN, Chauhan VS, Marwah JB (1993). Effect of an Antibiotic from
Oscillatoria late-virens on Growth, Photosynthesis, and Toxicity of
Microcystis aeruginosa. Curr Microbiol 26(4):223-228.
Claeyssens S, Chedeville A, Lavoinne A (1993). Inhibition of Protein
Phosphatases Activates Glucose-6-Phosphatase in Isolated Rat Hepatocytes.
FEBS Lett 315(1):7-10.
Conradt B, Shaw J, Vida T, Emr S, Wickner W (1992). Invitro Reactions of
Vacuole Inheritance in Saccharomyces Cerevisiae [effect of microcystin-
LR]. J Cell Biol 119(6):1469-1479.
Elder GH, Hunter PR, Codd GA (1993). Hazardous Freshwater Cyanobacteria
(Blue-Green Algae). Lancet 341(8859):1519-1520.
Elsaadi O, Cameron AS (1993). Illness Associated with Blue-Green Algae. Med
J Aust 158(11):792-793.
Katsuyama H, Morgan KG (1993). Mechanisms of Ca2+-Independent Contraction in
Single Permeabilized Ferret Aorta Cells [effect of microcystin-LR]. Circ
Res 72(3):651-657.
Kiviranta J (1992). Larvicidal effects of toxic cyanobacteria on yellow fever
Mosquito, Aedes aegypti. Acta Pharm Fenn 101:105-109.
Kozikowski AP, Ma D, Pang YP, Shum P, Likic V, Mishra PK, Macura S, Basu A,
Lazo JS, Ball RG(1993). Synthesis, Molecular Modeling, 2-D NMR, and
Biological Evaluation of ILV Mimics as Potential Modulators of Protein
Kinase C. J Am Chem Soc 115(10):3957-3965.
Lau AF, Siedlecki J, Anleitner J, Patterson GML, Caplan FR, Moore RE (1993).
Inhibition of Reverse Transcriptase Activity by Extracts of Cultured
Blue-Green Algae (Cyanophyta). Planta Med 59(2):148-151.
Mellgren G, Vintermyr OK, Boe R, Doskeland SO (1993). Hepatocyte DNA
Replication Is Abolished by Inhibitors Selecting Protein Phosphatase-2A
Rather Than Phosphatase-1. Exp Cell Res 205(2):293-301.
Ohta T, Nishiwaki R, Yatsunami J, Komori A, Suganuma M, Fujiki H (1992).
Hyperphosphorylation of Cytokeratins 8 and 18 by Microcystin-LR, a New
Liver Tumor Promoter, in Primary Cultured Rat Hepatocytes. Carcinogenesis
13(12):2443-2447.
Thompson WL, Pace JG (1992). Substances That Protect Cultured Hepatocytes
from the Toxic Effects of Microcystin-LR. Toxicol In Vitro 6(6):579.
Vintermyr OK, Gjertsen BT, Lanotte M, Doskeland SO (1993). Microinjected
Catalytic Subunit of cAMP-Dependent Protein Kinase Induces Apoptosis in
Myeloid Leukemia (IPC-81) Cells. Exp Cell Res 206(1):157-161.
PHYSIOLOGY and METABOLISM
Aiba H, Nagaya M, Mizuno T (1993). Sensor and Regulator Proteins from the
Cyanobacterium Synechococcus Species PCC 7942 That Belong to the Bacterial
Signal-Transduction Protein Families - Implication in the Adaptive
Response to Phosphate Limitation. Mol Microbiol 8(1):81-91.
Bonting CFC, Kortstee GJJ, Boekestein A, Zehnder AJB (1993). The Elemental
Composition Dynamics of Large Polyphosphate Granules in Acinetobacter
Strain 210A. Arch Microbiol 159(5):428-434.
Hippesanwald S (1993). Impact of Freeze Substitution on Biological Electron
Microscopy. Microsc Res Technique 24(5):400-422.
Kohn C, Schumann J (1993). Nucleotide Sequence and Homology Comparison of two
Genes of the Sulfate Transport Operon from the Cyanobacterium
Synechocystis Sp PCC 6803. Plant Mol Biol 21(2):409-412.
Ohmori K, Hirose M, Ohmori M (1993). An Increase in the Intracellular
Concentration of cAMP Triggers Formation of an Algal Mat by the
Cyanobacterium Spirulina platensis. Plant Cell Physiol 34(1):169-171.
Potts M, Sun H, Mockaitis K, Kennelly PJ, Reed D, Tonks NK (1993). A
Protein-Tyrosine/Serine Phosphatase Encoded by the Genome of the
Cyanobacterium Nostoc commune UTEX 584. J Biol Chem 268(11):7632-7635.
Thomsen JK, Cox RP (1993). Upper Temperature Limits for Growth and
Diazotrophy in the Thermophilic Cyanobacterium HTF Chlorogloeopsis. Arch
Microbiol 159(5):423-427.
LIPIDS and TEMPERATURE TOLERANCE
Los D, Horvath I, Vigh L, Murata N (1993). The Temperature-Dependent
Expression of the Desaturase Gene desA in Synechocystis PCC 6803. FEBS
Lett 318(1):57-60.
Merrano A (1992). Purification, Characterization and Function of
Dihydrolipoamide Dehydrogenase from the Cyanobacterium Anabaena Sp Strain
PCC 7119. Biochem J DEC 15;288( Part 3):823-830.
Nishiyama Y, Kovacs E, Lee CB, Hayashi H, Watanabe T, Murata N (1993).
Photosynthetic Adaptation to High Temperature Associated with Thylakoid
Membranes of Synechococcus PCC 7002. Plant Cell Physiol 34(2):337-343.
Quoc KP, Dubacq JP, Justin AM, Demandre C, Mazliak P (1993). Biosynthesis of
Eukaryotic Lipid Molecular Species by the Cyanobacterium Spirulina
platensis. Biochim Biophys Acta 1168(1):94-99.
Reddy AS, Nuccio ML, Gross LM, Thomas TL (1993). Isolation of a
Delta-6-Desaturase Gene from the Cyanobacterium Synechocystis Sp Strain
PCC 6803 by Gain-of-Function Expression in Anabaena Sp Strain PCC 7120.
Plant Mol Biol 22(2):293-300.
Ritter D, Yopp JH (1993). Plasma Membrane Lipid Composition of the Halophilic
Cyanobacterium Aphanothece halophytica. Arch Microbiol 159(5):435-439.
Stern N, Tietz A (1993). Octadecatetraenoate Synthesis in the Unicellular
Alga Isochrysis galbana - Studies with Intact and Broken Chloroplasts.
Biochim Biophys Acta 1167(3):248-256.
Torok Z, Szalontai B, Joo F, Wistrom CA, Vigh L (1993). Homogeneous Catalytic
Deuteration of Fatty Acyl Chains as a Tool to Detect Lipid Phase
Transitions in Specific Membrane Domains - A Fourier Transform Infrared
Spectroscopic Study. Biochem Biophys Res Commun 192(2):518-524.
Wada H, Schmidt H, Heinz E, Murata N (1993). Invitro Ferredoxin-Dependent
Desaturation of Fatty Acids in Cyanobacterial Thylakoid Membranes. J
Bacteriol 175(2):544-547.
SALINITY, HEAVY METALS, and STRESS RESPONSES
Broun II, Gorbik GP, Mirochnik OY (1992). Light-Induced Na+-Dependent H+
Uptake by the Cyanobacterium Synechocystis PCC 6803 - Detection of a
Mutant Strain Lacking Na+-Dependent Resistance to Protonophores.
Biochemistry-Engl Tr 57(10):1100-1103.
Fernandes TA, Iyer V, Apte K (1993). Differential Responses of
Nitrogen-Fixing Cyanobacteria to Salinity and Osmotic Stresses. Appl
Environ Microbiol 59(3):899-904.
Lippert K, Galinski EA, Truper HG (1993). Biosynthesis and Function of
Trehalose in Ectothiorhodospira Halochloris. Anton Leeuwenhoek Int J Gen
M 63(1):85-91.
Mamedov M, Hayashi H, Murata N (1993). Effects of Glycinebetaine and
Unsaturation of Membrane Lipids on Heat Stability of Photosynthetic
Electron Transport and Phosphorylation Reactions in Synechocystis
PCC 6803. Biochim Biophys Acta 1142(1-2):1-5.
Valiente EF, Avendano MD (1993). Sodium-Stimulation of Phosphate Uptake in
the Cyanobacterium Anabaena PCC 7119. Plant Cell Physiol 34(2):201-207.
Bhunia AK, Roy D, Banerjee SK (1993). Carbaryl-Induced Effects on Glutathione
Content, Glutathione Reductase and Superoxide Dismutase Activity of the
Cyanobacterium Nostoc muscorum. Lett Appl Microbiol 16(1):10-13.
Chang C, Sibley TH (1993). Accumulation and Transfer of Copper by Oocystis
pusilla. Bull Environ Contam Toxicol 50(5):689-695.
Demarsac NT, Houmard J (1993). Adaptation of Cyanobacteria to Environmental
Stimuli - New Steps Towards Molecular Mechanisms. FEMS Microbiol Rev
104(1-2):119-189.
Dubinin AV, Zastrizhnaya OM, Gusev MV (1992). Hydrogen Peroxide Production
by the Halophilic Cyanobacterium Microcoleus Chthonoplastes.
Microbiology-Engl Tr 61(3):261-266.
Garnham GW, Codd GA, Gadd GM (1993). Uptake of cobalt and cesium by
microalgal- and cyanobacterial-clay mixtures. Microb Ecol 25:71-82.
Gupta A, Morby AP, Turner JS, Whitton BA, Robinson NJ (1993). Deletion Within
the Metallothionein Locus of Cadmium-Tolerant Synechococcus PCC 6301
Involving a Highly Iterated Palindrome (HIP1). Mol Microbiol 7(2):189-195.
Huckle JW, Morby AP, Turner JS, Robinson NJ (1993). Isolation of a
Prokaryotic Metallothionein Locus and Analysis of Transcriptional Control
by Trace Metal Ions. Mol Microbiol 7(2):177-187.
Ivanov AY, Fomchenkov VM, Khasanova LA, Kuramshina ZM, Sadikov MM (1992).
Effect of Heavy Metal Ions on the Electrophysical Properties of Anacystis
nidulans and Escherichia coli. Microbiology-Engl Tr 61(3):319-326.
Kozitskaya VN, Komarenko EI, Chernyshova NA (1992). Structural and Functional
Peculiarities of Cyanobacterium Microcystis aeruginosa Depending on the
Effect of the Water Medium's Active Reaction. Microbiology-Engl Tr
61(2):151-155.
Lee LH, Lustigman B, Maccari J (1993). Effect of Copper on the Growth of
Anacystis nidulans. Bull Environ Contam Toxicol 50(4):600-607.
Lehel C, Gombos Z, Torok Z, Vigh L (1993). Growth Temperature Modulates
Thermotolerance and Heat Shock Response of
Cyanobacterium Synechocystis PCC 6803. Plant Physiol Biochem 31(1):81-88.
Michel KP, Pistorius EK (1992). Isolation of a Photosystem-II Associated
36-kDa Polypeptide and an Iron-Stress 34-kDa Polypeptide from Thylakoid
Membranes of the Cyanobacterium Synechococcus PCC 6301 Grown Under Mild
Iron Deficiency. Z Naturforsch C 47(11-12):867-874.
Morby AP, Turner JS, Huckle JW, Robinson NJ (1993). SmtB Is a Metal-Dependent
Repressor of the Cyanobacterial Metallothionein Gene smtA - Identification
of a Zn Inhibited DNA-Protein Complex. Nucleic Acids Res 21(4):921-925.
Murthy SDS, Mohanty P (1993). Time-Dependent Alterations in the Antenna
Pigment Protein Complex by Mercury Ions in the Cyanobacterium Spirulina
platensis. Biometals SPR;6(1):45-48.
Pandey PK, Singh SP (1993). Hg2+ Uptake in a Cyanobacterium. Curr Microbiol
26(3):155-159.
Rachlin JW, Grosso A (1993). The Growth Response of the Green Alga Chlorella
vulgaris to Combined Divalent Cation Exposure. Arch Environ Contam Toxicol
24(1):16-20.
Shuttleworth KL, Unz RF (1993). Sorption of Heavy Metals to the Filamentous
Bacterium Thiothrix strain A1. Appl Environ Microbiol 59(5):1274-1282.
Singh AL, Asthana RK, Srivastava SC, Singh SP (1992). Nickel Uptake and Its
Localization in a Cyanobacterium. FEMS Microbiol Lett 1;99(2-3):165-168.
Verma SK, Singh RK, Singh SP (1993). Copper Toxicity and Phosphate
Utilization in the Cyanobacterium Nostoc calcicola. Bull Environ Contam
Toxicol 50(2):192-198.
NITROGEN METABOLISM and NITROGEN FIXATION
Coronil T, Lara C, Guerrero MG (1993). Shift in Carbon Flow and Stimulation
of Amino Acid Turnover Induced by Nitrate and Ammonium Assimilation in
Anacystis nidulans. Planta 189(3):461-467.
Elmorjani K, Liotenberg S, Houmard J, Demarsac NT (1992). Molecular
Characterization of the Gene Encoding Glutamine Synthetase in the
Cyanobacterium Calothrix Sp PCC 7601. Biochem Biophys Res Commun DEC
30;189(3):1296-1302.
Jansson E, Martel A, Lindblad P (1993). Ornithine Cycle in Nostoc PCC 73102
- Stimulation of In vitro Ornithine Carbamoyl Transferase Activity by
Addition of Arginine. Curr Microbiol 26(2):75-78.
Luque I, Flores E, Herrero A (1993). Nitrite Reductase Gene from
Synechococcus Sp PCC 7942 - Homology Between Cyanobacterial and
Higher-Plant Nitrite Reductases. Plant Mol Biol 21(6):1201-1205.
Marco E, Orus MI (1993). Trichlorfon-Induced Inhibition of Nitrate and
Ammonium Uptake in Cyanobacteria. J Exp Bot 44(259):501-508.
Martel A, Jansson E, Garciareina G, Lindblad P (1993). Ornithine Cycle in
Nostoc PCC 73102 - Arginase, OCT and Arginine Deiminase, and the Effects
of Addition of External Arginine, Ornithine, or Citrulline. Arch Microbiol
159(6):506-511.
Murphy ST, Jackman DM, Mulligan ME (1993). Cloning and Nucleotide Sequence
of the Gene for Dinitrogenase Reductase (nifH) from the Heterocyst-Forming
Cyanobacterium Anabaena Sp L31. Biochim Biophys Acta 1171(3):337-340.
Ohki K, Zehr JP, Fujita Y (1992). Regulation of Nitrogenase Activity in
Relation to the Light-Dark Regime in the Filamentous Non-Heterocystous
Cyanobacterium Trichodesmium Sp NIBB 1067. J Gen Microbiol 138( Part
12):2679-2685.
Omata T, Andriesse X, Hirano A (1993). Identification and Characterization
of a Gene Cluster Involved in Nitrate Transport in the Cyanobacterium
Synechococcus sp. PCC 7942. Mol Gen Genet 236(2-3):193-202.
Prufert-Bebout L, Paerl HW, Lassen C (1993). Growth, Nitrogen Fixation, and
Spectral Attenuation in Cultivated Trichodesmium Species. Appl Environ
Microbiol 59(5):1367-1375.
Singh S (1993). Role of Glutamine Synthetase, Glutamine and NH4+ in the
Regulation of Glutamine Uptake in the Cyanobacterium Anabaena cycadeae.
J Gen Appl Microbiol Tokyo 39(1):57-64.
Singh S (1993). Regulation of Glutamate Metabolism in the Cyanobiont Nostoc
anth by Nitrogen Sources. J Basic Microbiol 33(1):41-45.
Singh S (1993). Role of Glutamine Synthetase Activity in the Uptake and
Metabolism of Arginine and Proline in the Cyanobacterium Anabaena
cycadeae. FEMS Microbiol Lett 106(3):335-340.
Singh S, Chakravarty D, Singh HN (1993). Mutational Replacement of Molybdenum
by Vanadium in Assimilation of N2 or NO3- as Nitrogen Source in the
Cyanobacterium Nostoc muscorum. Biochem Mol Biol Int 29(6):1083-1093.
Smith PT, King AD, Goodman N (1993). Isolation and Characterization of Urease
from Aspergillus niger. J Gen Microbiol 139( Part 5):957-962.
Srivastava R, Amla DV (1993). Physiological and Biochemical Analysis of the
Glutamine Synthetase-Impaired Mutants of the Nitrogen-Fixing
Cyanobacterium Nostoc muscorum. Curr Microbiol 26(4):205-215.
Thomas SP, Shanmugasundaram S (1992). Amino Acid Overproduction by Analog
Resistant Mutants of the Nitrogen Fixing Cyanobacterium Anabaena sp 287.
Appl Biochem Biotechnol 37(2):111-121.
Wagner SJ, Thomas SP, Kaufman RI, Nixon BT, Stevens SE (1993). The glnA Gene
of the Cyanobacterium Agmenellum quadruplicatum PR-6 Is Nonessential for
Ammonium Assimilation. J Bacteriol 175(3):604-612.
Bebout BM, Fitzpatrick MW, Paerl HW (1993). Identification of the Sources of
Energy for Nitrogen Fixation and Physiological Characterization of
Nitrogen-Fixing Members of a Marine Microbial Mat Community. Appl Environ
Microbiol 59(5):1495-1503.
Reddy KJ, Haskell JB, Sherman DM, Sherman LA (1993). Unicellular, Aerobic
Nitrogen-Fixing Cyanobacteria of the Genus Cyanothece. J Bacteriol
175(5):1284-1292.
Yakunin AF, Troshina OY, Jha M, Gogotov IN (1992). Effect of Ammonium on
Nitrogenase Activity in the Heterocystous Cyanobacterium Anabaena
variabilis. Microbiology-Engl Tr 61(3):256-260.
Zehr JP, Wyman M, Miller V, Duguay L, Capone DG (1993). Modification of the
Fe Proteinthi of Nitrogenase in Natural Populations of Trichodesmium
thiebautii. Appl Environ Microbiol 59(3):669-676.
DIFFERENTIATION and HYDROGENASE
Black TA, Cai Y, Wolk CP (1993). Spatial expression and autoregulation of
hetR, a gene involved in the control of heterocyst development in
Anabaena. Molec Microbiol 9:77-84.
Buikema WJ, Haselkorn R (1993). Molecular Genetics of Cyanobacterial
Development. Annu Rev Plant Physiol 4433-52.
Campbell D, Houmard J, Tandeau de Marsac N (1993). Electron Transport
Regulates Cellular Differentiation in the Filamentous Cyanobacterium
Calothrix. Plant Cell 5(4):451-463.
Haselkorn R (1992). Developmentally Regulated Gene Rearrangements in
Prokaryotes. Annu Rev Genet 26113-130.
Kaiser D, Losick R (1993). How and Why Bacteria Talk to Each Other. Cell
73(5):873-885.
Kangatharalingam N, Priscu JC, Paerl HW (1992). Heterocyst Envelope
Thickness, Heterocyst Frequency and Nitrogenase Activity in Anabaena flos
aquae - Influence of Exogenous Oxygen Tension. J Gen Microbiol
138:2673-2678.
Liang JH, Scappino L, Haselkorn R (1993). The patB Gene Product, Required for
Growth of the Cyanobacterium Anabaena Sp Strain PCC 7120 Under
Nitrogen-Limiting Conditions, Contains Ferredoxin and Helix-Turn-Helix
Domains. J Bacteriol 175(6):1697-1704.
Soriente A, Gambacorta A, Trincone A, Sili C, Vincenzini M, Sodano G (1993).
Heterocyst Glycolipids of the Cyanobacterium Cyanospira rippkae.
Phytochemistry 33(2):393-396.
Wolk CP, Elhai J, Kuritz T, Holland D (1993). Amplified Expression of a
Transcriptional Pattern Formed During Development of Anabaena. Mol
Microbiol 7(3):441-445.
Sarkar S, Pandey KD, Kashyap AK (1992). Simultaneous Photoproduction of
Hydrogen and Ammonia by a Non-Heterocystous Cyanobacterium Plectonema
boryanum. J Gen Appl Microbiol Tokyo 38(5):407-415.
Serebryakova LT, Zorin NA, Gogotov IN (1992). Hydrogenase Activity of
Filamentous Cyanobacteria. Microbiology-Engl Tr 61(2):107-112.
CARBON METABOLISM
De Philippis R, Ena A, Guastini M, Sili C, Vincenzini M (1992). Factors
Affecting Poly-beta-Hydroxybutyrate Accumulation in Cyanobacteria and in
Purple Non-Sulfur Bacteria. FEMS Microbiol Rev 103(2-4):187-194.
Grotjohann N, Schneider G, Kowallik W (1993). Different Forms of Fructose
1,6-Bisphosphatase in Chlorella. Z Naturforsch C 48(1-2):22-27.
Guy RD, Fogel ML, Berry JA (1993). Photosynthetic Fractionation of the Stable
Isotopes of Oxygen and Carbon. Plant Physiol 101(1):37-47.
Larimer FW, Soper TS (1993). Overproduction of Anabaena 7120
Ribulose-Bisphosphate Carboxylase/Oxygenase in Escherichia coli. Gene
126(1):85-92.
Lee GJ, McDonald KA, McFadden BA (1993). Leucine 332 influences the CO2/O2
specificity factor of ribulose-1,5-bisphosphate carboxylase/oxygenase from
Anacystis nidulans. Prot Sci 2:1147-1154.
Li LA, Gibson JL, Tabita FR (1993). The Rubisco Activase (rca) Gene Is
Located Downstream from rbcS in Anabaena Sp Strain CA and Is Detected in
Other Anabaena Nostoc Strains. Plant Mol Biol 21(5):753-764.
Luinenburg I, Coleman JR (1993). Expression of Escherichia coli
Phosphoenolpyruvate Carboxylase in a Cyanobacterium - Functional
Complementation of Synechococcus PCC 7942 ppc. Plant Physiol
101(1):121-126.
Marco E, Ohad N, Schwarz R, Liemanhurwitz J, Gabay C, Kaplan A (1993). High
CO2 Concentration Alleviates the Block in Photosynthetic Electron
Transport in an ndhB-Inactivated Mutant of Synechococcus Sp PCC 7942.
Plant Physiol 101(3):1047-1053.
Price GD, Howitt SM, Harrison K, Badger MR (1993). Analysis of a Genomic DNA
Region from the Cyanobacterium Synechococcus Sp Strain PCC 7942 Involved
in Carboxysome Assembly and Function. J Bacteriol 175(10):2871-2879.
Read BA, Tabita FR (1992). Amino acid substitutions in the small subunit of
ribulose-1,5-bisphosphate carboxylase/oxygenase that influence catalytic
activity of the holoenzyme. Biochem 31:519-525.
Read BA, Tabita FR (1992). A hybrid ribulosebisphosphate
carboxylase/oxygenase enzyme exhibiting a substantial increase in
substrate specificity factor. Biochem 31:5553-5560.
Schwarz R, Liemanhurwitz J, Hassidim M, Kaplan A (1992). Phenotypic
Complementation of High CO2-Requiring Mutants of the Cyanobacterium
Synechococcus Sp Strain PCC 7942 by Inosine 5'-Monophosphate. Plant
Physiol 100(4):1987-1993.
Stal LJ (1992). Poly(hydroxyalkanoate) in Cyanobacteria - An Overview. FEMS
Microbiol Rev 103(2-4):169-180.
PHOTOSYNTHESIS
Bader KP, Schmid GH, Ruyters G, Kowallik W (1992). Blue Light Enhanced
Respiratory Activity Under Photosynthetic Conditions in Chlorella - A Mass
Spectrometric Analysis. Z Naturforsch C 47(11-12):881-888.
Foguel D, Chaloub RM, Silva JL, Crofts AR, Weber G (1992). Pressure and Low
Temperature Effects on the Fluorescence Emission Spectra and Lifetimes of
the Photosynthetic Components of Cyanobacteria. Biophys J 63(6):1613-1622.
Greer DH, Laing WA, Woolley DJ (1993). The Effect of Chloramphenicol on
Photoinhibition of Photosynthesis and Its Recovery in Intact Kiwifruit
(Actinidia deliciosa) Leaves. Aust J Plant Physiol 20(1):33-43.
Kim JH, Glick RE, Melis A (1993). Dynamics of Photosystem Stoichiometry
Adjustment by Light Quality in Chloroplasts. Plant Physiol 102(1):181-190.
Kondo T, Strayer CA, Kulkarni RD, Taylor W, Ishiura M, Golden SS, Johnson CH
(1993). Circadian rhythms in prokaryotes: luciferase as a reporter of
circadian gene expression in cyanobacteria. Proc Natl Acad Sci USA.
Lapointe L, Huner NPA, Leblanc RM, Carpentier R (1993). Possible
Photoacoustic Detection of Cyclic Electron Transport Around Photosystem II
in Photoinhibited Thylakoid Preparations. Biochim Biophys Acta
1142(1-2):43-48.
Mi HL, Endo T, Schreiber U, Asada K (1992). Donation of Electrons from
Cytosolic Components to the Intersystem Chain in the Cyanobacterium
Synechococcus Sp PCC 7002 as Determined by the Reduction of P700+. Plant
Cell Physiol 33(8):1099-1105.
Mi HL, Endo T, Schreiber U, Ogawa T, Asada K (1992). Electron Donation from
Cyclic and Respiratory Flows to the Photosynthetic Intersystem Chain Is
Mediated by Pyridine Nucleotide Dehydrogenase in the Cyanobacterium
Synechocystis PCC 6803. Plant Cell Physiol 33(8):1233-1237.
Rudiger W (1992). Events in the Phytochrome Molecule After Irradiation.
Photochem Photobiol 56(5):803-809.
PHOTOSYSTEM I
Bouyoub A, Vernotte C, Astier C (1993). Functional Analysis of the two
Homologous psbA Gene Copies in Synechocystis PCC 6714 and PCC 6803. Plant
Mol Biol 21(2):249-258.
Chitnis VP, Xu Q, Yu L, Golbeck JH, Nakamoto H, Xie DL, Chitnis PR (1993).
Targeted Inactivation of the Gene psaL Encoding a Subunit of Photosystem I
of the Cyanobacterium Synechocystis Sp PCC 6803. J Biol Chem
268(16):11678-11684.
Golbeck JH (1993). Shared Thematic Elements in Photochemical Reaction
Centers. Proc Natl Acad Sci USA 90(5):1642-1646.
Guigliarelli B, Guillaussier J, More C, Setif P, Bottin H, Bertrand P (1993).
Structural Organization of the Iron-Sulfur Centers in Synechocystis 6803
Photosystem I - EPR Study of Oriented Thylakoid Membranes and Analysis of
the Magnetic Interactions. J Biol Chem 268(2):900-908.
Hatanaka H, Sonoike K, Hirano M, Katoh S (1993). Small Subunits of
Photosystem I Reaction Center Complexes from Synechococcus Elongatus.
1. Is the psaF Gene Product Required for Oxidation of Cytochrome c553.
Biochim Biophys Acta 1141(1):45-51.
Ikeuchi M, Sonoike K, Koike H, Pakrasi HB, Inoue Y (1992). A Novel 3.5-kDa
Protein Component of Cyanobacterial Photosystem I Complexes. Plant Cell
Physiol 33(8):1057-1063.
Kaurov YN, Aksyonova GE, Lovyagina ER, Veselova TV, Ivanov II (1992). On the
Nature of Thermally-Induced Delayed Luminescence of Photosystem I from
Thermophilic Cyanobacterial Membranes. Biol Membrany 9(8):845-857.
Krauss N, Hinrichs W, Witt I, Fromme P, Pritzkow W, Dauter Z, Betzel C,
Wilson KS, Witt HT, Saenger W (1993). 3-Dimensional Structure of System I
of Photosynthesis at 6 Angstrom Resolution. Nature 361(6410):326-331.
Mohamed A, Eriksson J, Osiewacz HD, Jansson C (1993). Differential Expression
of the psbA Genes in the Cyanobacterium Synechocystis 6803. Mol Gen Genet
238(1-2):161-168.
Muhlenhoff U, Haehnel W, Witt H, Herrmann RG (1993). Genes Encoding 11
Subunits of Photosystem I from the Thermophilic Cyanobacterium
Synechococcus Sp. Gene 127(1):71-78.
Rhiel E, Bryant DA (1993). Nucleotide Sequence of the psaE Gene of
Cyanobacterium Synechococcus Sp PCC 6301. Plant Physiol 101(2):701-702.
Rousseau F, Setif P, Lagoutte B (1993). Evidence for the Involvement of PSI-E
Subunit in the Reduction of Ferredoxin by Photosystem I. EMBO J
12(5):1755-1765.
Smart LB, Mcintosh L (1993). Genetic Inactivation of the psaB Gene in
Synechocystis Sp PCC 6803 Disrupts Assembly of Photosystem I. Plant Mol
Biol 21(1):177-180.
Smart LB, Warren PV, Golbeck JH, Mcintosh L (1993). Mutational Analysis of
the Structure and Biogenesis of the Photosystem I Reaction Center in the
Cyanobacterium Synechocystis Sp PCC 6803. Proc Natl Acad Sci USA
90(3):1132-1136.
Sonoike K, Hatanaka H, Katoh S (1993). Small Subunits of Photosystem I
Reaction Center Complexes from Synechococcus Elongatus. 2. The psaE Gene
Product Has a Role to Promote Interaction Between the Terminal Electron
Acceptor and Ferredoxin. Biochim Biophys Acta 1141(1):52-57.
Tsiotis G, Nitschke W, Haase W, Michel H (1993). Purification and
Crystallization of Photosystem I Complex from a Phycobilisome-Less Mutant
of the Cyanobacterium Synechococcus PCC 7002. Photosynth Res
35(3):285-297.
Turconi S, Schweitzer G, Holzwarth AR (1993). Temperature Dependence of
Picosecond Fluorescence Kinetics of a Cyanobacterial Photosystem I
Particle. Photochem Photobiol 57(1):113-119.
Vanderlee J, Bald D, Kwa SLS, Vangrondelle R, Rogner M, Dekker JP (1993).
Steady-State Polarized Light Spectroscopy of Isolated Photosystem I
Complexes. Photosynth Res 35(3):311-321.
Vanderstaay GWM, Boekema EJ, Dekker JP, Matthijs HCP (1993). Characterization
of Trimeric Photosystem I Particles from the Prochlorophyte Prochlorothrix
hollandica by Electron Microscopy and Image Analysis. Biochim Biophys Acta
1142(1-2):189-193.
Zhao J, Snyder WB, Muhlenhoff U, Rhiel E, Warren PV, Golbeck JH, Bryant D
(1993). Cloning and characterization of the psaE gene of the
cyanobacterium Synechococcus sp. PCC 7002: characterization of a psaE
mutant and overproduction of the protein in Escherichia coli. Molec
Microbiol 9:183-194.
PHOTOSYSTEM II
Anbudurai PR, Pakrasi HB (1993). Mutational Analysis of the PsbL Protein of
Photosystem II in the Cyanobacterium Synechocystis Sp PCC 6803.
Z Naturforsch C 48(3-4):267-274.
Astier C, Perewoska I, Picaud M, Kirilovsky D, Vernotte C (1993). Structural
Analysis of the QB Pocket of the D1 Subunit of Photosystem II in
Synechocystis PCC 6714 and PCC 6803. Z Naturforsch C 48(3-4):199-204.
Boerner RJ, Bixby KA, Nguyen AP, Noren GH, Debus RJ, Barry BA (1993). Removal
of Stable Tyrosine Radical D+ Affects the Structure or Redox Properties
of Tyrosine-Z in Manganese-Depleted Photosystem II Particles from
Synechocystis 6803. J Biol Chem 268(3):1817-1823.
Boichenko VA, Klimov VV, Mayes SR, Barber J (1993). Characterization of the
Light-Induced Oxygen Gas Exchange from the IC2 Deletion Mutant of
Synechocystis PCC 6803 Lacking the Photosystem II 33-kDa Extrinsic
Protein. Z Naturforsch C 48(3-4):224-233.
Cao J, Ohad N, Hirschberg J, Xiong J, Govindjee (1992). Binding Affinity of
Bicarbonate and Formate in Herbicide-Resistant D1 Mutants of Synechococcus
Sp PCC 7942. Photosynth Res 34(3):397-408.
Engels DH, Engels A, Pistorius EK (1992). Isolation and Partial
Characterization of an L-Amino Acid Oxidase and of Photosystem II
Complexes from the Cyanobacterium Synechococcus PCC 7942. Z Naturforsch
C 47(11-12):859-866.
Foguel D, Chaloub RM (1993). Effects of the Alkaloid Gramine on the
Light-Harvesting, Energy Transfer, and Growth of Anabaena Sp (PCC 7119).
Plant Physiol 101(2):633-639.
Haag E, Eatonrye JJ, Renger G, Vermaas WFJ (1993). Functionally Important
Domains of the Large Hydrophilic Loop of CP47 as Probed by
Oligonucleotide-Directed Mutagenesis in Synechocystis Sp PCC 6803.
Biochemistry 32(16):4444-4454.
Kless H, Orenshamir M, Ohad I, Edelman M, Vermaas W (1993). Protein
Modifications in the D2 Protein of Photosystem II Affect Properties of the
QB/Herbicide-Binding Environment. Z Naturforsch C 48(3-4):185-190.
Lind LK, Shukla VK, Nyhus KJ, Pakrasi HB (1993). Genetic and Immunological
Analyses of the Cyanobacterium Synechocystis Sp PCC 6803 Show That the
Protein Encoded by the psbJ Gene Regulates the Number of Photosystem II
Centers in Thylakoid Membranes. J Biol Chem 268(3):1575-1579.
Lysenko ES, Ogarkova OA, Tarasov VA (1993). Localization of Cyanobacterium
Synechocystis Sp PCC 6803 Photosynthetic Genes in Chloroplast and Nuclear
Genomes of Higher Plants. Genetika 29(2):348-353.
Maenpaa P, Kallio T, Mulo P, Salih G, Aro EM, Tyystjarvi E, Jansson C (1993).
Site-Specific Mutations in the D1 Polypeptide Affect the Susceptibility
of Synechocystis 6803 Cells to Photoinhibition. Plant Mol Biol 22(1):1-12.
Mayes SR, Dubbs JM, Vass I, Hideg E, Nagy L, Barber J (1993). Further
Characterization of the psbH Locus of Synechocystis Sp PCC 6803 -
Inactivation of psbH Impairs QA to QB Electron Transport in Photosystem
2. Biochemistry 32(6):1454-1465.
Miura K, Shimazu T, Motoki A, Kanai S, Hirano M, Katoh S (1993). Nucleotide
Sequence of the Mn-Stabilizing Protein Gene of the Thermophilic
Cyanobacterium Synechococcus Elongatus. Biochim Biophys Acta
1172(3):357-360.
Mor TS, Post AF, Ohad I (1993). The Manganese Stabilising Protein (MSP) of
Prochlorothrix hollandica Is a Hydrophobic Membrane-Bound Protein. Biochim
Biophys Acta 1141(2-3):206-212.
Pistorius EK (1993). The identity of the water oxidizing enzyme in
photosystem II is still controversial. Physiol Plant 87:624-631.
Race HL, Gounaris K (1993). Identification of the PsbH Gene Product as a
6-kDa Phosphoprotein in the Cyanobacterium Synechocystis 6803. FEBS Lett
323(1-2):35-39.
Satoh K, Kashino Y, Koike H (1993). Electron Transport from QA to
Thymoquinone in a Synechococcus Oxygen-Evolving Photosystem II Preparation
- Role of QB and Binding Affinity of Thymoquinone to the QB Site. Z
Naturforsch C 48(3-4):174-178.
Shen GZ, Eatonrye JJ, Vermaas WFJ (1993). Mutation of Histidine Residues in
CP47 Leads to Destabilization of the Photosystem II Complex and to
Impairment of Light Energy Transfer. Biochemistry 32(19):5109-5115.
Shen JR, Inoue Y (1993). Binding and Functional Properties of 2 New Extrinsic
Components, Cytochrome c550 and a 12-kDa Protein, in Cyanobacterial
Photosystem II. Biochemistry 32(7):1825-1832.
Shutilova NI, Klimov VV, Antropova TM, Shnyrov VL (1992). Thermal
Inactivation of the Oxygen-Evolving Complex of the Functional Core of
Photosystem II in Chloroplasts. Biochemistry-Engl Tr 57(10):1042-1048.
Tang XS, Sivaraja M, Dismukes GC (1993). Protein and Substrate Coordination
to the Manganese Cluster in the Photosynthetic Water Oxidizing Complex -
15N and 1H ENDOR Spectroscopy of the S2 State Multiline Signal in the
Thermophilic Cyanobacterium Synechococcus. J Am Chem Soc 115(6):2382-2389.
Tommos C, Davidsson L, Svensson B, Madsen C, Vermaas W, Styring S (1993).
Modified EPR Spectra of the Tyrosine(D) Radical in Photosystem II in
Site-Directed Mutants of Synechocystis sp. PCC 6803 - Identification of
Side Chains in the Immediate Vicinity of Tyrosine(D) on the D2 Protein.
Biochemistry 32(20):5436-5441.
Vermaas W (1993). Molecular Biological Approaches to Analyze Photosystem II
Structure and Function. Annu Rev Plant Physiol 44457-481.
Waelzlein G, Pistorius EK (1991). Inactivation of photosynthetic O2 evolution
in the cyanobacterium Anacystis nidulans PCC 6301: Influence of nitrogen
metabolites and divalent cation concentration. Z Natursorsch
46c:1024-1032.
PHYCOBILISOMES
Apt KE, Grossman AR (1993). Genes Encoding Phycobilisome Linker Polypeptides
on the Plastid Genome of Aglaothamnion neglectum (Rhodophyta). Photosynth
Res 35(3):235-245.
Apt KE, Grossman AR (1993). Characterization and Transcript Analysis of the
Major Phycobiliprotein Subunit Genes from Aglaothamnion neglectum
(Rhodophyta). Plant Mol Biol 21(1):27-38.
Bhalerao RP, Lind LK, Persson CE, Gustafsson P (1993). Cloning of the
Phycobilisome Rod Linker Genes from the Cyanobacterium Synechococcus Sp
PCC 6301 and Their Inactivation in Synechococcus Sp PCC 7942. Mol Gen
Genet 237(1-2):89-96.
Capuano V, Thomas JC, Demarsac NT, Houmard J (1993). An In vivo Approach to
Define the Role of the LCM, the Key Polypeptide of Cyanobacterial
Phycobilisomes. J Biol Chem 268(11):8277-8283.
Delorimier R, Wilbanks SM, Glazer AN (1993). Genes of the R-Phycocyanin-II
Locus of Marine Synechococcus spp and Comparison of Protein-Chromophore
Interactions in Phycocyanins Differing in Bilin Composition. Plant Mol
Biol 21(2):225-237.
Demidov AA, Borisov AY (1993). Numerical Modeling of Energy Migration in
C-Phycocyanin of the Blue-Green Alga Agmenellum quadruplicatum. Biofizika
38(1):133-143.
Demidov AA, Borisov AY (1993). Computer Simulation of Energy Migration in the
C-Phycocyanin of the Blue-Green Algae Agmenellum quadruplicatum. Biophys
J 64(5):1375-1384.
Dimagno L, Haselkorn R (1993). Isolation and Characterization of the Genes
Encoding Allophycocyanin Subunits and 2 Linker Proteins from Synechocystis
6714. Plant Mol Biol 21(5):835-845.
Ficner R, Lobeck K, Schmidt G, Huber R (1992). Isolation, Crystallization,
Crystal Structure Analysis and Refinement of B-Phycoerythrin from the Red
Alga Porphyridium Sordidum at 2.2 Angstrom Resolution. J Mol Biol
228(3):935-950.
Gillbro T, Sharkov AV, Kryukov IV, Khoroshilov EV, Kryukov PG, Fischer R,
Scheer H (1993). Forster Energy Transfer Between Neighbouring Chromophores
in C-Phycocyanin Trimers. Biochim Biophys Acta 1140(3):321-326.
Glauser M, Sidler W, Zuber H (1993). Isolation, Characterization and
Reconstitution of Phycobiliprotein Rod-Core Linker Polypeptide Complexes
from the Phycobilisome of Mastigocladus laminosus. Photochem Photobiol
57(2):344-351.
Grossman AR, Schaefer MR, Chiang GG, Collier JL (1993). Environmental Effects
on the Light Harvesting Complex of Cyanobacteria. J Bacteriol
175(3):575-582.
Hucke M, Schweitzer G, Holzwarth AR, Sidler W, Zuber H (1993). Studies on
Chromophore Coupling in Isolated Phycobiliproteins. 4. Femtosecond
Transient Absorption Study of Ultrafast Excited State Dynamics in Trimeric
Phycoerythrocyanin Complexes. Photochem Photobiol 57(1):76-80.
Kalla R, Bhalerao RP, Gustafsson P (1993). Regulation of Phycobilisome Rod
Proteins and Messenger RNA at Different Light Intensities in the
Cyanobacterium Synechococcus 6301. Gene 126(1):77-83.
Reuter W, Nickelreuter C (1993). Molecular Assembly of the Phycobilisomes
from the Cyanobacterium Mastigocladus laminosus. J Photochem Photobiol
B-Biol 18(1):51-66.
Roell MK, Morse DE (1993). Organization, Expression and Nucleotide Sequence
of the Operon Encoding R-Phycoerythrin alpha-Subunit and beta-Subunit from
the Red Alga Polysiphonia Boldii. Plant Mol Biol 21(1):47-58.
Sai PSM, Siebzehnrubl S, Mahajan S, Scheer H (1993). Fluorescence and
Circular Dichroism Studies on the Phycoerythrocyanins from the
Cyanobacterium Westiellopsis Prolifica. Photochem Photobiol 57(1):71-75.
Scharnagl C, Fischer SF (1993). Reversible Photochemistry in the
alpha-Subunit of Phycoerythrocyanin - Characterization of Chromophore and
Protein by Molecular Dynamics and Quantum Chemical Calculations. Photochem
Photobiol 57(1):63-70.
Schmidtgoff CM, Federspiel NA (1993). In vivo and In vitro Footprinting of
a Light-Regulated Promoter in the Cyanobacterium Fremyella diplosiphon.
J Bacteriol 175(6):1806-1813.
Schneider S, Prenzel CJ, Brehm G, Gedeck P, Sai PSM, Gottschalk L, Scheer H
(1993). A Comparison of Phycocyanins from 3 Different Species of
Cyanobacteria Employing Resonance-Enhanced Coherent Anti-Stokes Raman
Spectroscopy. Photochem Photobiol 57(1):56-62.
Sobczyk A, Schyns G, Demarsac NT, Houmard J (1993). Transduction of the Light
Signal During Complementary Chromatic Adaptation in the Cyanobacterium
Calothrix sp PCC 7601 - DNA-Binding Proteins and Modulation by
Phosphorylation. EMBO J 12(3):997-1004.
Stadnichuk IN, Khokhlachev AV, Tikhonova YV (1993). Polypeptide
gamma-Subunits of R-Phycoerythrin. J Photochem Photobiol B-Biol
18(2-3):169-175.
Wehrmeyer W, Morschel E, Vogel K (1993). Core Substructure in Phycobilisomes
of Red Algae. 2. The Central Part of the Tricylindrical Core - AP(CM) -
A Constituent of Hemidiscoidal Phycobilisomes of Rhodella violacea. Eur
J Cell Biol 60(1):203-209.
Westermann M, Reuter W, Schimek C, Wehrmeyer W (1993). Presence of Both
Hemidiscoidal and Hemiellipsoidal Phycobilisomes in a Phormidium Species
(Cyanobacteria). Z Naturforsch C 48(1-2):28-34.
Wilbanks SM, Glazer AN (1993). Rod Structure of a Phycoerythrin II-Containing
Phycobilisome. 2. Complete Sequence and Bilin Attachment Site of a
Phycoerythrin gamma-Subunit. J Biol Chem 268(2):1236-1241.
Wilbanks SM, Glazer AN (1993). Rod Structure of a Phycoerythrin II-Containing
Phycobilisome. 1. Organization and Sequence of the Gene Cluster Encoding
the Major Phycobiliprotein Rod Components in the Genome of Marine
Synechococcus Sp WH8020. J Biol Chem 268(2):1226-1235.
PIGMENTS
Fraser PD, Linden H, Sandmann G (1993). Purification and Reactivation of
Recombinant Synechococcus Phytoene Desaturase from an Overexpressing
Strain of Escherichia coli. Biochem J 291( Part 3):687-692.
Fujita Y, Matsumoto H, Takahashi Y, Matsubara H (1993). Identification of a
nifDK-Like Gene (ORF467) Involved in the Biosynthesis of Chlorophyll in
the Cyanobacterium Plectonema boryanum. Plant Cell Physiol 34(2):305-314.
Garcia-Pichel F, Wingard CE, Castenholz RW (1993). Evidence regarding the UV
sunscreen role of a mycosporine-like compound in the cyanobacterium
Gloeocapsa sp. Appl Environ Microbiol 59:170-176.
Linden H, Vioque A, Sandmann G (1993). Isolation of a Carotenoid Biosynthesis
Gene Coding for zeta-Carotene Desaturase from Anabaena PCC 7120 by
Heterologous Complementation. FEMS Microbiol Lett 106(1):99-104.
Matsunaga T, Burgess JG, Yamada N, Komatsu K, Yoshida S, Wachi Y (1993). An
Ultraviolet (UV-A) Absorbing Biopterin Glucoside from the Marine
Planktonic Cyanobacterium Oscillatoria Sp. Appl Microbiol Biotechnol
39(2):250-253.
Reddy KJ, Bullerjahn GS, Sherman LA (1993). Characteristics of
Membrane-Associated Carotenoid-Binding Proteins in Cyanobacteria and
Prochlorophytes. Carotenoids, Pt B 214 390-401.
Sandmann G, Fraser PD (1993). Differential Inhibition of Phytoene Desaturases
from Diverse Origins and Analysis of Resistant Cyanobacterial Mutants. Z
Naturforsch C 48(3-4):307-311.
ELECTRON TRANSPORT and BIOENERGETICS
Alge D, Peschek GA (1993). Characterization of a cta/CDE Operon-Like Genomic
Region Encoding Subunits I-III of the Cytochrome c Oxidase of the
Cyanobacterium Synechocystis PCC 6803. Biochem Mol Biol Int 29(3):511-525.
Alge D, Peschek GA (1993). Identification and Characterization of the ctaC
(coxB) Gene as Part of an Operon Encoding Subunit-I, Subunit-II, and
Subunit-III of the Cytochrome c Oxidase (Cytochrome aa3) in the
Cyanobacterium Synechocystis PCC 6803. Biochem Biophys Res Commun
191(1):9-17.
Howitt CA, Smith GD, Day DA (1993). Cyanide-Insensitive Oxygen Uptake and
Pyridine Nucleotide Dehydrogenases in the Cyanobacterium Anabaena
PCC 7120. Biochim Biophys Acta 1141(2-3):313-320.
Joliot P, Vermeglio A, Joliot A (1993). Supramolecular Membrane Protein
Assemblies in Photosynthesis and Respiration. Biochim Biophys Acta
1141(2-3):151-174.
Kaprelyants AS, Kell DB (1993). The Use of 5-Cyano-2,3-Ditolyl Tetrazolium
Chloride and Flow Cytometry for the Visualisation of Respiratory Activity
in Individual Cells of Micrococcus Luteus. J Microbiol Meth 17(2):115-122.
Knaff DB (1993). The Cytochrome bc1 Complexes of Photosynthetic Purple
Bacteria. Photosynth Res 35(2):117-133.
Mctavish H, Laquier F, Arciero D, Logan M, Mundfrom G, Fuchs J, Hooper AB
(1993). Multiple Copies of Genes Coding for Electron Transport Proteins
in the Bacterium Nitrosomonas Europaea.4.1 GENOME. J Bacteriol
175(8):2445-2447.
Medina M, Diaz A, Hervas M, Navarro JA, Gomez-Moreno C, De La Rosa MA, Tollin
G (1993). A comparative laser-flash absorption spectroscopy study of
Anabaena PCC 7119 plastocyanin and cytochrome c6 photooxidation by
photosystem I particles. Eur J Biochem 213:1133.
Bovy A, Devrieze G, Lugones L, Vanhorssen P, Vandenberg C, Borrias M,
Weisbeek P (1993). Iron-Dependent Stability of the Ferredoxin I
Transcripts from the Cyanobacterial Strains Synechococcus Species PCC 7942
and Anabaena Species PCC 7937. Mol Microbiol 7(3):429-439.
Dai HP, Kentemich T, Schmitz K, Muller B, Bothe H (1992). Distribution of
Thioredoxins in Heterocysts and Vegetative Cells of Cyanobacteria. J
Photochem Photobiol B-Biol 16(3-4):285-295.
Hervas M, Navarro F, Navarro JA, Chavez S, Diaz A, Florencio FJ, Delarosa MA
(1993). Synechocystis 6803 Plastocyanin Isolated from Both the
Cyanobacterium and E. coli Transformed Cells Are Identical. FEBS Lett
319(3):257-260.
Medina M, Diaz A, Hervas M, Navarro JA, Gomezmoreno C, Delarosa MA, Tollin
G (1993). A Comparative Laser-Flash Absorption Spectroscopy Study of
Anabaena PCC 7119 Plastocyanin and Cytochrome c6 Photooxidation by
Photosystem I Particles. Eur J Biochem 213(3):1133-1138.
Medina M, Gomezmoreno C, Tollin G (1992). Effects of Chemical Modification
of Anabaena Flavodoxin and Ferredoxin NADP+ Reductase on the Kinetics of
Interprotein Electron Transfer Reactions. Eur J Biochem 210(2):577-583.
Schmitz O, Kentemich T, Zimmer W, Hundeshagen B, Bothe H (1993).
Identification of the nifJ Gene Coding for Pyruvate-Ferredoxin
Oxidoreductase in Dinitrogen-Fixing Cyanobacteria. Arch Microbiol
160(1):62-67.
Stockman BJ, Euvrard A, Kloosterman DA, Scahill TA, Swenson RP (1993). 1H and
15N Resonance Assignments and Solution Secondary Structure of Oxidized
Desulfovibrio Vulgaris Flavodoxin Determined by Heteronuclear
3-Dimensional NMR Spectroscopy. J Biomol Nmr 3(2):133-149.
Tamagnini P, Yakunin AF, Gogotov IN, Lindblad P (1993). Plant-Type and
Bacterial-Type Ferredoxins in a Nitrogen-Fixing Cyanobacterium - Nostoc
Sp Strain PCC 73102. FEMS Microbiol Lett 107(1):37-42.
Yakunin AF, Hallenbeck PC, Troshina OY, Gogotov IN (1993). Purification and
Properties of a Bacterial-Type Ferredoxin from the Nitrogen-Fixing
Cyanobacterium Anabaena variabilis ATCC 29413. Biochim Biophys Acta
1163(2):124-130.
Bakels RHA, Vanwalraven HS, Krab K, Scholts MJC, Kraayenhof R (1993). On the
Activation Mechanism of the H+-ATP Synthase and Unusual Thermodynamic
Properties in the Alkalophilic Cyanobacterium Spirulina platensis. Eur J
Biochem 213(3):957-964.
Krab K, Bakels RHA, Scholts MJC, Vanwalraven HS (1993). Activation of the
H+-ATP Synthase in Thylakoid Vesicles from the Cyanobacterium
Synechococcus 6716 by H - Including a Comparison with Chloroplasts, and
Introducing a New Method to Calibrate Light-Induced. Biochim Biophys Acta
1141(2-3):197-205.
Krenn BE, Koppenaal F, Vanwalraven HS, Krab K, Kraayenhof R (1993).
Co-reconstitution of the H+-ATP Synthase and Cytochrome b563/c554 Complex
from a Thermophilic Cyanobacterium - High ATP Yield and Mutual Effects on
the Enzymatic Activities. Biochim Biophys Acta 1140(3):271-281.
Schluchter WM, Zhao JD, Bryant DA (1993). Isolation and Characterization of
the ndhF Gene of Synechococcus Sp Strain PCC 7002 and Initial
Characterization of an Interposon Mutant. J Bacteriol 175(11):3343-3352.
MOLECULAR GENETICS and METABOLISM OF MACROMOLECULES
Kuritz T, Ernst A, Black TA, Wolk CP (1993). High-Resolution Mapping of
Genetic Loci of Anabaena PCC 7120 Required for Photosynthesis and Nitrogen
Fixation. Mol Microbiol 8(1):101-110.
Vachhani AK, Iyer RK, Tuli R (1993). A Mobilizable Shuttle Vector for the
Cyanobacterium Plectonema boryanum. J Gen Microbiol 139:569-573.
Walton DK, Gendel SM, Atherly AG (1993). DNA Sequence and Shuttle Vector
Construction of Plasmid pGL3 from Plectonema boryanum PCC 6306. Nucleic
Acids Res 21(3):746.
Kim ST, Sancar A (1993). Photochemistry, Photophysics, and Mechanism of
Pyrimidine Dimer Repair by DNA Photolyase. Photochem Photobiol
57(5):895-904.
Kovacs SA, Oneil J, Watcharapijarn J, Moekirvan C, Vijay S, Silva V (1993).
Eubacterial Components Similar to Small Nuclear Ribonucleoproteins -
Identification of Immunoprecipitable Proteins and Capped RNAs in a
Cyanobacterium and a Gram-Positive Eubacterium. J Bacteriol
175(7):1871-1878.
Piechula S, Kur J, Bielawski K, Podhajska AJ (1992). Isolation and
Identification of the Restriction Endonuclease PtaI from Phormidium
Tadzschicicum, an Isoschizomer of BspMII. Nucleic Acids Res 20(24):6738.
Lehel C, Los D, Wada H, Gyorgyei J, Horvath I, Kovacs E, Murata N, Vigh L
(1993). A 2nd groEL-Like Gene, Organized in a groESL Operon Is Present in
the Genome of Synechocystis Sp PCC 6803. J Biol Chem 268(3):1799-1804.
Schmidt J, Subramanian AR (1993). Sequence of the Cyanobacterial tRNA(w) Gene
in Synechocystis PCC 6803 - Requirement of Enzymatic 3' CCA Attachment to
the Acceptor Stem. Nucleic Acids Res 21(10):2519.
Nakai M, Sugita D, Omata T, Endo T (1993). SecY Protein Is Localized in Both
the Cytoplasmic and Thylakoid Membranes in the Cyanobacterium
Synechococcus PCC 7942. Biochem Biophys Res Commun 193(1):228-234.
APPLIED CYANOBACTERIOLOGY
Bhaskar M, Sreenivasulu C, Venkateswarlu K (1992). Interactions of
Monocrotophos and Quinalphos with Anabaena torulosa Isolated from Rice
Soil. Biochem Int 28(5):767-773.
Megharaj M, Pearson HW, Venkateswarlu K (1993). Physiological and
Morphological Alterations Induced by Carbaryl and 1-Naphthol Combinations
in Nostoc Linckia Isolated from Soil. Curr Microbiol 27(1):41-45.
Milicia F, Favilli F (1993). Azolla symbiotic system's application as
biofertilizer for green garden crops. Symbiosis 14:495-500.
Nguyen VH, Alexeyev M, Kozyrovskaya N, Kordyum V, Elhai J (1992). Anabaena
thermalis: a nitrogen-fixing cyanobacterium associated with rice.
Biopolymers Cell 8:44-48.
Obreht Z, Kerby NW, Gantar M, Rowell P (1993). Effects of root-associated
N2-fixing cyanobacteria on the growth and nitrogen content of wheat
(Triticum vulgare L.) seedlings. Biol Fertil Soils 15:68-72.
Obulakondaiah M, Sreenivasulu C, Venkateswarlu K (1993). Nontarget Effects
of Carbaryl and Its Hydrolysis Product, 1-Naphthol, Towards Anabaena
Torulosa. Biochem Mol Biol Int 29(4):703-710.
Painter TJ (1993). Carbohydrate Polymers in Desert Reclamation - The
Potential of Microalgal Biofertilizers. Carbohyd Polym 20(2):77-86.
Roger PA, Zimmerman WJ, Lumpkin TA (1992). Microbiological management of
wetland rice fields. In: Soil Microbial Ecology (FB Metting Jr, ed).
Marcel Dekker, New York, pp.417-455.
Tadros MG, Smith W, Joseph B, Phillips J (1993). Yield and Quality of
Cyanobacteria - Spirulina maxima in Continuous Culture in Response to
Light Intensity. Appl Biochem Biotechnol SPR;39337-347.
Xu XD, Kong RQ, Hu YX (1993). High Larvicidal Activity of Intact Recombinant
Cyanobacterium Anabaena Sp PCC 7120 Expressing Gene-51 and Gene-42 of
Bacillus Sphaericus Sp 2297. FEMS Microbiol Lett 107(2-3):247-250.
Sailer M, Helms GL, Henkel T, Niemczura WP, Stiles ME, Vederas JC (1993).
15N-Labeled and 13C-Labeled Media from Anabaena Sp for Universal Isotopic
Labeling of Bacteriocins - NMR Resonance Assignments of Leucocin-A from
Leuconostoc gelidum and Nisin-A from Lactococcus lactis. Biochemistry
32(1):310-318.
ADDRESSES*ADDRESSES*ADDRESSES*ADDRESSES*ADDRESSES*ADDRESSES*ADDRESSES*ADD
CONTRIBUTORS
Bianca Brahamsha Scripps Institute of Oceonagraphy, University of
California-San Diego, La Jolla CA 92093 U.S.A.
(E-mail) BBrahamsha@Ssurf.Ucsd.Edu
John Cobley Dept. of Chemistry, University of San Francisco, 2130
Fulton St., San Francsico CA 94117 U.S.A.
(Tel) 415-666-6450, (E-mail) Cobley@Compserv.Usfca.Edu
Jari Kiviranta Dept. of Pharmacy, P.O. Box 15, University of Helsinki,
FIN-0014 Helsinki, FINLAND. (Tel) 358-0-1912635,
(Fax) 358-0-1912786.
Rogerio Lacaz-Ruiz Universidade de Sao Paulo - Faculdade de Zootecnia, CP23
CEP13630-000 Pirassununga-sp, BRAZIL.
(E-mail) RogLRuiz@Brusp.Ansp.Br
Nick Mann Dept. of Biological Sciences, University of Warwick,
Coventry, CV4 7AL UK (Tel) 0203-523523, (Fax) 0203-523568
(E-mail) NM@Dna.Bio.Warwick.Ac.Uk
Martin Mulligan Dept. of Biochemistry, Memorial Univ. of Newfoundland,
St. John's, Newfoundland A1B 3X9 CANADA.
(Tel) 709-737-7978, (Fax) 709-737-2422,
(E-mail) Mulligan@Kean.ucs.mun.ca
Brian Palenik Marine Biology Research Division, Scripps Institution of
Oceanography, University of California-San Diego, La
Jolla CA 92093 U.S.A. (E-mail) Ir108@sdcc1.ucsd.edu
Laurie Richardson Dept. of Biological Sciences, Florida International
University, University Park, Miami CA 33199 U.S.A.
(Tel) 305-348-1988, (Fax) 305-348-1986,
(E-mail) RichardL@Servax.Bitnet
Mike Schaefer School of Biological Sciences, University of Missouri-KC
BSB 213, 5100 Rockhill Rd, Kansas City MO 64110-2499
USA (Tel) 816-235-2573, (E-mail) MSchaefer@Vax1.Umkc.Edu
Olav Skulberg Norwegian Institute for Water Research, P.O.box 69
Korsvall, N-0808 Oslo 8 NORWAY
Bob Tabita Department of Microbiology, The Ohio State University,
484 West 12th Avenue, Columbus OH 43210-1292 U.S.A.
(Tel) 614-292-4297, (Fax) 614-292-1538
(E-mail) RTabita@Magnus.Acs.Ohio-State.Edu
Nikos Tsinoremas Dept. of Biology, Texas A&M University, College Station
TX 77843 U.S.A. (E-mail) Nicholas@Bio.Tamu.Edu
Bob Webb Dept. of Biological Sciences, University of Texas at El
Paso, El Paso TX U.S.A. (E-mail) jx02@utep.Bitnet
Jindong Zhao Applied Biosystems, 850 Lincoln Centre Dr., Foster City,
CA 94404 U.S.A. (Tel) 415-570-6667
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Send CONTRIBUTIONS to one of the addresses listed below. To SUBSCRIBE, send
$10 U.S. (or equivalent in any currency) per year to Jeff Elhai, along with
your name, telephone, FAX, and EMail numbers (if any), and a brief
description of your research interests for inclusion in the next Directory
of Cyanobacteriologists. If it is difficult for you to send hard currency,
send a note indicating your interest.
AUSTRALIA Steve Delaney Department of Biotechnology,
/NEW ZEALAND University of New South Wales, P.O.
Box 1, Kensington, New South Wales
AUSTRALIA 2033
AUSTRIA Georg Schmetterer Institut fur Physikalische Chemie,
Wahringerstrasse 42, A-1090 Wien
(EMail) A8422dad@Awiuni11
CANADA Neil Strauss Dept. of Botany, University of
Toronto, Toronto, Ontario M5S 1A1.
(E-mail) StrausNA@gpu.utcs.UToronto.Ca
P.R.CHINA Chao-Tsi Tseng Centre of Marine Sciences, Department
of Biology, Nanjing University,
Nanjing
CZECHOSLOV. Jiri Komarek Institute of Botany, CAS Dept. of
Hydrobotany, Dukelske 145, CS-37982
Trebon
FRANCE Nicole Tandeau de Marsac Physiologie Microbienne, Institut
Pasteur, 29 rue du Dr. Roux, 75724
Paris Cedex 15. (EMail) Cyano@Pasteur
GERMANY Wolfgang Lockau Institut fuer Botanik, Universitaet,
Universitaetsstr. 31, 8400
Regensburg
INDIA Joe Thomas Biotechnology Division, SPIC Science
Foundation, 110 Mount Road, Madras
600 032
ISRAEL Elisha Tel-Or Dept. of Agricultural Botany, The
Hebrew University, Rehovot 76100
(Tel) 08-481262
ITALY Mario Tredici Centro di Studio dei Microorganismi
Autotrof. (C.N.R.), P.le. delle
Cascine 27 51044 Firenze
(E-mail) D47000@Ifiidg.Fi.Cnr.It
NETHERLANDS Luuc Mur Laboratorium voor Microbiologie,
Universiteit voor Amsterdam, Nieuwe
Achtergracht 127, 1018 WS Amsterdam
SCANDANAVIA Olav Skulberg Norwegian Institute for Water
Research, P.O.box 69 Korsvall, N-0808
Oslo 8 NORWAY
U.K. Tony Walsby Dept. of Botany, University of
Bristol, Bristol BS8 1UG
ANYWHERE ELSE Jeff Elhai Dept. of Biological Sciences, Florida
International University, University
Park Campus, Miami FL 33199 USA.
(Tel) 305-348-3584, (Fax) 305-348-1986
(E-mail) Cyano@Servax.Bitnet
or Cyano@Servax.Fiu.Edu