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Published on April 2, 2004; 10.1104/pp.103.037754

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Received December 15, 2003
Returned for revision January 27, 2004
Accepted January 27, 2004

Phosphatidylglycerol Is Essential for Oligomerization of Photosystem I Reaction Center

Ildikó Domonkos *, Przemyslaw Malec , Anna Sallai , László Kovács , Kunihiro Itoh , Gaozhong Shen , Bettina Ughy , Balázs Bogos , Isamu Sakurai , Mihály Kis , Kazimierz Strzalka , Hajime Wada , Shigeru Itoh , Tibor Farkas , and Zoltán Gombos

Institute of Plant Biology, Biological Research Center of the Hungarian Academy of Sciences, H-6701 Szeged, Hungary
Department of Plant Physiology and Biochemistry, Faculty of Biotechnology, Jagiellonian University, PL-30-387 Krakow, Poland
Division of Material Science (Physics), Graduate School of Science, Nagoya University, Furocho, Chikusa, Nagoya 464-8601, Japan
Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802
Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Komamba, Tokyo 153-8902, Japan
Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, H-6701 Szeged, Hungary (T.F.)

* Corresponding author; email: domonkos{at}nucleus.szbk.u-szeged.hu.

Our earlier studies with the pgsA mutant of Synechocystis PCC6803 demonstrated the important role of phosphatidylglycerol (PG) in PSII dimer formation and in electron transport between the primary and secondary electron-accepting plastoquinones of PSII. Using a long-term depletion of PG from pgsA mutant cells, we could induce a decrease not only in PSII but also in PSI activity. Simultaneously with the decrease in PSI activity, dramatic structural changes of the PSI complex were detected. A 21-d PG depletion resulted in the degradation of PSI trimers and concomitant accumulation of monomer PSI. The analyses of PSI particles isolated by MonoQ chromatography showed that, following the 21-d depletion, PSI trimers were no longer detectable in the thylakoid membranes. Immunoblot analyses revealed that the PSI monomers accumulating in the PG-depleted mutant cells do not contain PsaL, the protein subunit thought to be responsible for the trimer formation. Nevertheless, the trimeric structure of PSI reaction center could be restored by readdition of PG, even in the presence of the protein synthesis inhibitor lincomycin, indicating that free PsaL was present in thylakoid membranes following the 21-d PG depletion. Our data suggest an indispensable role for PG in the PsaL-mediated assembly of the PSI reaction center.




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