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J. Biol. Chem., Vol. 281, Issue 45, 34227-34238, November 10, 2006

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PsbI Affects the Stability, Function, and Phosphorylation Patterns of Photosystem II Assemblies in Tobacco^*

Serena Schwenkert¹, Pavan Umate¹², Cristina Dal Bosco, Stefanie Volz, Lada Mlçochová, Mikael Zoryan, Lutz A. Eichacker, Itzhak Ohad, Reinhold G. Herrmann, and Jörg Meurer³

From the Department Biology I, Botany, Ludwig-Maximilians-University Munich, Menzingerstrasse 67, 80638 Munich, Germany and Department of Biological Chemistry and the Minerva Center of Photosynthesis Research, The Hebrew University of Jerusalem, Jerusalem 91904, Israel

Photosystem II (PSII) core complexes consist of CP47, CP43, D1, D2 proteins and of several low molecular weight integral membrane polypeptides, such as the chloroplast-encoded PsbE, PsbF, and PsbI proteins. To elucidate the function of PsbI in the photosynthetic process as well as in the biogenesis of PSII in higher plants, we generated homoplastomic knock-out plants by replacing most of the tobacco psbI gene with a spectinomycin resistance cartridge. Mutant plants are photoautotrophically viable under green house conditions but sensitive to high light irradiation. Antenna proteins of PSII accumulate to normal amounts, but levels of the PSII core complex are reduced by 50%. Bioenergetic and fluorescence studies uncovered that PsbI is required for the stability but not for the assembly of dimeric PSII and supercomplexes consisting of PSII and the outer antenna (PSII-LHCII). Thermoluminescence emission bands indicate that the presence of PsbI is required for assembly of a fully functional Q_A binding site. We show that phosphorylation of the reaction center proteins D1 and D2 is light and redox-regulated in the wild type, but phosphorylation is abolished in the mutant, presumably due to structural alterations of PSII when PsbI is deficient. Unlike wild type, phosphorylation of LHCII is strongly increased in the dark due to accumulation of reduced plastoquinone, whereas even upon state II light phosphorylation is decreased in psbI. These data attest that phosphorylation of D1/D2, CP43, and LHCII is regulated differently.

Received for publication, May 22, 2006 , and in revised form, August 18, 2006.

^* This work was supported by German Science Foundation Grants SFB184 and SFB TR1. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ These authors contributed equally to this work.

² Recipient of a fellowship from the Deutscher Akademischer Austauschdienst.

³ To whom correspondence should be addressed. Tel.: 49-89-17861288; Fax: 49-89-1782274; E-mail: joerg.meurer{at}lrz.uni-muenchen.de.

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