1997 Fiscal Year Final Research Report Summary
Phosphorylation of Proteins in Photosystem II
| Project/Area Number |
08044225
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| Research Category |
Grant-in-Aid for international Scientific Research
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| Allocation Type | Single-year Grants |
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| Section | Joint Research . |
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| Research Field |
植物生理
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| Research Institution | Ehime University |
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Principal Investigator |
HAYASHI Hidenori Ehime University, Faculty of Science, Professor, 理学部, 教授 (60124682)
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| Co-Investigator(Kenkyū-buntansha) |
OSMOND Berry The Austrarian National University, Professor, 総合科学研究所, 教授
FARDEN Kevin オタゴ大学, 生化学部, 準教授
EATONーRYE Ju オタゴ大学, 生化学部, 助教授
MASAKATSU Watanabe National Institute for Basic Biology, Associate Professor, 基礎生物学研究所, 助教授 (40124226)
MORITA Hayato Ehime University, Faculty of Science, Research Associate, 理学部, 助手 (50274303)
EATON-RYE Julian J. Otago University, Associate Professor
FARGEN Kevin J.L Otago University, Associate Professor
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| Project Period (FY) |
1996 – 1997
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| Keywords | Preotein Phosphorylation / D1 protein / Phostosynthesis / Photosystem / Cyanobacteria / Site-directed mutagenesis / Gene manipulation |
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| Research Abstract |
Photosynthesis is the most essential physiological process in plants as it converted the solar energy into the chemical energy available for all the living organisms and its efficiency should be kept above a certain level to survive under fluctuating environment, . A part of photosynthesis proceeds in a super-macro-protein complex, so called photosystem II and many mechanisms contribute to retain optimum reaction rate under unfavorable environmental conditions. It is know that Dl protein in PS II complex contain highly conserved threonine residue at N-terminal and this residue is phosphorylated under several conditions. It is possible that the phosphorylation of the threonine residue plays an important role in the response of the PS II complex to environmental stresses. So we tried to examined the effect of mutation of the threonine residue on the PS II stability. The major strategies for this purpose are 1) the New Zealand research group establish the site directed mutagenesis of cyanobacterial PS II complex including the oligonucleotide-directed mutagenesis of CP47 component 2) the Japanese research group evaluate the effect of mutation on the photosynthetic activities under various environmental conditions particularly under high temperature stress. We found various mutation of PSII complex cause the serious effect on the PSII acti-vities and the response of PSII complex to environmental stress. However, the mutation threonine residue in Dl protein PSII complex had little or no effects on its activities under high temperature stress. The results suggest that higher ordered structure of PSII complex should more important to retain its activities under various conditions.
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Research Products
(14 results)
