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Originally published In Press as doi:10.1074/jbc.M001468200 on March 21, 2000

J. Biol. Chem., Vol. 275, Issue 22, 17072-17079, June 2, 2000
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A New Subunit of Cytochrome b6f Complex Undergoes Reversible Phosphorylation upon State Transition*

Patrice HamelDagger , Jacqueline Olive§, Yves Pierre, Francis-André Wollman||, and Catherine de Vitry||**

From the Dagger  Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095-1569, the § Institut Jacques Monod, Université de Paris VII, 75005 Paris, France, the  Laboratoire de Physico-Chimie Moléculaire des membranes Biologiques, CNRS UPR 9052, Institut de Biologie Physico-Chimique, 75005 Paris, France, and the || Physiologie Membranaire et Moléculaire du Chloroplaste, CNRS UPR1261, Institut de Biologie Physico-Chimique, 75005 Paris, France

A 15.2-kDa polypeptide, encoded by the nuclear gene PETO, was identified as a novel cytochrome b6f subunit in Chlamydomonas reinhardtii. The PETO gene product is a bona fide subunit, subunit V, of the cytochrome b6f complex, because (i) it copurifies with the other cytochrome b6f subunits in the early stages of the purification procedure, (ii) it is deficient in cytochrome b6f mutants accumulating little of the complex, and (iii) it colocalizes with cytochrome f, which migrates between stacked and unstacked membrane regions upon state transition. Sequence analysis and biochemical characterization of subunit V shows that it has a one transmembrane alpha -helix topology with two large hydrophilic domains extending on the stromal and lumenal side of the thylakoid membranes, with a lumenal location of the N terminus. Subunit V is reversibly phosphorylated upon state transition, a unique feature that, together with its topological organization, points to the possible role of subunit V in signal transduction during redox-controlled short term and long term adaptation of the photosynthetic apparatus in eukaryotes.

* This work was supported by the CNRS UPR 1261 and by NIGMS, National Institutes of Health Grant GM48350 (to S. Merchant for P. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF222893.

** To whom correspondence should be addressed: Physiologie Membranaire et Moléculaire du Chloroplaste, CNRS UPR 1261, Institut de Biologie Physico-Chimique, 13 Rue Pierre et Marie Curie, 75005 Paris, France. Tel.: 33-1-58-41-5000; Fax: 33-1-58-41-5020; E-mail: catherine.devitry@ibpc.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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