2013 Fiscal Year Final Research Report
Elucidation of molecular functions of the oxygen-evolving complex homologs in chloroplasts
| Project/Area Number |
23780103
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
IFUKU KENTARO 京都大学, 生命科学研究科, 助教 (50359783)
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| Project Period (FY) |
2011 – 2013
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| Keywords | 植物 / 光合成 / 電子伝達 / 環境応答 / 分子進化 |
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| Research Abstract |
The oxygen-evolving complex (OEC) proteins are membrane-peripheral proteins bound to thylakoid lumenal side of photosystem (PS) II, and PsbP and PsbQ are the OEC proteins found in green plants. In addition, multiple homologs for PsbP and PsbQ have been identified in chloroplasts and in cyanobacteria; however, their functions have not been fully elucidated yet. In this study, we characterized molecular functions of the OEC homologs using mutants of Arabidopsis and cyanobacteria. It was found that the OEC homologs indeed have various functions in photosynthetic electron transport, such as the regulation of PSII activity under various light conditions and the accumulation of the chloroplast NAD(P)H dehydrogenase (NDH) complex that operates in cyclic electron transport around PSI. These results suggest that functional diversification of the OEC homologs has occurred during evolution to support the optimum photosynthesis.
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Research Products
(25 results)
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[Journal Article] Cross-Linking Evidence for Multiple Interactions of the PsbP and PsbQ Proteins in a Higher Plant Photosystem II Supercomplex2014
Author(s)
Ido, K., Nield, J., Fukao, Y., Nishimura, T., Sato, F., Ifuku, K
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Journal Title
J. Biol. Chem
Volume: (in press)
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[Journal Article] Identification of the basic amino acid residues on the PsbP protein involved in the electrostatic interaction with photosystem II2014
Author(s)
Nishimura, T., Uno, C., Ido, K., Nagao, R., Noguchi, T., Sato, F., Ifuku, K
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Journal Title
Biochim. Biophys. Acta
Volume: (in press)
DOI
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[Journal Article] The Conserved His-144 in the PsbP Protein Is Important for the Interaction between the PsbP N-terminus and the Cyt b_559 Subunit of Photosystem II2012
Author(s)
Ido, K., Kakiuchi, S., Uno, C., Nishimura, T., Fukao, Y., Noguchi, T., Sato, F., and Ifuku, K
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Journal Title
J. Biol. Chem
Volume: 287
Pages: 26377-26387
DOI
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[Journal Article] The PsbQ protein stabilizes the functional binding of the PsbP protein to photosystem II in higher plants2012
Author(s)
Kakiuchi, S., Uno, C., Ido, K., Nishimura, T., Noguchi, T., Ifuku, K., and Sato, F
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Journal Title
Biochim Biophys Acta (Bioenergetics)
Volume: 1817
Pages: 1346-1351
DOI
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[Presentation] Interaction of the PsbP protein in higher plant PSII complex2013
Author(s)
Nishimura, T., Asada, M., Ido, K., Mino, H., Sato, F., and Ifuku, K
Organizer
The 16^<th> International Congress on Photosynthesis
Place of Presentation
St. Louis, MO, USA
Year and Date
20130811-16
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