CYANONEWS
Volume 11 Number 1 February 1995
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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. (See address label for expiration
date). No charge for electronic version.
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 - Each news item contains,
prominently displayed, the name of a contact person. A Directory of
Cyanobacteriologists is distributed every two years or on request.
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*CONTENTS*CONTENTS*CONTENTS*CONTENTS*CONTENTS*CONTENTS*CONTENTS*CONTEN
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BULLETIN BOARD
* "Molecular Biology of Cyanobacteria" now available
* Translation, editing service
* Backpacking trip
* How to get the news out about collections of cyanobacteria
* Meetings
* Positions sought, Positions available
TRANSITIONS
* Comings and goings of ourselves
* Daniel Arnon (1910-1994)
NEWS
* Chromophore spectra made plain
* Startling glycolipid genes in hetR region
* Plastocyanin works in normally PC-less strain
* Calcium powers cyanobacterial membranes
* New extrinsic PSII protein
* Meeting report: Phototrophic Prokaryotes
REFERENCES
ADDRESSES
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BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD*BUL
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****** Matters Arising ******
That mammoth project, THE MOLECULAR BIOLOGY OF CYANOBACTERIA, edited by Don
Bryant, has finally been published, all 28 chapters and 916 pages. The book
is divided into four parts: (1) molecular evolution and taxonomy,
(2) structural and functional aspects of the photosynthetic apparatus, and
(3) biochemical processes, and (4) gene regulation and the phenomena they
regulate. It is available at US $355 (hardbound) or US $190 (paperback).
Contact (North America): Kluwer Academic Publishers Group, Order Dept.
P.O. Box 358, Accord Station, Hingham MA 02018-0358 USA. Tel: 617-
871-6600, Fax: 617-871-6528, E-mail: Kluwer@World.Std.Com
Contact (elsewhere): Kluwer Academic Publishers Group, Order Dept.,
P.O. Box 322, 3300 AH Dordrecht, The Netherlands. Tel: 31-78-524400,
Fax: 31-78-524474, E-mail: Services@Wkap.Nl
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Gisela Hoschek is offering a novel service. She is recently retired from
laboratory work (molecular biology, biochemistry, molecular genetics) but
wants to stay connected and active. Her idea is to offer her services to HELP
TRANSLATE OR EDIT research papers or grant applications in English written by
authors who are not native speakers. She is fluent in German and passable in
French.
Contact: Gisela Hoschek, 1124 Nardo Road, Encinitas, CA 92024 USA.
Tel: 619-944-4233, E-mail: Hoschek@Jeeves.Ucsd.Edu
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As seems to happen once every year or two, Peter Wolk is wondering
whether any cyanobacteriologist might care to accompany him on a BACKPACKING
TRIP in the U.S. Rockies. The trip will occur sometime this summer.
Contact: Peter Wolk, 22333cpw@msu.edu or 517-353-2049.
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P.K. Singh hopes to use the newsletter as a vehicle for disseminating
information about the various COLLECTIONS OF CYANOBACTERIA held throughout the
world. As a start, he has described the objectives of the National Facility
for Blue-Green Algal Collection (in New Delhi, India) of which he is the
Project Director. Its objectives are:
1.To act as a national center for cultures of cyanobacteria;
2.To conduct research on cyanobacteria, especially the occurrence and
distribution of N2-fixing strains, their isolation, maintenance, and
preservation, but also cyanobacterial physiology and genetics;
3.To provide advice to farmers in the use of cyanobacterial biofertilizers;
4.To organize seminars, conferences, and training sessions;
5.To act as a strong center for national research and development;
6.To provide advice on policy matters.
Contact: National Facility for Blue-Green Algal Collection (Auditorium
Complex), Indian Agricultural Research Institute, New Delhi-110012,
INDIA. Tel: 91-011-578-8431, Fax: 91-011-575-2006, E-mail: Guest%Bic-
iari@Dbt.Ernet.in
****** Meetings ******
The 12th Annual Eastern Regional Photosynthesis Conference is scheduled for
24-26 March, 1995 at Marine Biological Laboratory, Woods Hole, MA, USA.
Undergraduates, graduate students, and post-doctoral fellows are especially
encouraged to deliver oral presentations. A single fee covering registration,
accommodations for two nights, and meals starts at US$162. Checks should be
made payable to City College Bursar c/o Regional Photosynthesis Conference.
Contact: Marilyn Gunner, Dept. of Physics, City College of New York,
138th St. and Convent Ave, New York, NY 10031 USA. Tel: 212-650-5501.
Fax: 212-650-550312, E-mail: Gunner@Sci.Ccny.Cuny.Edu
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The Third European Workshop on the Molecular Biology of Cyanobacteria is
scheduled for 11-14 May, 1995 in Sevilla, Spain. The registration fee will be
25,000 Spanish pesetas, with hotel lodging starting at 18,500 pesetas per
person. Some fellowships are available. The deadline for receipt of payment
and registration is Feb 28, 1995. These fees may be paid by bank transfer to:
Cyanobacterial Workshop, account no. 43-475-527621, Banco Herrero, Calle
Rioja, no. 7, E-41001 Sevilla, Spain (remembering to state your name on the
bank transfer for identification).
Contact: Enrique Flores, Instituto de Bioquimica Vegetal y
Fotosintesis Universidad de Sevilla-CSIC Facultad de Biologia
Apartado 1113, E-41080 Sevilla Spain. Fax: +34-5-462 01 54,
Email:cyano@cica.es
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The VTH CYANOBACTERIAL MOLECULAR BIOLOGY WORKSHOP will again be on the Pacific
Ocean in Asilomar, California U.S.A., 21-25 July, 1995. Registration is U.S.
$50 and housing and meals begin at U.S.$225. Deadline for abstracts is May 1.
Deadline for registration is June 9.
Contact: Don Bryant, S-234 Frear Bldg., Dept. of Biochemistry and
Molecular Biology, The Pennsylvania State University, University
Park, PA 16802. Tel: 814-865-1992, E-mail: DAB14@Psuvm.Psu.Edu
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The FIRST INTERNATIONAL CONGRESS ON TOXIC CYANOBACTERIA (BLUE-GREEN ALGAE)
is the new descendent of the formerly biannual Nordic Symposia on Toxin-
producing Algae. The Congress will be held on the Danish island of Bornholm
in the Baltic on 20-24 August 1995. It is planned that the proceedings will
be published.
Contact: Peter Henriksen, Dept. of Phycology, Botanical Institute,
Щ. Farimagsgade 2 D, DK-1353 Copenhagen K, DENMARK.
Tel: 45-35-32-22-90 or 45-35-32-22-99, Fax: 45-35-32-23-21,
E-mail: PHenriks@Bot.Ku.Dk
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The 13th International Symposium on Cyanophyte Research will take place in
Rome 27 Aug to 3 Sep 1995. The Symposium will focus on taxonomy, extreme
environments, biodiversity, cyanobacterial associations with other
organisms, and ecophysiology. Registration is 200,000 lira. Meals and hotel
accommodations start at 900,000 lira for the nine day symposium.
Contact: Patrizia Albertano, Department of Biology, University of
Rome `Tor Vergata', via della Ricerca scientifica, 00133 Rome Italy.
Tel: 39-6-72594345, Fax: 39-6-2023500,
E-mail: Albertano@Tovvx1.Ccd.Utovrm.It
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The European Society for Photobiology will hold its 6th Congress in Cambridge
(Churchill College) from 2nd to 9th September 1995. The congress will have
special session on "Carotenoids in Photosynthesis and Medicine" and "Appli-
cation of protein engineering for the study of light reactions of oxygenic
photosynthesis"
Contact: Paul Heelis, Faculty of Science, Health and Medical Studies,
The North East Wales Institute, Plas Coch, Mold Road, Wrexham, Clwyd,
LLI 2AW,UK. Fax: 44 (0) 1978 290008, E-mail: Heelisp@Newi.Ac.Uk
****** Positions Offered ******
POSITION OFFERED: Post-Doc
CONTACT: Bruce Greenberg, Dept. of Biology, University of Waterloo,
Waterloo, Ontario N2L 3G1, CANADA. Tel: 519-888-4567 x3209,
Fax: 519-746-0614, E-mail: Greenber@Biology.Watstar.UWaterloo.CA
RESEARCH: (1) UV-B impact on plants, (2) Photoinduced toxicity of priority
pollutants to plants. Both projects will be carried out at the
biochemical and cellular levels, with effects on photosynthesis a major
interest.
SEND: CV and names of three references.
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POSITION OFFERED: Post-Doc
CONTACT: James Yungel, NASA Goddard Space Flight Center's Wallops Flight
Facility in the Airborne Oceanographic Lidar (AOL) program.
E-mail: Hoge@Osb1.Wff.Nasa.Gov or Yungel@Wff.Nasa.Wff
RESEARCH: Investigate optical properties of phycourobilin and
phycoerythrobilin pigments contained in marine phytoplankton as it
relates to remote detection of these pigments from laser excited
fluorescence spectra and passive ocean color spectra.
SEND: Brief description of experience in related research.
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POSITION OFFERED: Post-Doc
CONTACT: H.Y. Yamamoto, HITAHR, University of Hawaii, 3050 Maile Way,
Gilmore 202 B, Honolulu, Hawaii 96822, USA
RESEARCH: Biochemistry and mechanism of down regulation of PSII photochemical
efficiency by xanthophyll-dependent non-photochemical chlorophyll
fluorescence quenching.
REQUIREMENTS: Research experience using isolated chloroplast systems.
Experience or knowledge of chlorophyll fluorescence, xanthophyll cycle,
carbon-fixation, spectrophotometric methods and pigment-protein
separations is highly desirable. Candidate should be self-motivated,
able to work independently and accomplishment orientated.
SUPPORT: One year with possible extension for another year.
SEND: CV, letter of application, two confidential letters of recommendation.
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POSITION OFFERED: Post-Doc
CONTACT (before March 31): Carl Johnson c/o Susan Golden, Dept. of Biology,
Texas A&M University, College Station, TX 77843 U.S.A.
E-Mail: JohnsonC@Bio.Tamu.Edu
CONTACT (after March 31): Carl Johnson, Dept. of Biology, Box 1812-B,
Vanderbilt University, Nashville, TN 37235 U.S.A.
E-Mail: JohnsonC@Vuctrvax.Bitnet
RESEARCH: Study molecular basis of circadian rhythmicity in cyanobacteria,
using reporter strain to isolate, clone, and identify genes involved in
the circadian clockwork [see Science 266:1233-1236 and Proc Natl Acad
Science USA 90:5672-5676].
REQUIREMENTS: Training in current molecular genetic techniques and strong
interest in circadian rhythms.
SEND: CV, summary of doctoral dissertation and current research interests, two
letters of recommendation.
Positions Sought
POSITION SOUGHT: Post-doc or sabbatical replacement
CONTACT: S.A. Kulasooriya, Dept. of Botany, University of Peradeniya,
Peradeniya, SRI LANKA. Fax: 94-8-32343
TEACHING EXPERIENCE: 28 years at University of Peradeniya. Lectures,
laboratory classes, field classes in Introductory Botany, Plant
Diversity, Mycology, Microbiology, Soil Biology, Biological Nitrogen
Fixation, Soil Fertility.
RESEARCH EXPERIENCE (abridged):
Ph.D., University of London (1971), G.E. Fogg and Peter Fay, advisors
on "Heterocyst Differentiation and Nitrogen Fixation in Blue-green
Algae". See Proc Royal Soc Lond (1972) 181:31-52. Nitrogen
fixation in rice fields. See Ann Bot (1981) 47:31-52.
Sabbatical leave at International Rice Research Institute (IRRI),
examining rice field cyanobacteria, especially epiphytic strains.
See Blue-green Algae and Rice, by PA Roger and SA Kulasooriya
(1980), IRRI, Los Baдos, and Soil Sci Plant Nutr (1981) 27:19-27.
Nitrogen fixation by Azolla-cyanobacterial symbiosis Biological nitrogen
fixation and maintenance of soil fertility in sustainable
ecosystems. See Plant Soil (1991) 135:297-302, Biol Fert Soil
(1992)14:37-42.
SERVICE (abridged):
Visiting consultant FAO/IAEA Division of Soil Fertility, Irrigation and
Crop Production, Vienna, Austria
UNDP Advisory Board on Nitrogen Fixation, IRRI
Chairman, FAO Expert Consultation on Bio and Organic Fertilizers,
Bangkok.
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TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSI
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NANCY FEDERSPIEL has moved... You know all this? You heard long ago that she
left U. Idaho for a biotech outfit in California? Well, she's moved again.
This time to the Genome Center, with Ron Davis' group, at Stanford University.
She hopes someday to return to cyanos.
Genome Center, Dept. of Biochemistry, Stanford University, Stanford CA
94305. E-mail: NFeder@Genome.Stanford.Edu
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GOVINDJEE hasn't moved but electrons will have to travel a different path to
reach him.
E-mail: Govindje@aries.scs.uiuc.edu (note only one "e" at end) or
(preferably) Gov@Uiuc.Edu. E-mail with enclosures can be sent to
Govindjee@Powershare.Life.Uiuc.Edu. Fax: 217-244-7246 (office), and
217-337-6196 (home).
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P.K. SINGH has left the Indian Institute of Sugarcane Research to take a
position as Project Director of the National Facility for Blue-Green Algal
Collection [See announcement, this issue].
National Facility for Blue-Green Algal Collection (Auditorium
Complex), Indian Agricultural Research Institute, New Delhi-110012,
INDIA. Tel: 91-011-578-8431, Fax: 91-011-575-2006,
E-mail: Guest%Bic-iari@Dbt.Ernet.in
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ZHAO JINDONG, after leaving Don Bryant's lab at Pennsylvania State
University, and resting for a while at Applied Biosystems in California,
now finds himself in a faculty position at Beijing University, still
interested in photosynthetic electron transport.
Dept. of Plant Molecular Biology, College of Life Sciences, Beijing
University, Beijing 100871, P.R.CHINA. Tel: 86-1-250-1855, Fax: 86-1-
258-5864
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Daniel I. Arnon 1910-1994
Daniel I. Arnon died suddenly of cardiac arrest at the age of 84 on
Tuesday, December 20, 1994 in Berkeley, California. At the time of his death,
Arnon was an emeritus faculty member at the University of California at
Berkeley, where he had spent his entire academic career carrying out his
pioneering work on the biochemistry of photosynthesis. With his passing, an
era in the field of photosynthesis has ended.
In a series of historical papers in the mid-1950's, Arnon's Berkeley
group, which included M. B. Allen and F. R. Whatley, discovered that
chloroplasts were capable of synthesizing ATP in the light, in a process Arnon
called "photosynthetic phosphorylation" (photophosphorylation) to distinguish
it from oxidative phosphorylation. The first type of chloroplast
phosphorylation discovered, denoted "cyclic phosphorylation," produced only
ATP in the light. This discovery was followed by another revolutionary
finding--that both ATP and NADPH could be produced photochemically and that
their production was linked to the evolution of oxygen in a series of
reactions called "non-cyclic photophosphorylation.". As part of this series
of studies, isolated chloroplasts were found to be able to carry out complete
photosynthesis in the light, a finding that proved that "cell-free"
photosynthesis was possible .In an extensive series of papers with M. Losada
and A. Trebst that followed this work, the Arnon group then extended these
early observations by showing that the photophosphorylation reactions could
generate the ATP and NADPH required for CO2 assimilation. This was the first
demonstration that complete photosynthesis, the process central to life on our
planet, could be experimentally obtained outside a living cell. As a result
of this work, the field of photosynthesis had been permanently changed: for
the first time it was realized that the chloroplast had the complete capacity
to carry out the reactions of photosynthesis, whereby light-energy is
converted into organic compounds.
The discovery of non-cyclic and cyclic phosphorylation led Arnon to
consider the mechanism of these processes. This resulted in K. Tagawa and
Arnon identifying and characterizing the iron-sulfur protein, chloroplast
ferredoxin in the early 1960s. Several other laboratories had been working
with this protein under other names but the Berkeley work clarified the role
of this protein in both the cyclic and non-cyclic pathways. Through their
study of ferredoxin-NADP+ reductase, the enzyme actually involved in NADPH
formation, M. Shin and Arnon were able to define the mechanism of NADP+
reduction, and in further work, to present their view that ferredoxin serves
as the natural catalyst of the cyclic pathway. In characterizing chloroplast
ferredoxin, Tagawa and Arnon had noted that this carrier had a midpoint redox
potential more electronegative than the NADPH/NADP+ couple, raising the
possibility that CO2 fixation might occur directly through the input of
electrons from reduced ferredoxin without utilizing the reduced pyridine
nucleotide system. This realization stimulated studies on photosynthetic
bacteria which led to the discovery of the reductive carboxylic acid cycle for
CO2 fixation in work with Mike Evans and Bob Buchanan in the mid-1960s. This
pathway is independent of the pathway previously demonstrated in higher plants
by Melvin Calvin, J. Bassham and A. Benson, also on the UC Berkeley campus.
The 1970s led Arnon and his group to consider mechanisms of electron
transfer in chloroplast photosynthesis. Based on his belief of the role of
non-cyclic and cyclic phosphorylation in chloroplasts, Arnon proposed a
mechanism for electron transfer the ran against the main current in the
photosynthetic field: that Photosystem I was involved only in the cyclic
pathway and only Photosystem II was linked to the non-cyclic pathway. This
view, held in modified form until his death, differed from the widely accepted
Z-scheme for electron transport in chloroplasts in which the two photosystems
cooperate in transferring electrons from water to NADP+. Up to the time of his
death, Arnon was still regularly coming to his office in the Department of
Plant Biology, writing extensively on his views on photosynthesis.
Arnon was recognized professionally both nationally and internationally.
He was a member of the U. S. National Academy of Sciences and academies in
Sweden, France and Germany. He was a Guggenheim Fellow with David Keilin in
Cambridge, England and Hugo Theorell at the Karolinska Institute in Stockholm,
Sweden and a Fulbright Scholar with Otto Warburg in Berlin. In 1973 he was
awarded the National Medal of Science for "his fundamental research into the
mechanism of green plant utilization of light to produce chemical energy and
oxygen and for contributions to our understanding of plant nutrition." In
recent years we have seen the loss of major figures in our field: Robin Hill,
Bessel Kok and Warren Butler. Equally as significant is the passing of Dan
Arnon. His contributions over an almost 50 year period on this field are
inestimable.
Richard Malkin, Dept. of Plant Biology, University of California, Berkeley
(Editor's note: While all of us are indebted to Daniel Arnon for changing the
way we think about photosynthesis, some may not be aware that he also deserves
our remembrance every time we grow a strain in A&A (Allen & Arnon) medium).
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NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEW
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Theory Developed for Analysis of Polarization Spectra
In a previous issue of CyanoNews (Volume 10, Number 1, February 1994)
ANDREY DEMIDOV reported on his work developing a new theory for analyzing the
polarization spectra of complex molecular systems with energy transfer between
molecules (chromophores). Molecules can have strongly overlapping spectra.
Demidov succeeded in deriving analytical formulae for determination of the
polarization spectra (at steady-state) and depolarization kinetics (ы- pulse
excitation) in cases of double- and triple-chromophore complexes. The formulae
were tested by applying them to C-phycocyanin subunits and monomers, and good
agreement with experimental data by Mimuro et al. [Biochim Biophys Acta (1986)
848:155] were found. The results of these investigations have been published
(see list of his references below under PHYCOBILISOMES and CAROTENOIDS).
Demidov is now considering the case of higher aggregates - trimers,
hexamers, etc. His preliminary results are promising and can be used for
quantitative deconvolution of absorption and fluorescence spectra of
allophycocyanin trimers. Such deconvolution will provide individual spectra
of alpha and beta chromophores. Deconvolution involves absorption,
fluorescence, and polarization spectra, i.e. it is based on the spectroscopic
approach.
He is looking for someone who may be interested in cooperation on this
matter. Cooperation can be in the form of work (preferably) in some particular
laboratory having necessary facilities and APC supplies, or in the form of
supplying the experimental data.
Demidov can be reached c/o D Andrews, University of East Anglia, School
of Chemistry, Norwich, Norfolk NR4 7TJ UK, or by E-mail at
A.Demidov@Uea.Ac.Uk
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Plastocyanin Promotes Electron Transport in PC-less Strain
Plastocyanin, a copper-bearing protein, is used by plants and most green
algae to donate electrons to Photosystem I. The protein is relatively rare in
cyanobacteria, which use cytochrome c553 instead as the PSI donor.
Synechococcus PCC 7942 is an example of a cyanobacterium that evidently lacks
plastocyanin and the gene, petE, that encodes it. DIRK GEERTS and others at
Utrecht, in collaboration with Hendrik Schubert and Hans Matthijs, took a petE
gene from a cyanobacterium, Anabaena PCC 7937, that does use plastocyanin and
expressed it in Synechococcus, wondering whether the strain would make any
sense out of it at all. To their surprise, the foreign protein was readily
accepted by PSI, and electron flow through PSI was markedly enhanced.
The petE gene from Anabaena was expressed from an inducible E. coli
promoter, Ptrc, thereby disconnecting transcription of the gene from its
normal regulation by the availability of copper. The gene product was
efficiently processed in Synechococcus and properly targeted to the thylakoid
lumen. Isolated thylakoid membranes from strains expressing petE showed up to
2.5-fold higher rates of electron transport than native membranes, and a
similar enhancement was evident in whole cells.
The activity of exogenous plastocyanin in Synechococcus may have
interesting implications regarding the mechanism by which electrons are
distributed between photosynthesis and respiration. Plastocyanin nearly
abolished the competition between the two systems. These and other results are
described in a recently published paper [Geerts et al. (1994) J Biol Chem
269:28068-28075].
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Surprise Glycolipid Biosynthetic Genes in het Region
The region of the Anabaena PCC 7120 chromosome near hetN has already
provided a few surprises for those interested in heterocyst differentiation,
for example genes that in multicopy induce unscheduled heterocyst
differentiation [Black et al (1994) J Bacteriol 176:2282-2292]. CHRIS BAUER
tells us that the region still has a few eye-openers left. Chris also noted
that a cosmid containing the hetN region affected heterocyst differentiation,
but what really caught his attention were three genes upstream from hetN:
hglB, hglC, and hglD (for Heterocyst GlycoLipid).
hglB has already been partially characterized. It contains domains for
acyl-carrier protein and NAD(P)H с-ketoacyl reductase similar to those found
in polyketide or fatty acid synthases. According to Chris' sequence, hglC
contains acyl/malonyl ACP transferase and с-keto-synthase domains, and hglD
(only partially sequenced) also contains a с-keto-synthase domain.
Inactivation of any of the three genes gave rise to a Fix- phenotype:
regularly spaced, ultrastructurally normal heterocysts (as judged by light
microscopy) incapable of nitrogen fixation. All three genes, and hetN as well,
are transcribed from 6 to 12 hours after nitrogen limitation, as seen by
Northern time-course blots.
These observations prompted a thin layer chromatography experiment to
check for the presence of heterocyst-specific glycolipid in mutants defective
in hglB, hglC, or hglD. It turns out that all three mutants fail to produce
the lipid, and Chris now believes that the products of these genes are
involved in glycolipid biosynthesis.
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Calcium Fluxes Can Energize Cyanobacteria
Cyanobacteria have been isolated from fresh, brackish, salty, and
extremely saline waters, and many highly mineralized bodies of water are more
greatly enriched with Ca2+ or Mg2+ than with Na+ [Hammer UT (1986) Saline like
ecosystems of the world. W. Junk, Dordrecht, p. 126]. IGOR BROWN has been
inspired by two ideas regarding the earth's early environment to propose that
cyanobacteria living in calcium-enriched waters may use calcium fluxes to
couple bioenergetic reactions.
Ancient bodies of water are postulated to have been alkaline with Ca2+
as the major cation [Ronov (1964) Geochem [Moscow] 8:715], and cyanobacteria
are thought to have been amongst their first inhabitants [Zarvazin (1993)
Microbiol [Moscow] 62:789]. If these two ideas were true, reasoned Brown, then
saturation by Ca2+ and Mg2+ would have prevented the generation of effective
levels of ■ц[H+] or ■ц[Na+]. On this basis, they have proposed that Ca2+ may
under some conditions play the role of coupling cation [Brown II (1994)
Biochem [Moscow] 8:715]. Gloeobacter violaceus living on limestone [Rippka
(1974) Arch Microbiol 100:419] was studied to test this hypothesis.
Brown and Galina Gorbik previously showed that Na+
can support electrogenic import of extracellular H+ - - - - - - - - - -
- - - - - - - - - - - - - - - - - - - - - - - - - - - -byG. violaceus cells
from alkaline medium [Gorbik GP, Brown II (1994) Int Symp Photosynth Prokar.
Abstracts. Urbino, Italy. 1994. p.25]. Now they report that Ca2+ is able to
substitute for Na+ to support growth of the strain under alkaline conditions
as well as electrogenic import of extracellular protons. The optimal Ca2+
concentration for these phenomena is about 9 mM. G. violaceus is not able to
grow under alkaline conditions (pH >= 9) if any BG-11 medium salt containing
Na+ or Ca2+ is replaced by a similar K+-containing salt. Growth of the strain
is normal under alkaline conditions in standard BG-11 (approximately 20 mM
Na+).
On the basis of this and other data [Geisler M et al (1993) J Mol Biol
234:1284], Brown and Gorbik suggest that ■ц[Ca2+] may provide energetic coupling
in cyanobacterial membranes.
- - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - -
New Extrinsic Proteins Found in Photosystem II
SHEN JIAN-REN reports that his group has found two new extrinsic
proteins in purified cyanobacterial photosystem II particles, namely,
cytochrome c550 and a 12 kDa protein. They have demonstrated that these two
extrinsic proteins are required to maintain maximal activity of oxygen
evolution in cyanobacterial photosystem II.
- - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - - -
VIII INTERNATIONAL SYMPOSIUM ON PHOTOTROPHIC PROKARYOTES - Meeting Report
The triennial International Symposium on Phototrophic Prokaryotes called to
the ancient Italian village of Urbino the usual collection of red, green, and
blue-green aficionados. The Symposium exhibited the most vigorous competition
(dance contest) and youngest convener (Luca Zannoni, age 8) in recent memory
but also boasted a variety of interesting talks and poster. The perspectives
below are intended to provide a flavor of the meeting; a complete summary of
all the varied high points could not possibly fit into a single newsletter.
If you want a fuller account of progress in cyanobacteriology, you may have
to wait until the IX International Symposium, to be held in 1997 in Vienna,
Austria.
Antennae and Reaction Centers
Much of interest was presented concerning antenna systems. Rowe and
Griffiths have isolated a gene encoding a protochlorophyllide reductase from
Phormidium laminosum. It will be interesting to see if this enzyme functions
as the light-induced reductase in cyanobacteria. Going slightly further
afield, Partensky and LaRoche showed that the N-terminus of the apoprotein of
the light-harvesting apparatus from the prochlorophyte Prochlorococcus is 82%
similar to the CP43' protein (encoded by isiA). The authors speculated that
Prochlorococcus could have descended from cyanobacterial ancestors and had
replaced the phycobilisome with a CP43'-like antenna which might have given
them an advantage for growth in iron-depleted oceanic areas.
For the noncyanobacterially inclined, Judy Shiozawa and Reiner Feick
rekindled the chlorosome debate by presenting evidence that proteins play an
important role in chlorosome structure in Chloroflexus aurantiacus. Digestion
of purified chlorosomes by proteases produced distinct changes in the shape
of the chlorosomes. Katsiou and Tadros have cloned a new LH II gene family
from Rhodopseudomonas palustris which they have named рс[e] (bringing the total
number to five). The с[e] subunit is the same as the с[b] subunit, but the р[e] is
very different from the other р subunits. This may allow the formation of
complexes with different absorbance characteristics. Indeed, more than one
LH II can be detected in the ICM in vivo by spectroscopic analyses.
An interesting development from Kjaer, Golbeck, and Scheller on green-
sulfur bacterial reaction centers was presented. They have isolated reaction
centers from Chlorobium vibrioforme with two intact Fe-S centers which
resemble the higher plant F[A] and F[B] clusters. The isolated reaction center
complex contains 6 polypeptides and supported photoreduction of NADP+ when
ferredoxin and FNR were added. Returning to cyanobacteria, Muhlenhoff, Bryant,
Zhao, and Setif presented data on a cyanobacterial PS I complex that had been
cross-linked with flavodoxin. Flavodoxin was covalently linked to the PsaC and
PsaD proteins and required the PsaE protein in order to bind in the proper
orientation. This cross-linked complex could not support electron transport
to FNR. However, flavodoxin could be functionally photoreduced from the
semi-quinone to the fully reduced form. Wim Vermaas presented comparisons
between heliobacterial and cyanobacterial reaction center complexes: an
evolutionary model in which PS I and II of cyanobacteria evolved from a
homodimeric reaction center, which probably resembled the heliobacterial
reaction center.
-- Wendy Schluchter
Ecology
Much work on microbial mat ecology has examined how nutrient
availability may influence species composition and distribution. In these
complex photosynthetic systems nutrient availability may only play part of the
story. Light as an ecological factor had been largely unstudied. Dick
Castenholz presented results of a recent examination of how UV and visible
light may influence survival strategies of various cyanobacterial groups. This
work along with similar studies of deeper-lying Chloroflexus species (pre-
sented by Beverly Pierson) is providing interesting new insights into the
structure of mat communities. It will be interesting in the future to see how
field-based studies such as these will dovetail with pure-culture biochemical
work on, for example, complementary chromatic adaptation. The role of sulfide
and its metabolism by various cyanobacterial species in the laboratory is
combined with ongoing detailed field work in the work of Rethmeier et al., to
likewise generate a comprehensive picture of the role of sulfide in affecting
cyanobacterial photosynthetic activity and distribution.
Newly described species were the focus of several nice presentations.
A few that particularly caught my eye were: (1) a beautifully detailed study
of a red strain of Spirulina subsalsa from a freshwater lake (by Luisa
Tomaselli et al.) (2) the description of a Leptolyngbya spp. with an eye-spot
type structure by Patrizia Albertano and Maria Grilli Caiola, and (3) an
intriguing Phormidium sp. responsible for killing corals in the Florida Keys
which is currently being well-documented in situ utilizing microsensors for
making oxygen, sulfide and pH measurements in the field by Laurie
Richardson New advances in taxonomy are being provided by the use of
molecular techniques. Research in this area, utilizing these new and still
developing technologies, is providing something of an explosion of new
information. Annick Wilmotte and Michael Herdman both presented good overviews
of what we can and cannot get out of the various phylogenetic tree schemes
available along with some important interpretation caveats. These techniques
are finally offering us the tools needed to clarify the confusing taxonomic
picture of the cyanobacteria that we all know and love.
These taxonomic findings may also have large ecological implications.
One such example was new data on the group Microcoleus chthonoplastes which
is suggesting that this group maintains a high degree of genotypic and
phenotypic homology world-wide with important implications for a high degree
of specificity for their particular niche habitat.
This meeting also provided a chance for many of us ecologically-inclined
souls to hear and see presentations on a somewhat bewildering array of
biochemical and molecular topics. In particular the series on reaction centers
were particularly interesting even if they sent the majority of ecologists out
looking for molecular-speak glossaries. Edification is good for the soul.
Especially in surroundings like the Toscany valley. In conclusion, many thanks
to the organizers. It was a great meeting!
-- Lee Prufert-Bebout
Light Receptor and Signal Cascade in Cyanobacteria?
The mechanisms by which cyanobacteria recognize changes in light quality
and intensity is thus far incompletely understood. Studies aimed at
understanding the signal transduction pathway linking light to light-regulated
behavior may proceed profitably down two parallel tracks: analysis of
light-regulated genes and comparative studies of photoreceptors.
Susan Golden described the transcriptional regulation of the psbA genes
of Synechococcus PCC 7942, encoding the D1 proteins of photosystem II. It is
very interesting that the transcription of a psbA gene is regulated by blue
light signal. The cis element for the blue light response has been
provisionally identified using many mutants carrying deletions in the 5'
upstream region of the psbA genes. The blue light signal is very likely to be
recognized by a specific photoreceptor or photoreceptors in cyanobacterial
cells. A mutant defective in the blue light response might provide a clue as
to the nature of the cyanobacterial blue light receptor. Franck Chauvat
identified sequence elements common to light-regulated promoters of
Synechocystis PCC 6803. The mechanisms of signal transduction of light will
be gradually solved by the isolation of light-regulated genes and genetic
studies of mutants defective in the regulation of their expression by light.
Meanwhile, a direct approach to defining the associated photoreceptors have
been producing interesting insights. W.D. Hoff presented a photoreceptor of
halophilic purple bacteria. They purified the photoactive yellow protein (PYP)
and determined the molecular structure of PYP. A photocycle of PYP is similar
to that of rhodopsin. However, the chromophore of PYP is not a retinal. The
chromophore is surrounded by the apoprotein, and PYP associates with the
membrane. The structure of PYP is very different from that of rhodopsin.
Hans Matthijs suggested that a rhodopsin-like receptor acts as a sensor
for complementary chromatic adaptation of the cyanobacterium, Fremyella
diplosiphon (Calothrix). They showed that the cyanobacterium contains a
retinal. It should be proven whether a photoreceptor homologous to PYP can
be found in cyanobacteria or whether cyanobacteria generally contain a
retinal. However, it is likely that cyanobacteria contain a photoreceptor
similar to the well-known photoreceptors.
-- Toshio Sakamoto
Cyanobacterial Development
We are coming closer to discovering how heterocyst-forming cyanobacteria
determine the frequency and spacing of heterocysts along a filament. The
results from Jeff Elhai's poster imply that the determining factor for the
initiation of heterocyst development may reside in individual cells and not
signals from adjacent cells in a filament. He found that long filaments of
Anabaena containing luxAB driven by the hetR promoter and filaments sonicated
to single cells both expressed the same level of luciferase activity upon
induction by nitrogen deprivation. Consistent with this result, an EM survey
showed that a single-cell mutant of the same strain responds quite
inhomogeneously to nitrogen starvation: only about 5% of its cells produce
heterocyst-specific polysaccharide.
From the results of Peter Rowell et al. one can begin to build a model
to explain Elhai's results. They found that formazan deposition in A.
cylindrica filaments incubated with MTT was localized to cell poles and
distributed in a pattern along a filament at potential sites of heterocyst
development. Thus an apparent differential accumulation of polarly localized
respiratory electron transport, possibly laid down as a function of pole age,
may have a role in determining which cells are destined to become heterocysts.
At sites where intercalary heterocysts will form, two vegetative cells with
nearly equal amounts of formazan deposition are found; these two cells must
somehow communicate to decide which will generate the daughter cell that
differentiates into a heterocyst. Jack Meeks noted that in many Fox- mutants
of Nostoc ATCC 29133 intercalary heterocyst doublets are common, possibly
because of a defect in this cell to cell communication.
Of course akinetes exhibit polarity as well. Sili and Vincenzini
presented some beautiful micrographs showing polar germination of Cyanospira
akinetes.
Bill Buikema and Bob Haselkorn reported obtaining up to 15% heterocysts
along a filament by overexpressing hetR transcription in Anabaena PCC 7120
containing a plasmid
with hetR behind the copper inducible petE promoter. - - - - - - - - - - -
- - - - - - - - - - - - - - - - - - - - - - - - - - -Itwill be interesting to
see if HetR is a point of control for increasing the frequency of heterocysts
in symbiotic systems. Bill Buikema is investigating the green fluorescent
protein (GFP) as an alternative reporter to luxAB in cyanobacteria. Expression
of GFP is easy to detect and has advantages over luxAB in not requiring a
substrate or oxygen for activity but, unlike luxAB, it is apparently toxic at
high concentrations. As was repeatedly stressed, luxAB can serve as a useful
reporter even without a $140,000 photometer.
Several different sized transcripts per gene, whether due to multiple
promoters or processing of larger transcripts, appears to be a common theme
in cyanobacteria. For example, Mike Summers reported 16 different transcripts
within the 4 gene zwf region, encoding glucose-6-phosphate dehydrogenase. As
the case with most cyanobacterial transcripts, it is unknown how the levels
of the specific mRNAs are regulated. In a poster, Martin Mulligan et al.
showed the ubiquity of RNA-binding proteins in cyanobacteria. These proteins
are known to have a variety of functions in eukaryotes (including in
chloroplasts, where post-transcriptional regulation predominate).
Regarding hormogonia differentiation, I reported that in Nostoc
ATCC 29133, just 2 bases upstream from a gene involved in decreasing
sensitivity to a hormogonia inducing factor, there is a gene with homology to
the same family of NAD(P)H-oxidoreductases that includes hetN. Perhaps
proteins of this family are of use in the production or modification of
signals affecting cyanobacterial differentiation. In two posters from Dave
Adams' lab, S. Babic reported the isolation and initial characterization of
mutants in hormogonium formation and H. Doherty reported cloning ftsZ from A.
7120; future work will examine whether ftsZ expression is regulated early in
hormogonium development. Doug Campbell has found that hormogonium
differentiation in Calothrix is favored by signals that inhibit heterocyst
formation and vice versa. The role, if any, of the PII protein (encoded by
glnB) in a hormogonia/heterocyst differentiation-signaling pathway is still
under investigation.
--Mike Cohen
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****** EVOLUTION, SYSTEMATICS, and PROCHLOROPHYTES ******
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****** ECOLOGY and SYMBIOSIS ******
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****** TOXINS and NATURAL SUBSTANCES ******
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****** TOXINS and NATURAL SUBSTANCES (Physiological Effects) ******
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****** PHYSIOLOGY ******
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CIRCADIAN RHYTHM
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MEMBRANES & LIPIDS
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temperature photoinhibition is accelerated by the unsaturation of
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Sakamoto T, Wada H, Nishida I, Ohmori M, Murata N (1994). Delta 9 acyl-lipid
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Sato N (1994). Effect of Exogenous Glucose on the Accumulation of Monoglucosyl
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Stocker A, Netscher T, Ruttimann A, Muller RK, Schneider H, Todaro LJ, Derungs
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STRESS RESPONSES
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Mallick N, Rai LC (1994). Kinetic Studies of Mineral Uptake and Enzyme
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NITROGEN METABOLISM
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the planktonic marine cyanobacterium Trichodesmium thiebautii. Appl
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NITROGENASE, HYDROGENASE, and DIFFERENTIATION
Angeloni SV, Potts M (1994). Analysis of the sequences within and flanking the
cyanoglobin-encoding gene, glbN, of the cyanobacterium Nostoc commune
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Fernandez-Piдas F, Leganes F, Wolk CP (1994). A third genetic focus required
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Frias JE, Flores E, Herrero A (1994). Requirement of the regulatory protein
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PHOTOSYNTHESIS
Barber J, Andersson B (1994). Revealing the blueprint of photosynthesis.
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McColl SM, Evans EH (1994). Sidedness in cyanobacterial thylakoid membranes.
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Vangrondelle R, Dekker JP, Gillbro T, Sundstrom V (1994). Energy transfer and
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Warner KM, Bullerjahn GS (1994). Light-dependent tyrosine phosphorylation in
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PHOTOSYSTEM I
Armbrust TS, Odom WR, Guikema JA (1994). Structural analysis of photosystem
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Fromme P, Schubert WD, Krauss N (1994). Structure of photosystem I:
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Gobets B, Vanamerongen H, Monshouwer R, Kruip J, Rogner M, Vangrondelle R,
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Kruip J, Bald D, Boekema E, Rogner M (1994). Evidence for the existence of
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Mannan RM, Pakrasi HB, Sonoike K (1994). The PsaC protein is necessary for the
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Setif PQY, Bottin H (1994). Laser flash absorption spectroscopy study of
ferredoxin reduction by photosystem I in Synechocystis sp. PCC 6803:
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Vanhaeringen B, Dekker JP, Bloemendal M, Rogner M, Vangrondelle R,
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Woolf VM, Wittmershaus BP, Vermaas WFJ, Tran TD (1994). Resolution of low-
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Xu Q, Armbrust TS, Guikema JA, Chitnis PR (1994). Organization of photosystem
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Xu QA, Guikema JA, Chitnis PR (1994). Identification of surface-exposed
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Xu Q, Jung YS, Chitnis VP, Guikema JA, Golbeck JH, Chitnis PR (1994).
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Xu Q, Odom WR, Guikema JA, Chitnis VP, Chitnis PR (1994). Targeted deletion
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PHOTOSYSTEM II
Anbudurai PR, Mor TS, Ohad I, Shestakov SV, Pakrasi HB (1994). The ctpA gene
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Barber J (1994). Photosystem II: No longer the black box of photosynthesis.
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Burnap RL, Qian M, Shen JR, Inoue Y, Sherman LA (1994). Role of disulfide
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and binding of the extrinsic manganese-stabilizing protein to the
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Derose VJ, Mukerji I, Latimer MJ, Yachandra VK, Sauer K, Klein MP (1994).
Comparison of the manganese oxygen-evolving complex in photosystem II
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Elanskaya IV, Allakhverdiev SI, Boichenko VA, Klimov VV, Demeter S, Timofeev
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Gleiter HM, Haag E, Shen JR, Eatonrye JJ, Inoue Y, Vermaas WFJ, Renger G
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Mamedov MD, Beshta OE, Samuilov VD, Semenov AY (1994). Electrogenicity at the
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Mamedov MD, Lovyagina ER, Verkhovskii MI, Semenov AY, Cherepanov DA, Shinkarev
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Nishiyama Y, Hayashi H, Watanabe T, Murata N (1994). Photosynthetic oxygen
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Nixon PJ, Diner BA (1994). Analysis of water-oxidation mutants constructed in
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Putnam-Evans C, Bricker TM (1994). Site-directed mutagenesis of the CP47
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Shestakov SV, Anbudurai PR, Stanbekova GE, Gadzhiev A, Lind LK, Pakrasi HB
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PHYCOBILISOMES and CAROTENOIDS
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Westermann M, Ernst A, Brass S, Boger P, Wehrmeyer W (1994). Ultrastructure
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and expression in Escherichia coli of the gene coding for phytoene
synthase from the cyanobacterium Synechocystis sp. PCC 6803. Biochim
Biophys Acta 1218:145-152
Mayer SM, Rieble S, Beale SI (1994). Metal requirements of the enzymes
catalyzing conversion of glutamate to ы-aminolevulinic acid in extracts
of Chlorella vulgaris and Synechocystis sp. PCC 6803. Arch Biochem
Biophys 312:203-209
Schreiber U (1994). New emitter-detector-cuvette assembly for measuring
modulated chlorophyll fluorescence of highly diluted suspensions in
conjunction with the standard PAM fluorometer. Z Naturforsch C 49:646-
656
ELECTRON TRANSPORT and BIOENERGETICS
Caffrey MS (1994). Strategies for the study of cytochrome c structure and
function by site-directed mutagenesis. Biochimie 76:622-630
Diaz A, Navarro F, Hervas M, Navarro JA, Chavez S, Florencio FJ, Delarosa MA
(1994). Cloning and correct expression in E. coli of the petJ gene
encoding cytochrome c6 from Synechocystis 6803. FEBS Lett 347:173-177
Malakhov MP, Wada H, Los DA, Semenenko VE, Murata N (1994). A new type of
cytochrome c from Synechocystis PCC 6803. J Plant Physiol 144:259-264
Mamedov MD (1994). Effect of thylakoid lipids on the activity of cytochrome
bf complex. Biochemistry-Engl Tr 59:625-627
Meyer TE, Tollin G, Cusanovich MA (1994). Protein interaction sites obtained
via sequence homology. The site of complexation of electron transfer
partners of cytochrome c revealed by mapping amino acid substitutions
onto three-dimensional protein surfaces. Biochimie 76:480-488
Ortega JM, Hervas M, Delarosa MA, Losada M (1994). Redox properties of
cytochrome b559 in photosynthetic membranes from the cyanobacterium
Synechocystis sp PCC 6803. J Plant Physiol 144:454-461
Peschek GA, Obinger C, Sherman DM, Sherman LA (1994). Immunocytochemical
localization of the cytochrome c oxidase in a cyanobacterium,
Synechococcus PCC 7942 (Anacystis nidulans). Biochim Biophys Acta
1187:369-372
Schmetterer G, Alge D, Gregor W (1994). Deletion of cytochrome c oxidase genes
from the cyanobacterium Synechocystis sp. PCC 6803: Evidence for
alternative respiratory pathways. Photosynth Res 42:43-50
Cartagena E, Bes MT, Gomez Moreno C, Peleato ML (1994). Purification and
characterization of ferredoxin-NADP+ reductase from the green alga
Chlorella fusca. Physiol Plant 91:645-650
Geerts D, Schubert H, Devrieze G, Borrias M, Matthijs HCP, Weisbeek PJ (1994).
Expression of Anabaena PCC 7937 plastocyanin in Synechococcus PCC 7942
enhances photosynthetic electron transfer and alters the electron
distribution between photosystem I and cytochrome c oxidase. J Biol Chem
269:28068-28075
Gomez Moreno C, Bes MT (1994). Structural requirements for the electron
transfer between a flavoprotein and viologens. Biochim Biophys Acta
1187:236-240
Gomez Moreno C, Medina M, Hurley JK, Cusanovich MA, Markley JL, Cheng H, Xia
B, Chae YK, Tollin G (1994). Protein engineering for the elucidation of
the mechanism of electron transfer in redox proteins. Biochem Soc Trans
22:796-800
Hurley JK, Medina M, Gomez Moreno C, Tollin G (1994). Further characterization
by site-directed mutagenesis of the protein-protein interface in the
ferredoxin/ferredoxin: NADP+ reductase system from Anabaena: Requirement
of a negative charge at position 94 in ferredoxin for rapid electron
transfer. Arch Biochem Biophys 312:480-486
Medina M, Gomez Moreno C, Cammack R (1994). ESR and ENDOR characterization of
flavodoxin from Anabaena sp. PCC 7119. Biochem Soc Trans 22:S371
Navarro JA, Hervas M, Pueyo JJ, Medina M, Gomezmoreno C, Delarosa MA, Tollin
G (1994). Laser flash-induced photoreduction of photosynthetic
ferredoxins and flavodoxin by 5-deazariboflavin and by a viologen
analogue. Photochem Photobiol 60:231-236
Poncelet M, Cassierchauvat C, Chauvat F (1994). Sequence of the flavodoxin-
encoding gene from the cyanobacterium Synechocystis PCC 6803. Gene
145:153-154
Razquin P, Schmitz S, Fillat MF, Peleato ML, Bohme H (1994). Transcriptional
and translational analysis of ferredoxin and flavodoxin under iron and
nitrogen stress in Anabaena sp. strain PCC 7120. J Bacteriol 176:7409-
7411
Vermaas WFJ (1994). Molecular-genetic approaches to study photosynthetic and
respiratory electron transport in thylakoids from cyanobacteria. Biochim
Biophys Acta 1187:181-186
Bakels RHA, Vanwalraven HS, Vanwielink JE, Vanderzwetdegraaff I, Krenn BE,
Krab K, Berden JA, Kraayenhof R (1994). The effect of sulfite on the ATP
hydrolysis and synthesis activity of membrane-bound H+-ATP synthase from
various species. Biochem Biophys Res Commun 201:487-492
Brown II, (1994). Is Ca2+ the third coupling ion? (Hypothesis). Biochem
(Moscow) 59:1321-1323
Kanamaru K, Kashiwagi S, Mizuno T (1994). A copper-transporting P-type ATPase
found in the thylakoid membrane of the cyanobacterium Synechococcus
species PCC 7942. Mol Microbiol 13:369-377
Moezelaar R, Stal LJ (1994). Fermentation in the unicellular cyanobacterium
Microcystis PCC 7806. Arch Microbiol 162:63-69
Phung LT, Ajlani G, Haselkorn R (1994). P-type ATPase from the cyanobacterium
Synechococcus 7942 related to the human Menkes and Wilson disease gene
products. Proc Natl Acad Sci USA 91:9651-9654
Sand O, Petersen IM, Jorgen J, Iversen L (1994). Purification and some
properties of glyceraldehyde 3-phosphate dehydrogenase from
Synechococcus sp. Anton Leeuwenhoek Int J Gen M 65:133-142
Steinemann D, Lill H, Junge W, Engelbrecht S (1994). Over-production,
renaturation and reconstitution of delta and epsilon subunits from
chloroplast and cyanobacterial F-1. Biochim Biophys Acta 1187:354-359
Wernergrune S, Gunkel D, Schumann J, Strotmann H (1994). Insertion of a
''chloroplast-like'' regulatory segment responsible for thiol modulation
into т-subunit of F0F1-ATPase of the cyanobacterium Synechocystis 6803
by mutagenesis of atpC. Mol Gen Genet 244:144-150
Vanderstaay GWM, Staehelin LA (1994). Biochemical characterization of protein
composition and protein phosphorylation patterns in stacked and
unstacked thylakoid membranes of the prochlorophyte Prochlorothrix
hollandica. J Biol Chem 269:24834-24844
MOLECULAR GENETICS, EPISOMES, AND METABOLISM OF MACROMOLECULES
Chemeresyuk NN, Elanskaya IV (1994). Cloning and Expression of Hordein B1-Gene
of Barley (Hordeum vulgare L.) in cyanobacterium Synechocystis sp.
PCC 6803 and Escherichia coli. Genetika 30:1141-1145
Sarma TA, Singh R (1994). Isolation and Characterization of Temperature-
Sensitive Mutants of Cyanophage-N-1. Acta Virol 38:11-16
Tsinoremas NF, Kutach AK, Strayer CA, Golden SS (1994). Efficient gene
transfer in Synechococcus sp. strains PCC 7942 and PCC 6301 by
interspecies conjugation and chromosomal recombination. J Bacteriol
176:6764-6768
Biniszkiewicz D, Cesnaviciene E, Shub DA (1994). Self-splicing group I intron
in cyanobacterial initiator methionine tRNA: Evidence for lateral
transfer of introns in bacteria. EMBO J 13:4629-4635
Fernandez-Piдas F, Wolk CP (1994). Expression of luxCD-E in Anabaena sp can
replace the use of exogenous aldehyde for in vivo localization of
transcription by luxAB. Gene 150:169-174
Houmard J (1994). Gene transcription in filamentous cyanobacteria.
Microbiology Uk 140(Part 3):433-441
Pascual A, Vioque A (1994). Sequence and structure of the RNA subunit of RNase
P from the cyanobacterium Pseudoanabaena sp. PCC 6903. Biochim Biophys
Acta 1218:463-465
Schyns G, Sobczyk A, Demarsac NT, Houmard J (1994). Specific initiation of
transcription at a cyanobacterial promoter with RNA polymerase purified
from Calothrix sp. PCC 7601. Mol Microbiol 13:887-896
Tan XL, Varughese M, Widger WR (1994). A light-repressed transcript found in
Synechococcus PCC 7002 is similar to a chloroplast-specific small
subunit ribosomal protein and to a transcription modulator protein
associated with х54. J Biol Chem 269:20905-20912
Soper BW, Reddy KJ (1994). Identification of a nuclease and host restriction-
modification in the unicellular, aerobic nitrogen-fixing cyanobacterium
Cyanothece sp. J Bacteriol 176:5565-5570
Yang XY, Daniel H, McFadden BA (1994). A facile method to study DNA synthesis
in the cyanobacterium Synechocystis PCC 6803. Curr Microbiol 29:171-175
Yang XY, Daniell H, McFadden B (1994). In vitro replication of cyanobacterial
plasmids from Synechocystis PCC 6803. Plasmid 32:195-207
Malakhov MP, Semenenko VE (1994). Codon usage in genes of cyanobacterium
Synechocystis PCC 6803. Russ J Plant Physiol 41:141-146 ([Engl])
Welsh PL, Johnson DR, Zhang YS, Breitenberger CA (1994). Synechocystis sp.
PCC 6803 fusB gene, located outside of the str operon, encodes a
polypeptide related to protein synthesis factor EF-G. Plant Mol Biol
25:735-738
Kim M, Choi YK (1994). A new Synechococcus cyanophage from a reservoir in
Korea. Virology 204:338-342
Koltukova NV, Kadyrova GK, Mendzhul MI, Muradov MM (1993). Effect of
Cyanophage A-1 Reproduction on Proteolysis in the Cells of Anabaena
variabilis. Microbiology-Engl Tr 62:627-629
Singh S, Bhatnagar A, Kashyap AK (1994). Energetics of cyanophage N-1
multiplication in the diazotrophic cyanobacterium Nostoc muscorum.
Microbios 78:259-265
APPLIED CYANOBACTERIOLOGY
Colwell FS, Pryfogle PA, Lee BD, Bishop CL (1994). Use of a cyanobacterium as
a particulate tracer for terrestrial subsurface applications. J
Microbiol Meth 20:93-101
Maquieira A, Elmahadi HAM, Puchades R (1994). Immobilized cyanobacteria for
on-line trace metal enrichment by flow injection atomic absorption
spectrometry. Anal Chem 66:3632-3638
Megharaj M, Madhavi DR, Sreenivasulu C, Umamaheswari A, Venkateswarlu K
(1994). Biodegradation of Methyl Parathion by Soil Isolates of
Microalgae and Cyanobacteria. Bull Environ Contam Toxicol 53:292-297
Swain N, Rath B, Adhikary SP (1994). Growth response of the cyanobacterium
Microcystis aeruginosa to herbicides and pesticides. J Basic Microbiol
34:197-204
Windhovel U, Geiges B, Sandmann G, Boger P (1994). Engineering Cyanobacterial
Models Resistant to Bleaching Herbicides. Pestic Biochem Physiol 49:63-
71
Hayashi O, Katoh T, Okuwaki Y (1994). Enhancement of antibody production in
mice by dietary Spirulina platensis. J Nutr Sci Vitaminol 40:431-441
Skulberg OM (1994). Oscillatorialean cyanoprokaryotes and their application
for algal culture technology. Arch Hydrobiol/Suppl 105, Algological
Studies 75:265-278
Alhasan RH, Sorkhoh NA, Albader D, Radwan SS (1994). Utilization of
hydrocarbons by cyanobacteria from microbial mats on oily coasts of the
Gulf. Appl Microbiol Biotechnol 41:615-619
Bockris JO, Bhardwaj RC, Tennakoon CLK (1994). Electrochemistry of waste
removal - A review. Analyst 119:781-789
Kuritz T, Wolk CP (1995). Use of filamentous cyanobacteria for biodegradation
of organic pollutants. Appl Environ Microbiol 61:234-238
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AUSTRALIA Steve Delaney Department of Biotechnology,
/NEW ZEALAND University of New South Wales, P.O.
Box 1, Kensington, New South Wales
AUSTRALIA 2033 (Tel) 02-697-2056
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Biologie, Humboldt-UniversitДt,
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INDIA Joe Thomas Biotechnology Division, SPIC Science
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600 032. (Tel) 432342 (Fax) 432163
ISRAEL Elisha Tel-Or Dept. of Agricultural Botany, The
Hebrew University, Rehovot 76100
(Tel) 08-481262
ITALY Mario Tredici Departimento di Scienze e Tecnologie
Alimentari e Microbiologiche.
Universita degli Studi di Firenze,
P.le.delle Cascine 27 51044 Firenze.
(Tel) 055-352051 (Fax) 055-330431
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Universiteit voor Amsterdam, Nieuwe
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(Tel) 31-20-525-7056
(Fax) 31-20-525-5802
(E-mail) A417LMur@Horus.Sara.NL
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Research, P.O.box 69 Korsvall, N-0808
Oslo 8 NORWAY. (Tel) 47 22 185266
(Fax) 47 22 185200
U.K. Tony Walsby Dept. of Botany, University of
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(Tel) 0272-303030
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International University, University
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(Tel) 305-348-3584, (Fax)305-348-1986
(E-mail) Cyano@Servax.Fiu.Edu