|
|
||||||||
|
First published online April 2, 2004; 10.1104/pp.103.037754 Plant Physiology 134:1471-1478 (2004) © 2004 American Society of Plant Biologists Phosphatidylglycerol Is Essential for Oligomerization of Photosystem I Reaction Center1Institute of Plant Biology, Biological Research Center of the Hungarian Academy of Sciences, H6701 Szeged, Hungary (I.D., A.S., L.K., B.U., B.B., M.K., Z.G.); Department of Plant Physiology and Biochemistry, Faculty of Biotechnology, Jagiellonian University, PL30387 Krakow, Poland (P.M., K.S.); Division of Material Science (Physics), Graduate School of Science, Nagoya University, Furocho, Chikusa, Nagoya 4648601, Japan (K.I., S.I.); Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802 (G.S.); Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Komamba, Tokyo 1538902, Japan (I.S., H.W.); and Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, H6701 Szeged, Hungary (T.F.)
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.
1 This work was supported by grants from the Hungarian Science Foundation (OTKA; grant nos. T 34174 and T 38408), by the Dr. Rollin D. Hotchkiss Foundation (I.D.), and cofinanced by the European Union (Center of Excellence grant; contract no. BIER ICA1CT200070012) and the Polish Committee for Scientific Research (grant no. 158/E338/SPUBM/5 PR UE/DZ 9/20012003). Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.037754. * Corresponding author; e-mail domonkos{at}nucleus.szbk.u-szeged.hu; fax 3662433434. Received December 15, 2003; returned for revision January 27, 2004; accepted January 27, 2004. This article has been cited by other articles:
|
|||||||||||||||||||||||||||||||||||||||||||||||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| ASPB Publications | PLANT PHYSIOLOGY® | THE PLANT CELL | |
|---|---|---|---|