| Effects of the lack of phosphatidylglycerol on the donor side of photosystem II. | |
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MedLine Citation:
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PMID: 17513482 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Our previous studies with the pgsA mutant of the cyanobacterium Synechocystis sp. PCC6803 (hereafter termed pgsA mutant), which is defective for the biosynthesis of phosphatidylglycerol (PG), revealed an important role for PG in the electron acceptor side of photosystem II (PSII), especially in the electron transport between plastoquinones Q(A) and Q(B). This study now shows that PG also plays an important role in the electron donor side of PSII, namely, the oxygen-evolving system. Analyses of purified PSII complexes indicated that PSII from PG-depleted pgsA mutant cells sustained only approximately 50% of the oxygen-evolving activity compared to wild-type cells. Dissociation of the extrinsic proteins PsbO, PsbV, and PsbU, which are required for stabilization of the manganese (Mn) cluster, followed by the release of a Mn atom, was observed in PSII of the PG-depleted mutant cells. The released PsbO rebound to PSII when PG was added back to the PG-depleted mutant cells, even when de novo protein synthesis was inhibited. Changes in photosynthetic activity of the PG-depleted pgsA mutant cells induced by heat treatment or dark incubation resembled those of DeltapsbO, DeltapsbV, and DeltapsbU mutant cells. These results suggest that PG plays an important role in binding extrinsic proteins required for sustaining a functional Mn cluster on the donor side of PSII. |
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Authors:
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Isamu Sakurai; Naoki Mizusawa; Shunsuke Ohashi; Masami Kobayashi; Hajime Wada |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2007-05-18 |
Journal Detail:
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Title: Plant physiology Volume: 144 ISSN: 0032-0889 ISO Abbreviation: Plant Physiol. Publication Date: 2007 Jul |
Date Detail:
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Created Date: 2007-07-09 Completed Date: 2007-11-13 Revised Date: 2010-09-16 |
Medline Journal Info:
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Nlm Unique ID: 0401224 Medline TA: Plant Physiol Country: United States |
Other Details:
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Languages: eng Pagination: 1336-46 Citation Subset: IM |
Affiliation:
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Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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metabolism* Electron Transport / physiology Fluorescence Lipid Metabolism Manganese / metabolism* Mutation Oxygen / metabolism Phosphatidylglycerols / metabolism* Photosynthesis / physiology Photosystem II Protein Complex / metabolism* Synechocystis / genetics, metabolism*, physiology |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Phosphatidylglycerols; 0/Photosystem II Protein Complex; 7439-96-5/Manganese; 7782-44-7/Oxygen |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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