Tatsuo Omata

Nagoya University

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Shin‐ichi Maeda

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Nobuyuki Takatani

Nagoya University

Makiko Aichi

Chubu University

Teruo Ogawa

Center for Excellence in Molecular Plant Sciences

Iwane Suzuki

University of Tsukuba

Norio Murata

National Institute for Basic Biology

Masaki Kobayashi

Hokkaido University

Kouji Kojima

Sojo University

Kazutaka Ikeda

Kazusa DNA Research Institute

Akihiro Kato

Shibaura Institute of Technology

Cooperative Institutions

Nagoya University

The University of Tokyo

Japan Science and Technology Agency

Kyoto University

Osaka University

Tohoku University

National Institute for Basic Biology

Tokyo University of Science

University of Tsukuba

Istituti di Ricovero e Cura a Carattere Scientifico

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Functional Plant Biology (2002)

Gillian Dean Murray R. Badger Mari Shibata Hiroshi Ohkawa Hirokazu Katoh

In this short article, the co-convenors of CCM2001 outline the significant advances achieved in aquatic CCM research that appear in this Special Issue.The cyanobacterium Synechocystis sp.strain PCC6803 possesses two CO 2 uptake systems, plus two types of HCO 3 -transporter.These authors have generated mutants of Synechocystis PCC6803 in which one, or a combination, of these inorganic carbon acquisition mechanisms is disrupted.The response of these mutants to growth under various CO 2 and pH regimes is discussed.

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10.1071/fpv29n3toc

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Structure, function, and regulation of the cyanobacterial high-affinity bicarbonate transporter

Science Access (2001)

Tatsuo Omata

Exposure of high-CO2-grown cells of cyanobacteria to inorganic carbon-limitation induces transcription of particular genes and expression of high-affinity CO2 and HCO3- transport systems. Among the low-CO2-inducible transcription units of Synechococcus sp. strain PCC 7942 is the cmpABCD operon, which encodes an ATP-binding cassette (ABC) transporter involved in HCO3- uptake. The three genes, cmpBCD, encode membrane components of an ABC transporter, whereas cmpA encodes a 42-kD protein anchored to the plasma membrane, which binds HCO3- with high affinity (Kd = 5 m M) and acts as the substrate-binding protein of the transporter. A deletion mutant of cmpAB (M42) retains low CO2-inducible activity of HCO3- transport, indicating occurrence of HCO3- transporter(s) distinct from the one encoded by cmpABCD. Since HCO3- uptake by low CO2-induced M42 cells shows lower affinity for external HCO3- than for wild-type cells under the same conditions, it is deduced that the HCO3- transporter encoded by cmpABCD has the highest affinity for HCO3- among the HCO3- transporters present in the cyanobacterium. The low CO2-responsive induction of the cmpABCD operon requires a LysR family protein CmpR, which is similar to CbbR (RbcR), the activator of the CO2 fixation operons of chemoautotrophic and purple photosynthetic bacteria. In the mutant of cmpR, low CO2-induced upregulation of the rbcLS and ccmKLMNO operons was not abolished but enhanced, indicating presence of multiple mechanisms for low CO2-responsive gene activation in cyanobacteria.

Transcription

10.1071/sa0403431

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Data Submission System for Cyanobacterial DNA Chip Consortium

Ikuo Uchiyama Tomoki Miwa Hiroyo Nishide Iwane Suzuki Tatsuo Omata

murata@nibb.ac.jp kanehisa@kuicr.kyoto-u.ac.jp 1 National Institute for Basic Biology 2 Research Center for Computational Science 3 Center for Integrative Bioscience, Okazaki National Research Institutes, Nishigonaka 38, Myodaiji, Okazaki 444-8585, Japan 4 Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusaku, Nagoya 464-8601, Japan 5 Graduate School of Arts and Sciences, University of Tokyo, 3-8-1 Komaba, Meguroku, Tokyo 153-8902, Japan 6 Institute for Chemical Research, Kyoto University, Gokasho, Uji 611-0011, Japan

Okazaki fragments

Research center

Basic Research

10.11234/gi1990.11.235

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A novel nitrite reductase gene from the cyanobacterium Plectonema boryanum

Journal of Bacteriology (1995)

Iwane Suzuki Hideaki Kikuchi Shigetada Nakanishi Yuichi Fujita T. Sugiyama

The gene (nirA) for nitrite reductase was cloned from the nonheterocystous, filamentous cyanobacterium Plectonema boryanum. The predicted protein consists of 654 amino acids and has a calculated molecular weight of 72,135. The deduced amino acid sequence from positions 1 to 511 is strongly similar to the entire sequence of the ferredoxin-dependent nitrite reductases from other phototrophs, while the remainder of the protein is unique to the Plectonema nitrite reductase. The C-terminal portion of the protein (amino acids 584 to 654) is 30 to 35% identical to [2Fe-2S] ferredoxins from higher plants and cyanobacteria, with all of the four Cys residues involved in binding of the [2Fe-2S] cluster in the ferredoxins being conserved. Immunoblotting analysis of the extracts of P. boryanum cells showed that the NirA polypeptide has an apparent molecular mass of 75 kDa. An insertional mutant of nirA lacked the 75-kDa polypeptide, had no nitrite reductase activity, and failed to grow on nitrate and nitrite, indicating that the novel nirA is the sole nitrite reductase gene in P. boryanum and that the NirA polypeptide with the ferredoxin-like domain is the apoprotein of the functional nitrite reductase. As in Synechococcus sp. strain PCC7942, nirA is the first gene of a large transcription unit (> 7 kb in size) and is repressed by ammonium and derepressed simply by deprivation of ammonium from the medium. The development of nitrite reductase activity was, however, found to require the presence of nitrate in the medium.

10.1128/jb.177.21.6137-6143.1995

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Citations (54)

[Gene manipulation in cyanobacteria].

PubMed (1990)

Tatsuo Omata Hajime Wada Nobuo Murata

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Loss of Cytochrome cM Stimulates Cyanobacterial Heterotrophic Growth in the Dark

Plant and Cell Physiology (2014)

Yuto Hiraide Kenshiro Oshima Takatomo Fujisawa Kazuma Uesaka Yuu Hirose

Although cyanobacteria are photoautotrophs, they have the capability for heterotrophic metabolism that enables them to survive in their natural habitat. However, cyanobacterial species that grow heterotrophically in the dark are rare. It remains largely unknown how cyanobacteria regulate heterotrophic activity. The cyanobacterium Leptolyngbya boryana grows heterotrophically with glucose in the dark. A dark-adapted variant dg5 isolated from the wild type (WT) exhibits enhanced heterotrophic growth in the dark. We sequenced the genomes of dg5 and the WT to identify the mutation(s) of dg5. The WT genome consists of a circular chromosome (6,176,364 bp), a circular plasmid pLBA (77,793 bp) and two linear plasmids pLBX (504,942 bp) and pLBY (44,369 bp). Genome comparison revealed three mutation sites. Phenotype analysis of mutants isolated from the WT by introducing these mutations individually revealed that the relevant mutation is a single adenine insertion causing a frameshift of cytM encoding Cyt cM. The respiratory oxygen consumption of the cytM-lacking mutant grown in the dark was significantly higher than that of the WT. We isolated a cytM-lacking mutant, ΔcytM, from another cyanobacterium Synechocystis sp. PCC 6803, and ΔcytM grew in the dark with a doubling time of 33 h in contrast to no growth of the WT. The respiratory oxygen consumption of ΔcytM grown in the dark was about 2-fold higher than that of the WT. These results suggest a suppressive role(s) for Cyt cM in regulation of heterotrophic activity.

Synechocystis

Wild type

10.1093/pcp/pcu165

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Fractionation of Nitrogen Isotopes during the Uptake and Assimilation of Ammonia<italic><xref ref-type="fn" rid="fn1"><sup>l</sup></xref></italic> by Plants

Plant and Cell Physiology (1991)

Tadakatsu Yoneyama Tatsuo Omata Satoshi Nakata Jinya Yazaki

Two varieties (Nihonbare and Koshihikari) of rice plants (Oryza sativa L.) were grown hydro-ponically with two levels (20 and 100 mg N liter −1) of ammonia. Variations in levels of natural abundance of 15N (δ15N) were analyzed in the ammonia and organic nitrogen of shoots and roots, as well as in the ammonia in the culture solution. There was substantial fractionation of nitrogen isotopes during the uptake of ammonia. When plants absorbed a large proportion of ammonia from a solution with a low concentration, less negative δ15N values in plants and high positive δ15N values in the ammonia remaining in solution were observed. The reverse was found when a smaller fraction of ammonia was absorbed from a solution with a higher concentration of ammonia. The δl5N values of ammonia in shoots and roots were higher than in the respective constituent organic nitrogen, suggesting the fractionation of nitrogen isotopes during the assimilation of ammonia. Wild-type and mutant cells of the cyanobacterium (blue-green alga) Synechococcus PCC 7942 were grown in nitrate- or ammonia-containing medium as the source of nitrogen. Fractionation of nitrogen isotopes during the uptake of nitrate was limited, whereas that during the uptake of ammonia was considerable.

Isotopes of nitrogen

10.1093/oxfordjournals.pcp.a078199

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Plant Cell Physiol-2015-Kato-2467-77

Akihiro Kato Nobuyuki Takatani Kazuhide Use Kazuma Uesaka Kazutaka Ikeda

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MOESM3 of Modulation of the balance of fatty acid production and secretion is crucial for enhancement of growth and productivity of the engineered mutant of the cyanobacterium Synechococcus elongatus

Figshare (2016)

Akihiro Kato Kazuhide Use Nobuyuki Takatani Kazutaka Ikeda Miyuki Matsuura