Site-directed mutagenesis of amino acid residues of D1 protein interacting with phosphatidylglycerol affects the function of plastoquinone QB in photosystem II
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- 作者：Kaichiro Endo ; Naoki Mizusawa ; Jian-Ren Shen ; Masato Yamada…
- 关键词：D1 ; Phosphatidylglycerol ; Photosystem II ; Site ; directed mutagenesis ; Synechocystis sp. PCC 6803
- 刊名：Photosynthesis Research
- 出版年：2015
- 出版时间：December 2015
- 年：2015
- 卷：126
- 期：2-3
- 页码：385-397
- 全文大小：3,924 KB
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Naoki Mizusawa (2) (3)
Jian-Ren Shen (4)
Masato Yamada (5)
Tatsuya Tomo (5)
Hirohisa Komatsu (6)
Masami Kobayashi (6)
Koichi Kobayashi (1)
Hajime Wada (1)
1. Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro-ku, Tokyo, 153-8902, Japan
2. Department of Frontier Bioscience, Hosei University, Koganei, Tokyo, 184-8584, Japan
3. Research Center for Micro-Nano Technology, Hosei University, Koganei, Tokyo, 184-0003, Japan
4. Photosynthesis Research Center, Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka, Okayama, 700-8530, Japan
5. Faculty of Science, Tokyo University of Science, Kagurazaka, Shinjuku-ku, Tokyo, 162-8601, Japan
6. Division of Materials Science, Faculty of Pure and Applied Science, University of Tsukuba, Ibaraki, 305-8573, Japan - 刊物类别：Biomedical and Life Sciences
- 刊物主题：Life Sciences
Plant Physiology - 出版者：Springer Netherlands
- ISSN：1573-5079
文摘
Recent X-ray crystallographic analysis of photosystem (PS) II at 1.9-? resolution identified 20 lipid molecules in the complex, five of which are phosphatidylglycerol (PG). In this study, we mutagenized amino acid residues S232 and N234 of D1, which interact with two of the PG molecules (PG664 and PG694), by site-directed mutagenesis in Synechocystis sp. PCC 6803 to investigate the role of the interaction in PSII. The serine and asparagine residues at positions 232 and 234 from the N-terminus were mutagenized to alanine and aspartic acid, respectively, and a mutant carrying both amino acid substitutions was also produced. Although the obtained mutants, S232A, N234D, and S232AN234D, exhibited normal growth, they showed decreased photosynthetic activities and slower electron transport from QA to QB than the control strain. Thermoluminescence analysis suggested that this slower electron transfer in the mutants was caused by more negative redox potential of QB, but not in those of QA and S2. In addition, the levels of extrinsic proteins, PsbV and PsbU, were decreased in PSII monomer purified from the S232AN234D mutant, while that of Psb28 was increased. In the S232AN234D mutant, the content of PG in PSII was slightly decreased, whereas that of monogalactosyldiacylglycerol was increased compared with the control strain. These results suggest that the interactions of S232 and N234 with PG664 and PG694 are important to maintain the function of QB and to stabilize the binding of extrinsic proteins to PSII. Keywords D1 Phosphatidylglycerol Photosystem II Site-directed mutagenesis Synechocystis sp. PCC 6803