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Published on May 18, 2007; 10.1104/pp.107.098731


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Received March 1, 2007
Accepted May 14, 2007

Effects of the Lack of Phosphatidylglycerol on the Donor Side of Photosystem II

Isamu Sakurai , Naoki Mizusawa , Shunsuke Ohashi , Masami Kobayashi , and Hajime Wada *

Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Komaba 3-8-1, Meguro-ku, Tokyo 153-8902, Japan; Institute of Materials Science, University of Tsukuba, Ibaraki 305-8573, Japan

* Corresponding author; email: hwada{at}bio.c.u-tokyo.ac.jp.

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 QA and QB. The present 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 ~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 Mn-cluster, followed by the release of a manganese atom, was observed in PSII of the PG-depleted mutant cells. The released PsbO re-bound 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 {Delta}psbO, {Delta}psbV and {Delta}psbU mutant cells. These results suggest that PG plays an important role in the binding of extrinsic proteins required for sustaining a functional Mn-cluster on the donor side of PSII.




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