| Project/Area Number |
07404045
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
植物生理
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| Research Institution | The University of Tokyo |
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Principal Investigator |
OHMORI Masayuki The University of Tokyo, Graduate School of Arts and Sciences, Professor, 大学院・総合文化研究科, 教授 (80013580)
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| Co-Investigator(Kenkyū-buntansha) |
IKEUCHI Masahiko The University of Tokyo, Graduate School of Arts and Sciences, Asociate Professo, 大学院・総合文化研究科, 助教授 (20159601)
小関 良宏 東京農工大学, 工学部, 助教授 (50185592)
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| Project Period (FY) |
1995 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥37,100,000 (Direct Cost: ¥37,100,000)
Fiscal Year 1998: ¥2,700,000 (Direct Cost: ¥2,700,000)
Fiscal Year 1997: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1996: ¥10,400,000 (Direct Cost: ¥10,400,000)
Fiscal Year 1995: ¥21,600,000 (Direct Cost: ¥21,600,000)
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| Keywords | cyclic AMP / adenylate cyclase / cyanobacteria / phosphorylation / light / signal transduction / ラン薬 / サイフリックAMP / 赤色光 / 近赤外光 / 青色光 / 自己リン酸化 / cAMP / 植物 / CAMP / 分子生物学 |
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| Research Abstract |
1) Effect of different wave lengths of light on cellular cAMP content. Action spectra on the change in cellular cAMP by irradiating different wave lengths of light revealed that in Anabaena cylindricared light decreased the cAMP level whereas far-red light increased it. On the other hand, blue light increased the cellular cAMP level in Synechocystis sp. PCC 6803. It was further shown that in the Synechocystis blue light enhanced motility of the cells. This enhancement was probably due to the blue light-increased cellular cAMP.We concluded that light somehow affected cellular cAMP level, which regulated cell motility of cyanobacteria.
2) A cyanobacterial adenylate cyclase protein, CyaC, was activated by autophosphorylation and a subsequent phosphotransfer reaction.
We have isolated genes for 10 different adenylate cyclases from cyanobacteria. Each adenylate cyclase consists of a common catalytic domain and a very specified regulatory domain. An adenylate cyclase named CyaC contains domains of bacterial two component regulatory proteins ; a sensory kinase domain, two response regulator domains and an ETR-like domain. CyaC autophosphorylate in its sensory kinase domain and the phosphorous was transferred to the response regulator domain. The catalytic activity of CyaC was enhanced by autophosphorylation and a subsequent phosphotransfer reaction.
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