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First published online October 5, 2007; 10.1104/pp.107.106781

Plant Physiology 145:1361-1370 (2007)
© 2007 American Society of Plant Biologists

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BIOENERGETICS AND PHOTOSYNTHESIS

Digalactosyldiacylglycerol Is Required for Stabilization of the Oxygen-Evolving Complex in Photosystem II1,[C],[OA]

Isamu Sakurai2, Naoki Mizusawa, Hajime Wada and Naoki Sato*

Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Meguro-ku, Tokyo 153–8902, Japan

The galactolipid digalactosyldiacylglycerol (DGDG) is present in the thylakoid membranes of oxygenic photosynthetic organisms such as higher plants and cyanobacteria. Recent x-ray crystallographic analysis of protein-cofactor supercomplexes in thylakoid membranes revealed that DGDG molecules are present in the photosystem II (PSII) complex (four molecules per monomer), suggesting that DGDG molecules play important roles in folding and assembly of subunits in the PSII complex. However, the specific role of DGDG in PSII has not been fully clarified. In this study, we identified the dgdA gene (slr1508, a ycf82 homolog) of Synechocystis sp. PCC6803 that presumably encodes a DGDG synthase involved in the biosynthesis of DGDG by comparison of genomic sequence data. Disruption of the dgdA gene resulted in a mutant defective in DGDG synthesis. Despite the lack of DGDG, the mutant cells grew as rapidly as the wild-type cells, indicating that DGDG is not essential for growth in Synechocystis. However, we found that oxygen-evolving activity of PSII was significantly decreased in the mutant. Analyses of the PSII complex purified from the mutant cells indicated that the extrinsic proteins PsbU, PsbV, and PsbO, which stabilize the oxygen-evolving complex, were substantially dissociated from the PSII complex. In addition, we found that heat susceptibility but not dark-induced inactivation of oxygen-evolving activity was notably increased in the mutant cells in comparison to the wild-type cells, suggesting that the PsbU subunit is dissociated from the PSII complex even in vivo. These results demonstrate that DGDG plays important roles in PSII through the binding of extrinsic proteins required for stabilization of the oxygen-evolving complex.


1 This work was supported by Grants-in-Aid for Scientific Research (no. 18770029 to N.M., nos. 18017005 and 16GS0304 to N.S.) and a Research Fellowship for Young Scientists (no. 11578 to I.S.) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan.

2 Present address: Research Institute for Bioresources, Okayama University, Chuo 2-20-1, Kurashiki 710–0046, Japan.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Naoki Sato (naokisat{at}bio.c.u-tokyo.ac.jp).

[C] Some figures in this article are displayed in color online but in black and white in the print edition.

[OA] Open Access articles can be viewed online without a subscription.

www.plantphysiol.org/cgi/doi/10.1104/pp.107.106781

* Corresponding author; e-mail naokisat{at}bio.c.u-tokyo.ac.jp.

Received August 2, 2007; accepted September 26, 2007; published October 5, 2007.







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