CYANONEWS
Volume 10 Number 2 July 1994
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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 - Look at the end of a news
item for a contact person. Also, 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:
* New Directory of Cyanobacteriologists available
* Toxin newsgroup reincarnated
* Asian molecular miology workshop advanced
* Meetings
* Monographs
* Positions available
TRANSITIONS
* Comings and goings of ourselves
* Passing of Akira Mitsui
NEWS:
* Mind of toxic Microcystis revealed
* N2-fixation by Trichodesmium regulated by light
* Nostoc immobilization boosts H2-evolution
REFERENCES
ADDRESSES
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BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD*BULLETIN BOARD*BU
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****** Matters Arising ******
A new edition of the DIRECTORY OF CYANOBACTERIOLOGISTS is now available.
The Directory lists more than 450 names, addresses, and research interests of
cyanobacteriologists. While not an exhaustive list, the Directory may be
useful in finding addresses for reprint requests or communicating with
colleagues. A geographical cross-reference is given at the end of the
Directory.
The Directory is currently available only in electronic form. Those who
access the newsletter electronically should have received separate
instructions describing how to obtain the Directory. Printed copies will be
distributed at the Photosynthetic Prokaryote meeting, Sept 1994, or by mail
to those not attending the meeting. To assure yourself of a copy,...
CONTACT: Jeff Elhai, Dept. of Biological Sciences, Florida
International University, Miami FL 33199, U.S.A. (Tel) 305-348-3584,
(Fax) 305-348-1986, (E-Mail) Cyano@Servax.Fiu.Edu
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A NEWSGROUP devoted to the discussion of all aspects of SECONDARY
METABOLITE PRODUCTS from cyanobacteria is on-line. This free computer
service bounces E-mail messages submitted by a correspondent automatically
to all subscribers, facilitating a global discussion of matters of
interest. To mark the new incarnation of this newsgroup, the name has been
changed from Cyan-Tox to CYANO-TOX -- old subscribers take note!
Subscribers to the old newsgroup will need to resubscribe.
To subscribe to the newsgroup, send an E-mail message to
Mailserv@Desire.Wright.Edu (don't fill in the subject heading), and give
the following command as the text of the message: SUBSCRIBE CYANO-TOX. You
will receive a welcome message describing how to make use of the newsgroup.
If you fail to receive such a message within a few days, contact Tony
Arment so that a real human being (Tony) can get your name by the bugs that
may afflict the new system.
CONTACT: Tony Arment, Dept. of Biological Sciences, Wright State
University, Dayton OH 45435, U.S.A. (Tel) 513-873-3173, (Fax) 513-
873-3301, (E-Mail) AArment@Desire.Wright.Edu
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Europe and North America both have their CYANOBACTERIAL MOLECULAR BIOLOGY
WORKSHOPS, serving as a means of bringing together graduate students and post-
docs as well as more senior workers in a cozy, informal setting. "WHY NOT
ASIA?" asks S. Shanmugasundaram. Few cyanobacteriologists in eastern Asia are
able to attend the major meetings of interest, even though their need for
communication and cooperative efforts is even more acute than that of their
North American and European colleagues. He suggests that Asian
cyanobacteriologists with a molecular bent would profit by a local meeting
that provides an opportunity for junior as well as senior scientists to
present their work, a forum in which to discuss the problems of practicing
molecular biology in developing countries, and the possibility of finding
creative, cooperative solutions to those problems. If you are interested in
seeing such a meeting come about then...
CONTACT: S. Shanmugasundaram, Department of Microbiology, School of
Biological Sciences, Madurai Kamaraj University, Madurai 625021,
INDIA, (Tel) 91-452-85691 or 91-452-85642, (Fax) 91-452-85205,
(E-Mail) bga%bic_mku@Imtech.ernet.in
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G. SUBRAMANIAN has brought to our attention a laboratory manual entitled
"Manual of Techniques in Cyanobacterial Research", edited by himself and
others. Although the manual was designed for training workshops, it may also
be useful as a compendium of techniques for the cyanobacteriological
laboratory. The manual includes descriptions of techniques for the
identification and isolation of marine cyanobacteria, ecological techniques,
and many protocols for physiological and biochemical measurements. Each
protocol is presented in a cookbook format, listing the principle of the
assay, the reagents required, and a step-by-step procedure. The manual may be
purchased for US $10 (or its equivalent) to cover the costs of production and
postage.
CONTACT: Scientist-In-Charge, National Facility for Marine
Cyanobacteria, Bharathidasan University, Palkalaiperur,
Tiruchirapalli 620 024, INDIA. (Tel) 91-431-896-352, (Fax) 91-31-
96245, (Telex) 0455-253 BARD.
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A 240-page monograph entitled "ALGAL TOXINS IN SEAFOOD AND DRINKING
WATER", edited by Ian Falconer, has recently been published by Academic
Press, Harcourt Brace & Company, Marrickville, Australia. Thevolume
provides information on the identification of toxic marine and fresh-water
algae, the routine analysis and effects of algal toxins, their veterinary
and public health impact, and control measures currently in use. Much of
the book focuses on cyanobacteria and their toxins.
****** Meetings ******
The 1st European NITROGEN FIXATION CONFERENCE is scheduled for 28
August to 3 September, 1994 in Szeged, Hungary.
CONTACT: Laszlo Dallmann, Biological Research Center, Hungarian
Academy of Sciences, Szeged, P.O. Box 521, H-6701, HUNGARY
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The VII International Symposium on PHOTOTROPHIC PROKARYOTES is still on
for 10-15 September 1994 in Urbino, Italy.
CONTACT: Organizing Secretariat of the VIII ISPP, S.Ventura,
CNR-CSMA, p.le delle Cascine 27, I-50144 Firenze, ITALY. (Tel) +39-
55-350542 or -352051, (Fax) +39-55-330431,
(E-mail) Ventura@csma.fi.cnr.it
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A unique conference, entitled Asian Regional Conference on ECOTECHNOLOGY
FOR SUSTAINABLE DEVELOPMENT will take place 19 through 26 Oct 1994, in
Beijing, P.R. China and, at the same time, throughout the world by computer
hookup. The conference will feature three days of field trips to sites that
demonstrate an integrated systems approach to sustainable development (for
those physically at the meeting). Papers will be available via E-mail.
CONTACT (Chinese Participants): Li Wenhua, President of Special
Committee for Sustainable Development, Chinese Society of Science and
Technology for Social Development, 19 Zhonguancun Road, Beijing
100080, PR China. (E-mail) LiWH@Bepc2.ihep.ac.cn
or CONTACT (all others): Eng-Leong Foo (Director). UNESCO Microbial
Resources Center, MTC-Karolinska Institute, S 171 77 Stockholm,
Sweden. (Tel) 08-728-7145, (Fax) 08-331547,
(E-mail) Eng-Leong.Foo@mtc.ki.se
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The International Symposium/Workshop on BIOLOGICAL NITROGEN FIXATION
ASSOCIATED WITH RICE is scheduled for 28 November to 2 December, 1994, in
Dhaka, Bangladesh. Some of the topics of the meeting include: (1) Azolla-
Anabaena associations, (2) free-living cyanobacteria in rice fields, and
(3) microflora associated with rice roots.
CONTACT: Mustafizur Rahman, Coordinaror, International
Symposium/Workshop on Biological Nitrogen Fixation Associated with
Rice. Post Bax GPO-4151, Dhaka-1000, Bangladesh. (Tel) 500191,
(Telex) 632345 IGR BJ, (Fax) 880-2-863476 or 880-2-863794.
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The Third European Workshop on the MOLECULAR BIOLOGY OF CYANOBACTERIA
will be held in Sevilla, Spain, in 1995. The tentative dates are 12-14 May
(Friday through Sunday). The first circular may be expected some time during
July, 1994.
CONTACT: Enrique Flores, Instituto de Bioqu¡mica Vegetal y
Fotos¡ntesis, Universidad de Sevilla-CSIC, Apartado 1113, 41080
Sevilla, SPAIN. (Tel) 34-5-455-70-86, (Fax) 34-5-462-0154,
(E-Mail) Flores@Cica.Es
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The 10th International Congress on NITROGEN FIXATION will be held 28 May
1995 to 3 June 1995 in St. Petersburg Russia.
CONTACT: Igor Tikhonovich, Congress Organizer, Research Institute for
Agricultural Microbiology, P.B. 364, General Post Office, 190000, St.
Petersburg, RUSSIA. (Fax) 812-470-43-62, (E-Mail) Chief@Riam.Spb.Su
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The Vth CYANOBACTERIAL MOLECULAR BIOLOGY WORKSHOP is now set for 21-25
July 1995 in Asilomar, California.
CONTACT: Don Bryant, S-231 Frear Bldg., Dept. of Biochemistry and
Molecular Biology, The Pennsylvania State University, University
Park, PA 16802, U.S.A. (Tel) 814-865-1992, (Fax) 814-863-7024,
(E-mail) Dab14@Psuvm.Bitnet or DAB14@Psuvm.Psu.Edu
or CONTACT: Neil Straus, Department of Botany, University of Toronto,
Toronto, Ontario, Canada M5S1A1. (Tel) 416-978-3532, (Fax) 416-978-
5878, (E-Mail) Straus@Botany.UToronto.Ca
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The Xth INTERNATIONAL PHOTOSYNTHESIS CONGRESS will take place in
Montpellier, France, 20-25 August 1995. The congress will cover all aspects
of photosynthesis, from photophysics to environmental aspects, in all
photosynthetic organisms, from bacteria to higher plants.
CONTACT: Paul Mathis, DBCM-SBE, CEA Saclay, Batiment 532, 91191
Gif-sur-Yvette CEDEX, France. (Fax) 33-1 69 08 87 17.
****** Positions Offered ******
POSITION OFFERED: Post-Doc
CONTACT: Bridgette Barry, Department of Biochemistry,
140 Gortner Lab., University of Minnesota, St. Paul
55108, U.S.A. (Fax) 612-625-5780,
(E-Mail) barry@molbio.cbs.umn.edu
RESEARCH: Difference infrared and EPR spectroscopies to study the mechanism
of electron transfer in photosystem II [MacDonald et al (1993) Proc Natl
Acad Sci USA 90:11024].
SUBMIT: CV and three letters of recommendation.
POSITION OFFERED: Post-Doc
CONTACT: Terry Bricker, Dept. of Botany, Louisiana State University, Baton
Rouge, LA 70803 U.S.A. (E-Mail) btbric%lsuvm.Bitnet@Uga.Cc.Uga.Edu
RESEARCH: Protein-protein interactions in Photosystem II [Frankel & Bricker
(1992) Biochem 31:11059]
REQUIREMENTS: Working knowledge of PAGE and HPLC, and should be interested in
learning techniques for protein modification and analysis.
SUPPORT: Initial salary of $20,000/year and may be extended through a second
year.
SUBMIT: CV, three letters of recommendation.
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POSITION OFFERED: Post-Doc
CONTACT: Toivo Kallas, Dept. of Biology and Microbiology, University of
Wisconsin-Oshkosh, Oshkosh WI 54901, U.S.A. (Tel) 414-424-7084,
(E-Mail) Kallas@Vaxa.Cis.UWOsh.Edu, (Fax) 414-424-1101,
RESEARCH: Overproduction, reconstitution with Fe-S centers and Rieske-depleted
cytochrome b6f complex, and structure/function analysis of mutant forms
of the Rieske Fe-S, electron transport protein. The project will involve
strong interinstitutional collaborations and the candidate would also
have the opportunity to gain teaching experience if he/she so desires.
REQUIREMENTS: Experience in molecular biology, protein chemistry, and/or EPR
spectroscopy is desirable.
SUPPORT: Approximately $22,500 yearly (11 month appointment) for two years.
SUBMIT: CV, brief description of interests, and the names, addresses, phone,
FAX, and E-Mail numbers of three references.
START: September 1, 1994 (or earlier). Please call for further information.
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POSITION OFFERED: Post-Doc or Technician
CONTACT: Shirley Raps, Dept. of Biological Sciences, Hunter College, 695
Park Ave., New York, NY 10021, U.S.A. (Tel) 212-772-5281,
(E-Mail) Raps@GeneCtr.Hunter.Cuny.Edu
RESEARCH: Characterizing genetic basis of toxin production in Microcystis.
Gene cloning and construction of shuttle vector.
REQUIREMENTS: Knowledge of cyanobacteria and molecular biology.
SUPPORT: Two years with possibility of a third.
START: immediately
SUBMIT: CV, two letters of recommendation
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POSITIONS OFFERED: Post-Doc
CONTACT: Constantin Rebeiz, Laboratory of Plant Pigment Biochemistry and
Photobiology, 240 A, PABL, 1201 West Gregory Ave., University of
Illinois, Urbana IL 61801, U.S.A. (Tel) 217-333-1968.
(E-Mail) Tino@Vmd.Cso.Uiuc.Edu
RESEARCH (Position #1): The development of a reconstituted cell-free system
capable of total chloroplast assembly. Beside monitoring the successful
assembly of a functional chloroplast in vitro, the research will involve
trapping and decoding messages produced by various constituents of the
reconstituted cell as they coordinate their efforts in bringing about
total chloroplast differentiation in vitro.
REQUIREMENTS (Position #1): Some expertise in one or more of the following
disciplines: (1) porphyrin biochemistry, (2) thylakoid protein
isolation, purification and characterization, (3) subcellular organelle
isolation, purification and characterization, (4) plant molecular
biological techniques and (5) biofiber techniques.
RESEARCH (Position #2): Cloning of gene encoding [4-vinyl]Chlorophyllide a
reductase (4VCR) [Biochem (1992) 31:8460-8464], important in chlorophyll
biosynthetic heterogeneity in plants.
REQUIREMENTS (Position #2): Some expertise in one or more of following:
(1) Porphyrin biochemistry, (2) Protein isolation, purification, and
characterization, (3) Plant molecular biology techniques.
START: Beginning Oct. 1, 1994
SEND: CV plus three letters of recommendation
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POSITION: Post-doc
CONTACT: Daniel Vaulot. (Tel) 33-98 29 23 34,
(E-Mail) Vaulot@univ-Rennes1.Fr, (Fax) 33-98 29 23 24.
LOCATION: CNRS, Station Biologique, Roscoff, France (Britanny).
RESEARCH: Molecular structure and regulation of the photosynthetic apparatus
of a recently discovered, marine procaryote (Prochlorococcus sp.). This
organism, now grown routinely in culture, plays a key role in the
photosynthetic production of the tropical oceans. Work will consists of
sequencing key photosynthetic genes and studying their regulation in
reponse to changes in light and nutrients. This work is also supported
by a 200.000 FF grant from the Centre National de la Recherche
Scientifique covering equipment and supplies.
REQUIREMENTS: Doctorate degree with experience in Molecular
Biology/Biochemistry applied to Photosynthetic organisms. Citizenship
from European Community or Associated State except France.
SUBMIT: CV with list of refereed publications (before August 1, 1995)
START: Early 1995
SUPPORT: 13.800 FF/month (EEC Human and Mobility Fellowship)
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POSITION: Research biochemist or molecular biologist specializing in
photosynthesis.
CONTACT: National Research Center Demokritos, Administrative Directorate,
Athens, Greece 15310. (Tel) 301-653-2649, (Fax) 301-651-2172
SUPPORT: Initial Level C appointments are for three years. After that staffer
are eligible for promotion to the tenured Level B.
SUBMIT: Full application plus supporting documents due not later than August
1994.
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TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANSITIONS*TRANS
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ULRICH FISCHER and J. RETHMEIER have moved from Universit„t Oldenburg to
Universit„t Bremen.
Universit„t Bremen, FB2, Marine Mikrobiologie, Postfach 33 04 40,
28334 Bremen, GERMANY
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NANCY FEDERSPIEL has departed from academia, leaving her position at
University of Idaho in favor of one in Silicon Valley.
Microcide Pharmaceuticals, 850 Maude Ave., Mountain View, CA 94043,
U.S.A. (Tel) 415-428-1550, (Fax) 415-428-3550,
(E-Mail) NFeder@Microcide.Com
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Akira Mitsui (1929-1994)
Akira Mitsui died of cancer related complications on May 31, 1994 in
Miami Florida. He will be missed by his friends and colleagues, both here in
Miami and around the world.
Mitsui was born in Shizuoka, Japan. He received his Ph.D. from Tokyo
University in 1958. Mitsui resided in Miami for 22 years and was a Professor
of Marine Biology and Fisheries at the Rosenstiel School of Marine and
Atmospheric Science at the University of Miami. He was also the Director of
both the International Research Center for Marine Bioscience and Technology,
and the International Research Center for Biological Hydrogen Production.
Mitsui's research focused on the biochemistry, bioenergetics, and
biotechnology of marine photosynthetic organisms. He collected and maintained
an extensive collection of marine cyanobacteria and photosynthetic bacteria.
The focus of his research included; hydrogen production for clean energy and
a clean environment, nitrogen fixation for fertilization and energy
conservation, aquaculture for a clean source of food and protein, food
additives and pharmaceuticals for a healthy society, and
chemicals and biochemicals for the development of useful materials. Mitsui was
a prolific author of research papers and reviews, and he served often as an
invited speaker at international conferences.
Mitsui spent his lifetime on research and the technological development
of a clean global environment and a healthy society. From his advisors at
Tokyo University, Hiroshi Tamiya, Atushi Watanabe, and Eijiro Yakushiji, he
learned his originality, his patience, and his joy of research. From these,
Akira developed his own missions and dreams, although he knew that his goals
were not those of a single generation. His hope was that the younger
generation could continue his efforts with their own ideas and technology.
Akira Mitsui was kind and generous, and he greatly enjoyed entertaining
friends and colleagues from around the world, attested to by the hundreds of
photographs that line the hallways of his research center. He was an
outstanding scientist, father, and person, who was always patient and
thoughtful. Throughout his lifetime he was a great influence on many students
and colleagues. He will be fondly remembered by all who knew him.
-- Catherine Campbell
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NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NEWS*NE
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Immobilization by Titanium Dioxide Increases Hydrogen Evolution:
A Tribute to Alexander Krasnovsky
While laboratory strains of cyanobacteriology are often prized for their
abilities to grow uniformly in culture, wild cyanobacteria frequently grow
adhered to surfaces or to themselves. Immobilization of cyanobacteria,
typically in artificial matrices, has been studied by several groups, hoping
to exploit the stability and other characteristics of the system for
biotechnological applications. OLGA BEKASOVA now tells us that the
polyurethane foams, calcium alginate beads, and other often used supports have
a simple alternative: the addition to the medium of 4g/l titanium dioxide
(TiO2), followed by intensive bubbling with air enriched in CO2.
Bekasova's work in the laboratory of Alexander Krasnovsky (see below)
demonstrated that Nostoc muscorum immobilized in this fashion have swollen
mucilaginous capsules, resulting in the increase of the filament thickness
from 4 to 12 æm, an altered ratio of photosynthetic pigments, and achange in
the efficiency of excitation energy migration. Specifically, energy migration
increased between phycobilins and decreased between phycobilisomes and
chlorophylls.
Of particular note was the effect of immmobilization by TiO2 on hydrogen
evolution under anaerobic conditions. In media lacking an exogenous electron
donor, H2 was produced by immobilized cells only in darkness, in contrast to
H2-production by free-living cells, which required light. With an exogenous
electron donor, methyl viologen reduced by dithionite, the rate of H2 evolution
was three orders of magnitude higher in immobilized cells than in free-living
cells. Thus, immobilization of cyanobacteria by TiO2 influences both carbon and
hydrogen metabolism.
A full account of this work has been published [Biokhim (1993)
58:1587-1593; Russ J of Plant Physiol (1993) 40:717-722 (Russ), 40:835-840
(Engl)]. Olga brought it to our attention in honor of Alexander Krasnovsky,
a pioneer in the field of photosynthesis, who died May 16, 1993. She has also
published a retrospective of work in Krasnovsky's laboratory concerning the
biochemistry and biophysics of phycobilisomes [Biofizika (1993) 38:1003-1024]
in an issue devoted to his memory.
Olga Bekasova, Bakh Institute of Biochemistry, Russian Academy of
Sciences, Leninskii pr. 33, Moscow, 117071 Russia.
(E-Mail) Inbio@Glas.Apc.Org
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Why Does Microcystis Make Toxins?
Cyanobacteria produce a variety of toxins, to the great torment of
livestock and occasionally humans as well. Amongst the most intensively
studied of the cyanobacterial toxins are the protein phosphatase inhibitors,
typified by microcystin-LR, a toxin produced by Microcystis aeruginosa. These
toxins wreak havoc within mammals, destroying their livers and accelerating
tumor formation. The ill effects of these toxins are largely attributable to
the inhibition of two of the major protein phosphatases in mammals, PP1 and
PP2A [Runnegar MT et al (1993) Am J Physiol 265:G224-G230], with the latter
binding more stably to the toxins [Toivola DM et al (1994) FEBS Lett
344:175-180]. The liver damage induced by microcystin-LR is due to marked
cytoskeletal alterations which [Eriksson JE et al (1990) Biochem Biophys Res
Comm 173:1347-1353], interestingly, indicates that a continuous fine-tuning
of phosphatases and kinases is required to maintain cytoskeletal integrity
[Eriksson JE et al (1992) Proc Natl Acad Sci USA 89:11093-11097]. A second
class of cyanobacterial toxins, typified by lyngbyatoxin A (also called
teleocidin), acts on the other side of the biochemical equation: increasing
protein phosphorylation by the activation of a specific protein kinase
[Kozikowski AP et al (1991) J Med Chem 34:2420-2430].
The question remains: why should cyanobacteria be so interested in
making us sick? JEN YUN SHEEN has recently reported [Sheen J (1993) EMBO J
12:3487-3505] what may be an important part of the answer. She found that
okadaic acid, a compound with similar inhibitory action as microcystin-LR,
blocks the activity of protein phosphatases in maize and inhibits the
light-dependent expression of rbcSZm1 (encoding a subunit of rubisco) and
C4ppdkZm1 (encoding pyruvate phosphate dikinase). Okadaic acid also inhibits
the greening of etiolated leaves in response to light, explicable if active
protein phosphatase is required in general for the proper response of
light-regulated genes.
Microcystin-LR, even more potently than okadaic acid, inhibits plant
protein phosphatases [MacKintosh C et al (1990) FEBS Lett 264:187-192],
suggesting the possibility that the class of cyanobacterial toxins it
represents interferes with the normal response of plants to light. Indeed,
toxin production by Microcystis rises with light intensity, well beyond the
overall increase in protein synthesis [Utkilen H & Gjolme N (1992) Appl
Environ Microbiol 58:1321-1325]. Although microcystins may affect zooplankton
[Carmichael WW (1994) Sci Am 270(1):78-86] and mosquitos [Kiviranta J (1992)
Acta Pharm Fenn 101:105-109], predators of cyanobacteria, it is tempting to
speculate that the toxins may serve cyanobacteria by subverting the ability
of their algal competitors to adapt to higher light intensities.
And so we may be innocent bystanders, caught up in the crossfire between
algal belligerents, a fitting retribution for the devastation we ourselves
heap upon plants as a byproduct of OUR wars.
Jen Yun Sheen, Department of Molecular Biology, Wellman 11,
Massachusetts General Hospital, Boston, MA 02114 USA.
(E-Mail) Sheen@Frodo.Mgh.Harvard.Edu
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Nitrogenase Expression in Trichomes of Trichodesmium (Revisited)
In the last issue of CyanoNews (Vol. 10, No. 1), the possibility was
raised that Trichodesmium may be able to maintain nitrogen fixation against
saturating levels of O2 in seawater by limiting nitrogenase activity to a
specialized zone of cells central to the trichome. KAORI OHKI was moved to
describe results from her own laboratory that do not fit well with this view.
She and coworkers use a strain of Trichodesmium (Trichodesmium sp.
NIBB1067) isolated from Kuroshio Waters off Japan Island and kept in the lab
since 1983. They have found that colony formation is not necessary for N2
fixation by Trichodesmium. Indeed, the highest nitrogen-fixation activity is
observed in the exponential growth phase, when trichomes are separated from
one another [Ohki & Fujita (1988) Mar Biol 98:111-114]. Immunoelectron
microscopic images using antibodies raised against the Fe-protein of
nitrogenase show that almost all cells in the exponential growth phase
synthesize nitrogenase. The group also found that in Trichodesmium the three
genes (nifHDK) encoding nitrogenase are contiguous regardless of nitrogen
source [Zehr et al (1991) J Bacteriol 173:7059-7062], unlike the case of
heterocystous cyanobacteria, where nifD is interrupted in vegetative cells but
not in heterocysts. These results have convinced Ohki's group that
Trichodesmium does not develop cells specialized for N2-fixation.
How then does Trichodesmium protect nitrogenase against poisoning by O2?
One clue may lie in the observation that Trichodesmium requires light to
maintain nitrogenase activity. Activity was completely lost when cells were
incubated in the dark for 3 to 5 hrs, and illumination for more than 1 hr was
needed for reactivation, a process requiring protein synthesis. During dark
incubation, the Fe-protein of nitrogenase increases its apparent molecular
mass on SDS-PAGE, while during reactivation in the light, the apparent
molecular mass decreases [Ohki & Fujita (1992) In: Progress in Photosynthesis,
p.103; Zehr et al. (1992) J Gen Microbiol 138:2679-2685].
To explain the maintenance of nitrogenase activity in Trichodesmium,
Ohki and coworkers postulate that: (1) light is necessary not only for
supplying ATP and/or reducing power to N2-fixation but also for maintaining
nitrogenase in an active form, and (2) activation of nitrogenase that has been
inactivated by photosynthetically produced O2 may be achieved by a light-
dependent activating process.
Kaori Ohki, Department of Marine Science, School of Marine Science and
Technology, Tokai University, Shimizu, Shizuoka 424, JAPAN. (Fax) 81-
434-34-5096.
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****** EVOLUTION, SYSTEMATICS, and PROCHLOROPHYTES ******
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****** TOXINS and NATURAL SUBSTANCES (Physiological Effects) ******
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****** PHYSIOLOGY and METABOLISM ******
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****** STRESS RESPONSES ******
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****** NITROGEN METABOLISM ******
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****** NITROGENASE and HYDROGENASE ******
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****** DIFFERENTIATION ******
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****** CARBON METABOLISM ******
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Fuchs B, Suttner P, Sterner S, Wastlhuber R, Loos E (1994). Disproportionating
transglycosylase (D-enzyme) in green algae and cyanobacteria. Partial
purification and characterization. Z Naturforsch C 49:163-170.
Marco E, Martinez I, Ronentarazi M, Orus MI, Kaplan A (1994). Inactivation of
ccmO in Synechococcus sp Strain PCC 7942 Results in a Mutant Requiring
High Levels of CO2. Appl Environ Microbiol 60:1018-1020.
Ogawa T, Amichay D, Gurevitz M (1994). Isolation and Characterization of the
ccmM Gene Required by the Cyanobacterium Synechocystis PCC6803 for
Inorganic Carbon Utilization. Photosynth Res 39:183-190.
Ogawa T, Marco E, Orus MI (1994). A Gene (ccmA) Required for Carboxysome
Formation in the Cyanobacterium Synechocystis sp Strain PCC 6803. J
Bacteriol 176:2374-2378.
Palmqvist K, Ogren E, Lernmark U (1994). The CO2-Concentrating Mechanism Is
Absent in the Green Alga Coccomyxa - A Comparative Study of
Photosynthetic CO2 and Light Responses of Coccomyxa, Chlamydomonas
reinhardtii and Barley Protoplasts. Plant Cell Environ 17:65-72.
Palmqvist K, Yu JW, Badger MR (1994). Carbonic Anhydrase Activity and
Inorganic Carbon Fluxes in Low-CI and High-CI Cells of Chlamydomonas
reinhardtii and Scenedesmus obliquus. Physiol Plant 90:537-547.
Raven JA, Newman JR (1994). Requirement for Carbonic Anhydrase Activity in
Processes Other Than Photosynthetic Inorganic Carbon Assimilation. Plant
Cell Environ 17:123-130.
Williams TG, Colman B (1994). Rapid Separation of Carbonic Anhydrase Isozymes
Using Cellulose Acetate Membrane Electrophoresis. J Exp Bot 45:153-158.
Yu JW, Price GD, Badger MR (1994). Characterisation of CO2 and HCO3- Uptake
During Steady-State Photosynthesis in the Cyanobacterium Synechococcus
PCC 7942. Aust J Plant Physiol 21:185-195.
Yu LW, Price GD, Badger MR (1994). A Mutant Isolated from the Cyanobacterium
Synechococcus PCC 7942 Is Unable to Adapt to Low Inorganic Carbon
Conditions. Plant Physiol 104:605-611.
****** PHOTOSYNTHESIS ******
Arieli B, Shahak Y, Taglicht D, Hauska G, Padan E (1994). Purification and
Characterization of Sulfide-Quinone Reductase, a Novel Enzyme Driving
Anoxygenic Photosynthesis in Oscillatoria Limnetica. J Biol Chem
269:5705-5711.
Bader KP, Hoper S (1994). Stimulatory Effects of an Ammonium Salt Biocide on
Photosynthetic Electron Transport Reactions. Z Naturforsch C 49:87-94.
Boekema EJ, Boonstra AF, Dekker JP, Rogner M (1994). Electron Microscopic
Structural Analysis of Photosystem I, Photosystem II, and the
Cytochrome b6/f Complex from Green Plants and Cyanobacteria. J Bioenerg
Biomembrane 26:17-29.
Huzisige H, Ke B (1993). Dynamics of the History of Photosynthesis Research.
Photosynth Res 38:185-209.
Laible PD, Zipfel W, Owens TG (1994). Excited State Dynamics in
Chlorophyll-Based Antennae - The Role of Transfer Equilibrium. Biophys
J 66:844-860.
Muller C, Reuter W, Wehrmeyer W, Dau H, Senger H (1993). Adaptation of the
Photosynthetic Apparatus of Anacystis nidulans to Irradiance and
CO2-Concentration. Bot Acta 106:480-487.
Mullineaux CW (1993). Inhibition by Phosphate of Light-State Transitions in
Cyanobacterial Cells. Photosynth Res 38:135-140.
Schmid GH, Bader KP, Schulder R (1994). A Study on the Life Time of the
S-3-State in the Filamentous Cyanobacterium Oscillatoria Chalybea. Z
Naturforsch C 49:108-114.
Shen GZ, Vermaas WFJ (1994). Chlorophyll in a Synechocystis sp. PCC 6803
mutant without photosystem I and photosystem II core complexes -
Evidence for peripheral antenna chlorophylls in cyanobacteria. J Biol
Chem 269:13904-13910.
Trinkunas G, Holzwarth AR (1994). Kinetic Modeling of Exciton Migration in
Photosynthetic Systems. 2. Simulations of Excitation Dynamics in
Two-Dimensional Photosystem Core Antenna/Reaction Center Complexes.
Biophys J 66:415-429.
Vermaas WFJ, Shen GZ, Styring S (1994). Electrons Generated by Photosystem II
Are Utilized by an Oxidase in the Absence of Photosystem I in the
Cyanobacterium Synechocystis sp PCC 6803. FEBS Lett 337:103-108.
****** PHOTOSYSTEM I ******
Chitnis VP, Chitnis PR (1993). PsaL Subunit is Required for the Formation of
Photosystem I Trimers in the Cyanobacterium Synechocystis sp. PCC 6803.
FEBS Lett 336:330-334.
Falzone CJ, Kao YH, Zhao JD, Bryant DA, Lecomte JTJ (1994). Three-dimensional
solution structure of PsaE from the cyanobacterium Synechococcus sp.
strain PCC 7002, a photosystem I protein that shows structural homology
with SH3 domains. Biochemistry 33:6052-6062.
Falzone CJ, Kao YH, Zhao JD, MacLaughlin KL, Bryant DA, Lecomte JTJ (1994).
H-1 and N-15 NMR assignments of PsaE, a photosystem I subunit from the
cyanobacterium Synechococcus sp. strain PCC 7002. Biochemistry
33:6043-6051.
Hastings G, Kleinherenbrink FAM, Lin S, Blankenship RE (1994). Time-Resolved
Fluorescence and Absorption Spectroscopy of Photosystem I. Biochemistry
33:3185-3192.
Herman PL, Adiwilaga K, Golbeck JH, Weeks DP (1994). Sequence of a psaC Gene
from the Cyanobacterium Synechococcus sp PCC 6301. Plant Physiol
104:1459-1461.
Luneberg J, Fromme P, Jekow P, Schlodder E (1994). Spectroscopic
Characterization of PS I Core Complexes from Thermophilic Synechococcus
sp - Identical Reoxidation Kinetics of A(1)(-) Before and After Removal
of the Iron-Sulfur-Clusters FA and FB. FEBS Lett 338:197-202.
Mi H, Endo T, Schreiber U, Ogawa T, Asada K (1994). NAD(P)H
Dehydrogenase-Dependent Cyclic Electron Flow Around Photosystem I in the
Cyanobacterium Synechocystis PCC 6803 - A Study of Dark-Starved Cells
and Spheroplasts. Plant Cell Physiol 35:163-173.
Nyhus KJ, Sonoike K, Pakrasi HB (1994). Nucleotide sequences of the psaA and
the psaB genes encoding the reaction center proteins of Photosystem I
in Anabaena variabilis ATCC 29423. BBA-Bioenergetics 1185:247-251.
Odom WR, Hodges R, Chitnis PR, Guikema JA (1993). Characterization of
Synechocystis sp. PCC 6803 in Iron-Supplied and Iron-Deficient Media.
Plant Mol Biol 23:1255-1264.
Tziatzios C, Schuck P, Schubert D, Tsiotis G (1994). The molar mass of an
active photosystem I complex from the cyanobacterium Synechococcus
PCC 7002. Z Naturforsch C 49:220-222.
Xu QA, Yu LA, Chitnis VP, Chitnis PR (1994). Function and Organization of
Photosystem I in a Cyanobacterial Mutant Strain That Lacks PsaF and PsaJ
Subunits. J Biol Chem 269:3205-3211.
****** PHOTOSYSTEM II ******
Bader KP, Renger G, Schmid GH (1993). A Mass Spectrometric Analysis of the
Water-Splitting Reaction. Photosynth Res 38:355-361.
Bisen PS, Shanthy S (1993). Characterization of a DCMU-Resistant Mutant of the
Filamentous, Diazotrophic Cyanobacterium Anabaena doliolum. J Plant
Physiol 142:557-563.
Boerner RJ, Barry BA (1994). EPR Evidence That the M(+) Radical, Which Is
Observed in 3 Site-Directed Mutants of Photosystem II, Is a Tyrosine
Radical. J Biol Chem 269:134-137.
Bowlby NR, Espe M, Bhatnagar R, Wang J, Hoganson C, McIntosh L, Babcock G
(1993). Analytical Procedures for the Quantification of Isotopic Amino
Acid Incorporation into Photosynthetic Proteins of Synechocystis
PCC 6803. Photosynth Res 38:379-386.
Chu HA, Nguyen AP, Debus RJ (1994). Site-directed photosystem II mutants with
perturbed oxygen-evolving properties. 2. Increased binding or
photooxidation of manganese in the absence of the extrinsic 33-kDa
polypeptide in vivo. Biochemistry 33:6150-6157.
Chu HA, Nguyen AP, Debus RJ (1994). Site-directed photosystem II mutants with
perturbed oxygen-evolving properties. 1. Instability or inefficient
assembly of the manganese cluster in vivo. Biochemistry 33:6137-6149.
Etienne AL, Kirilovsky D (1993). The Primary Structure of D1 Near the QB
Pocket Influences Oxygen Evolution. Photosynth Res 38:387-394.
Kanervo E, Maenpaa P, Aro EM (1993). D1 Protein Degradation and psbA
Transcript Levels in Synechocystis PCC 6803 During Photoinhibition
Invivo. J Plant Physiol 142:669-675.
Kirilovsky D, Rutherford AW, Etienne AL (1994). Influence of DCMU and
Ferricyanide on Photodamage in Photosystem II. Biochemistry
33:3087-3095.
Kruse O, Radunz A, Schmid GH (1994). Phosphatidylglycerol and beta-Carotene
Bound Onto the D1-Core Peptide of Photosystem II in the Filamentous
Cyanobacterium Oscillatoria chalybea. Z Naturforsch C 49:115-124.
Kulkarni RD, Golden SS (1994). Adaptation to High Light Intensity in
Synechococcus sp Strain PCC 7942 - Regulation of Three psbA Genes and
Two Forms of the D1 Protein. J Bacteriol 176:959-965.
Leonhardt K, Straus NA (1994). Photosystem II Genes isiA, psbDI and psbC in
Anabaena sp PCC 7120 - Cloning, Sequencing and the Transcriptional
Regulation in Iron-Stressed and Iron-Repleted Cells. Plant Mol Biol
24:63-73.
MacDonald GM, Boerner RJ, Everly RM, Cramer WA, Debus RJ, Barry BA (1994).
Comparison of Cytochrome b559 Content in Photosytem-II Complexes from
Spinach and Synechocystis Species PCC 6803. Biochemistry 33:4393-4400.
Misra HS, Desai TS (1993). Involvement of Acceptor Side Components of PSII in
the Regulatory Mechanism of Plectonema boryanum Grown
Photoautotrophically Under Diazotrophic Condition. Biochem Biophys Res
Commun 194:1001-1007.
Mullineaux CW, Holzwarth AR (1993). Effect of Photosystem II Reaction Centre
Closure on Fluorescence Decay Kinetics in a Cyanobacterium. Biochim
Biophys Acta 1183:345-351.
Perewoska I, Etienne AL, Miranda T, Kirilovsky D (1994). S-1 Destabilization
and Higher Sensitivity to Light in Metribuzin-Resistant Mutants. Plant
Physiol 104:235-245.
Picorel R, Williamson DL, Yruela I, Seibert M (1994). The State of Iron in the
Oxygen-Evolving Core Complex of the Cyanobacterium Phormidium laminosum
- Mossbauer Spectroscopy. BBA-Bioenergetics 1184:171-177.
Ruff M, Pistorius EK (1993). Isolation and partial characterization of a
manganese and chloride binding protein present in highly purified
photoystem II complexes of the thermophilic cyanobacterium Synechococcus
sp.: The protein being detected by its L-arginine metabolizing activity.
Z Naturforsch 49c:95-107.
Satoh K, Katoh S, Donner A, Oettmeier W (1994). Binding Affinities of Oxidized
and Reduced Forms of Tetrahalogenated Benzoquinones to the QB Site in
Oxygen-Evolving Photosystem II Particles from Synechococcus elongatus.
Plant Cell Physiol 35:461-468.
Shen GZ, Boussiba S, Vermaas WFJ (1993). Synechocystis sp PCC 6803 Strains
Lacking Photosystem I and Phycobilisome Function. Plant Cell
5:1853-1863.
Smart LB, Bowlby NR, Anderson SL, Sithole I, McIntosh L (1994). Genetic
Manipulation of the Cyanobacterium Synechocystis sp PCC 6803 -
Development of Strains Lacking Photosystem I for the Analysis of
Mutations in Photosystem II. Plant Physiol 104:349-354.
Stamatakis C, Papageorgiou GC (1993). Stabilization of Photosystem II
Particles Isolated from the Thermophilic Cyanobacterium Phormidium
laminosum with Glycinebetaine and Glycerol. Biochim Biophys Acta
1183:333-338.
Tang XS, Diner BA (1994). Biochemical and Spectroscopic Characterization of
a New Oxygen-Evolving Photosystem II Core Complex from the
Cyanobacterium Synechocystis PCC 6803. Biochemistry 33:4594-4603.
Taoka S, Jursinic PA, Seibert M (1993). Slow Oxygen Release on the First Two
Flashes in Chemically Stressed Photosystem II Membrane Fragments Results
from Hydrogen Peroxide Oxidation. Photosynth Res 38:425-431.
Tiwari S, Mohanty P (1993). Cobalt Chloride Induced Stimulation of
Photosystem II Electron Transport in Synechocystis sp PCC 6803 Cells.
Photosynth Res 38:463-469.
Vermaas W, Vass I, Eggers B, Styring S (1994). Mutation of a Putative Ligand
to the Non-Heme Iron in Photosystem II - Implications for QA Reactivity,
Electron Transfer, and Herbicide Binding. BBA-Bioenergetics
1184:263-272.
Vermaas WFJ, Styring S, Schroder WP, Andersson B (1993). Photosynthetic Water
Oxidation - The Protein Framework. Photosynth Res 38:249-263.
Zhang ZH, Mayes SR, Vass I, Nagy L, Barber J (1993). Characterization of the
psbK Locus of Synechocystis sp PCC 6803 in Terms of Photosystem II
Function. Photosynth Res 38:369-377.
****** PHYCOBILISOMES and CAROTENOIDS ******
Bekasova OD (1993). Biochemistry of Phycobilisomes [Russ.]. Biofizika
38:1003-1024.
Bhalerao RP, Gustafsson P (1994). Factors Influencing the Phycobilisome Rod
Composition of the Cyanobacterium Synechococcus sp PCC 7942 - Effects
of Reduced Phycocyanin Content, Lack of Rod-Linkers, and over-Expression
of the Rod-Terminating Linker. Physiol Plant 90:187-197.
Collier JL, Grossman AR (1994). A Small Polypeptide Triggers Complete
Degradation of Light-Harvesting Phycobiliproteins in Nutrient-Deprived
Cyanobacteria. EMBO J 13:1039-1047.
Ducret A, Sidler W, Frank G, Zuber H (1994). The Complete Amino Acid Sequence
of R-Phycocyanin-I alpha and beta Subunits from the Red Alga
Porphyridium Cruentum -Structural and Phylogenetic Relationships of the
Phycocyanins Within the Phycobiliprotein Families. Eur J Biochem
221:563-580.
MacColl R, Williams EC, Eisele LE, McNaughton P (1994). Chromophore topography
and exciton splitting in phycocyanin 645. Biochemistry 33:6418-6423.
Mullineaux CW (1994). Excitation Energy Transfer from Phycobilisomes to
Photosystem I in a Cyanobacterial Mutant Lacking Photosystem II.
BBA-Bioenergetics 1184:71-77.
Newman J, Mann NH, Carr NG (1994). Organization and Transcription of the
Class I Phycoerythrin Genes of the Marine Cyanobacterium Synechococcus
sp WH7803. Plant Mol Biol 24:679-683.
Parker W, Goebel P, Ross CR, Song PS, Stezowski JJ (1994). Molecular Modeling
of Phytochrome Using Constitutive C-Phycocyanin from Fremyella
diplosiphon as a Putative Structural Template. Bioconjugate Chemistry
5:21-30.
Redecker D, Wehrmeyer W, Reuter W (1993). Core Substructure of the
Hemiellipsoidal Phycobilisome from the Red Alga Porphyridium Cruentum.
Eur J Cell Biol 62:442-450.
Reuter W, Westermann M, Brass S, Ernst A, Boger P, Wehrmeyer W (1994).
Structure, Composition, and Assembly of Paracrystalline
Phycobiliproteins in Synechocystis sp Strain BO 8402 and of
Phycobilisomes in the Derivative Strain BO 9201. J Bacteriol
176:896-904.
Biswal B, Smith AJ, Rogers LJ (1994). Changes in Carotenoids But Not in D1
Protein in Response to Nitrogen Depletion and Recovery in a
Cyanobacterium. FEMS Microbiol Lett 116:341-347.
Jones MC, Jenkins JM, Smith AG, Howe CJ (1994). Cloning and Characterisation
of Genes for Tetrapyrrole Biosynthesis from the Cyanobacterium Anacystis
nidulans R2. Plant Mol Biol 24:435-448.
Linden H, Misawa N, Saito T, Sandmann G (1994). A Novel Carotenoid
Biosynthesis Gene Coding for zeta-Carotene Desaturase - Functional
Expression, Sequence and Phylogenetic Origin. Plant Mol Biol 24:369-379.
Martinez-Ferez I, Vioque A, Sandmann G (1994). Mutagenesis of an Amino Acid
Responsible in Phytoene Desaturase from Synechocystis for Binding of the
Bleaching Herbicide Norflurazon. Pestic Biochem Physiol 48:185-190.
Windhovel U, Geiges B, Sandmann G, Boger P (1994). Expression of Erwinia
uredovora Phytoene Desaturase in Synechococcus PCC 7942 Leading to
Resistance Against a Bleaching Herbicide. Plant Physiol 104:119-125.
****** ELECTRON TRANSPORT and BIOENERGETICS ******
Alge D, Schmetterer G, Peschek GA (1994). The Gene Encoding Cytochrome c
Oxidase Subunit I from Synechocystis PCC6803. Gene 138:127-132.
Kang C, Chitnis PR, Smith S, Krogmann DW (1994). Cloning and sequence analysis
of the gene encoding the low potential cytochrome c of Synechocystis
PCC 6803. FEBS Lett 344:5-9.
Manasse RS, Bendall DS (1993). Characteristics of Cyclic Electron Transport
in the Cyanobacterium Phormidium laminosum. Biochim Biophys Acta
1183:361-368.
Martens N, Hall EAH (1994). Diaminodurene as a Mediator of a Photocurrent
Using Intact Cells of Cyanobacteria. Photochem Photobiol 59:91-98.
Sone N, Tano H, Ishizuka M (1994). The genes in the thermophilic
cyanobacterium Synechococcus vulcanus encoding cytochrome c oxidase.
BBA-Bioenergetics 1185:255 (correction of 1183:130).
Chae YK, Abildgaard F, Mooberry ES, Markley JL (1994). Multinuclear,
Multidimensional NMR Studies of Anabaena 7120 Heterocyst Ferredoxin -
Sequence-Specific Resonance Assignments and Secondary Structure of the
Oxidized Form in Solution. Biochemistry 33:3287-3295.
Cheng H, Xia B, Reed GH, Markley JL (1994). Optical, EPR, and H-1 NMR
Spectroscopy of Serine-Ligated [2Fe-2S] Ferredoxins Produced by
Site-Directed Mutagenesis of Cysteine Residues in Recombinant Anabaena
7120 Vegetative Ferredoxins. Biochemistry 33:3155-3164.
Ghassemian M, Wong B, Ferreira F, Markley JL, Straus NA (1994). Cloning,
sequencing and transcriptional studies of the genes for cytochrome c555
and plastocyanin from Anabaena sp. PCC 7120. Microbiology-Uk
140:1151-1159.
Gisselmann G, Klausmeier P, Schwenn JD (1993). The Ferredoxin - Sulphite
Reductase Gene from Synechococcus PCC 7942. Biochim Biophys Acta
1144:102-106.
Hervas M, Ortega JM, Navarro JA, Delarosa MA, Bottin H (1994). Laser Flash
Kinetic Analysis of Synechocystis PCC 6803 Cytochrome c6 and
Plastocyanin Oxidation by Photosystem I. BBA-Bioenergetics 1184:235-241.
Ho KK, Tan S (1994). Use of Adsorption Chromatography on Sephacryl S-500 for
Improved Separation of Isoforms of Soluble Photosynthetic Catalysts from
Cyanobacteria. J Liq Chromatogr 17:833-845.
Holden HM, Jacobson BL, Hurley JK, Tollin G, Oh BH, Skjeldal L, Chae YK, Cheng
H, Xia B, Markley J (1994). Structure-Function Studies of [2Fe-2S]
Ferredoxins. J Bioenerg Biomembrane 26:67-88.
Jelesarov I, Depascalis AR, Koppenol WH, Hirasawa M, Knaff DB, Bosshard H
(1993). Ferredoxin Binding Site on Ferredoxin:NADP(+) Reductase -
Differential Chemical Modification of Free and Ferredoxin-Bound Enzyme.
Eur J Biochem 216:57-66.
Karplus PA, Bruns CM (1994). Structure-Function Relations for Ferredoxin
Reductase. J Bioenerg Biomembrane 26:89-99.
Lelong C, Setif P, Lagoutte B, Bottin H (1994). Identification of the Amino
Acids Involved in the Functional Interaction Between Photosystem I and
Ferredoxin from Synechocystis sp PCC 6803 by Chemical Cross-Linking. J
Biol Chem 269:10034-10039.
Schrautemeier B, Cassing A, Bohme H (1994). Characterization of the Genome
Region Encoding an Fdxh-Type Ferredoxin and a New 2[4Fe-4S] Ferredoxin
from the Nonheterocystous, Nitrogen-Fixing Cyanobacterium Plectonema
boryanum PCC 73110. J Bacteriol 176:1037-1046.
Zhang LL, Pakrasi HB, Whitmarsh J (1994). Photoautotrophic Growth of the
Cyanobacterium Synechocystis sp PCC 6803 in the Absence of Cytochrome
c553 and Plastocyanin. J Biol Chem 269:5036-5042.
Dubinin AV, Gerasimenko LM (1993). Dark Anaerobic Metabolism of Halophilic
Cyanobacterium Microcoleus chtonoplastes. Microbiology-Engl Tr
62:391-394.
Lill H, Steinemann D, Nelson N (1994). Mutagenesis of the B'-Subunit of
Synechocystis sp PCC 6803 ATP-Synthase. BBA-Bioenergetics 1184:284-290.
Neisser A, Fromwald S, Schmatzberger A, Peschek GA (1994). Immunological and
Functional Localization of Both F-Type and P-Type ATPases in
Cyanobacterial Plasma Membranes. Biochem Biophys Res Commun 200:884-892.
Vanwalraven HS, Lutter R, Walker JE (1993). Organization and Sequences of
Genes for the Subunits of ATP Synthase in the Thermophilic
Cyanobacterium Synechococcus 6716. Biochem J 294:239-251.
Fukuda H, Sakai M, Nagahama K, Fujii T, Matsuoka M, Inoue Y, Ogawa T (1994).
Heterologous Expression of the Gene for the Ethylene-Forming Enzyme from
Pseudomonas syringae in the Cyanobacterium Synechococcus. Biotechnol
Lett 16:1-6.
****** LABORATORY AND GENETIC TOOLS ******
Prabaharan D, Sumathi M, Subramanian G (1994). Ability to Use Ampicillin as
a Nitrogen Source by the Marine Cyanobacterium Phormidium valderianum
BDU 30501. Curr Microbiol 28:315-320.
Sethu KMP, Prabha TN, Venkataraman LV (1994). Preparation of protoplasts from
the cyanobacterium Spirulina platensis and a novel viability assay. Lett
Appl Microbiol 18:241-244.
Shestopalov VI, Nashchokina OO, Shestakov SV, Yankovskii NK (1994).
Construction of the Genomic Library of the Cyanobacterium Synechocystis
sp. PCC 6803 in a Cosmid Vector. Genetika 30:452-455.
Subramanian G, Uma L, Thajuddin N, Prabaharan D, Sekar S, Sundararaman M,
Sophia Rajini V (1994). Manual of Techniques in Cyanobacterial Research.
Bharathidasan University.
Thacker SP, Kothari RM, Ramamurthy V (1994). Obtaining Axenic Cultures of
Filamentous Cyanobacterium Spirulina. Biotechniques 16:216-217.
Mermet-Bouvier P, Chauvat F (1994). A Conditional Expression Vector for the
Cyanobacteria Synechocystis sp Strains PCC 6803 and PCC 6714 or
Synechococcus sp Strains PCC 7942 and PCC 6301. Curr Microbiol
28:145-148.
Moser DP, Zarka D, Kallas T (1993). Characterization of a Restriction Barrier
and Electrotransformation of the Cyanobacterium Nostoc PCC 7121. Arch
Microbiol 160:229-237.
Sode K, Tatara M, Hatano N, Matsunaga T (1994). Foreign Gene Expression in
Marine Cyanobacteria Under Pseudo-Continuous Culture. J Biotechnol
33:243-248.
Kurokawa M, Tominaga H, Ashida H, Sawa Y, Ochiai H (1994). Replication of
filamentous cyanobacterial plasmids, pPF1 from Phormidium foveolarum and
pPB1 from Plectonema boryanum. Biosci Biotechnol Biochem 58:796-797.
Muro-Pastor AM, Kuritz T, Flores E, Herrero A, Wolk CP (1994). Transfer of a
Genetic Marker from a Megaplasmid of Anabaena sp Strain PCC 7120 to a
Megaplasmid of a Different Anabaena Strain. J Bacteriol 176:1093-1098.
Schaefer MR, Chiang GG, Cobley JG, Grossman AR (1993). Plasmids from Two
Morphologically Distinct Cyanobacterial Strains Share a Novel
Replication Origin. J Bacteriol 175:5701-5705.
Yang XY, McFadden BA (1994). The Complete DNA Sequence and Replication
Analysis of the Plasmid pCB2.4 from the Cyanobacterium Synechocystis
PCC 6803. Plasmid 31:131-137.
****** METABOLISM OF DNA, RNA, and PROTEIN ******
Houmard J (1994). Gene transcription in filamtentous cyanobacteria. Microbiol
140:433-441.
Kim ST, Sancar A, Essenmacher C, Babcock GT (1993). Time-Resolved EPR Studies
with DNA Photolyase - Excited-State FADH(0) Abstracts an Electron from
Trp306 to Generate FADH(-), the Catalytically Active Form of the
Cofactor. Proc Natl Acad Sci USA 90:8023-8027.
Mulligan ME, Jackman DM, Murphy ST (1994). Heterocyst-Forming Filamentous
Cyanobacteria Encode Proteins That Resemble Eukaryotic RNA-Binding
Proteins of the RNP Family. J Mol Biol 235:1162-1170.
Pinevich A, Grigoryeva I (1994). Epifluorescence Microscopy of Anabaena sp -
Nucleoid Configurations and Evidence for Inclusion-Associated DNA.
Experientia 50:44-48.
Sancar A (1994). Structure and Function of DNA Photolyase. Biochemistry
33:2-9.
Sugita M, Sugiura M (1994). The Existence of Eukaryotic Ribonucleoprotein
Consensus Sequence-Type RNA-Binding Proteins in a Prokaryote,
Synechococcus 6301. Nucleic Acids Res 22:25-31.
Ueno T, Ito H, Kotani H, Kimizuka F, Nakajima K (1993). Cloning and Expression
of the NspV Restriction-Modification Genes of Nostoc-sp. Strain
PCC 7524. Nucleic Acids Res 21:3899.
Zaug AJ, McEvoy MM, Cech TR (1993). Self-Splicing of the Group-I Intron from
Anabaena Pre-Transfer-RNA - Requirement for Base-Pairing of the Exons
in the Anticodon Stem. Biochemistry 32:7946-7953.
Barbrook AC, Packer JCL, Howe CJ (1993). Components of the Protein
Translocation Machinery in the Thermophilic Cyanobacterium Phormidium
laminosum. Biochem Biophys Res Commun 197:874-877.
Mackle MM, Zilinskas BA (1994). Role of Signal Peptides in Targeting of
Proteins in Cyanobacteria. J Bacteriol 176:1857-1864.
Nakai M, Nohara T, Sugita D, Endo T (1994). Identification and
Characterization of the SecA Protein Homologue in the Cyanobacterium
Synechococcus PCC 7942. Biochem Biophys Res Commun 200:844-851.
Salvi S, Trinei M, Lanfaloni L, Pon CL (1994). Cloning and Characterization
of the Gene Encoding an Esterase from Spirulina platensis. Mol Gen Genet
243:124-126.
****** APPLIED CYANOBACTERIOLOGY ******
Markov SA, Lichtl R, Rao KK, Hall DO (1993). A hollow fibre photobioreactor
for continuous production of hydrogen by immobilized cyanobacteria under
partial vacuum. Int J Hydrogen Energy 18:901-906.
Boussiba S (1993). Production of the nitrogen-fixing cyanobacterium Anabaena
siamensis in a closed tubular reactor for rice farming. Microb Releases
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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
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) NTMarsac@Pasteur.Fr
GERMANY Wolfgang Lockau Biochemie der Pflanzen, Fachbereich
Biologie, Humboldt-Universit„t,
Invalidenstr. 42, 10 115 Berlin
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 Departimento di Scienze e Tecnologie
Alimentari e Microbiologiche.
Universita degli Studi di Firenze,
P.le. delle Cascine 27 51044 Firenze.
(Tel) 055-352051
(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