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The Synechocystis sp PCC 6803 Oxa1 Homolog Is Essential for Membrane Integration of Reaction Center Precursor Protein pD1^[W]

^a Department for Molecular Botany, University Ulm, D-89069 Ulm, Germany
^b Department for Biology I, Botany, Ludwig-Maximilians-University, D-80638 Munich, Germany
^c Max-Planck-Institute of Molecular Plant Physiology, D-14476 Potsdam-Golm, Germany

¹ To whom correspondence should be addressed. E-mail soll{at}lrz.uni-muenchen.de or lutz.eichacker{at}lrz.uni-muenchen.de; fax 49-89-17861185 or 49-89-17861209.

Synechocystis sp PCC 6803 Slr1471p, an Oxa1p/Alb3/YidC homolog, is an essential protein for cell viability for which functions in thylakoid membrane biogenesis and cell division have been proposed. Using a fusion of green fluorescent protein to the C terminus of Slr1471p, we found that the mutant slr1471-gfp is photochemically inhibited when light intensities increase to 80 µmol·m^–2·s^–1. We show that photoinhibition correlates with an increased redox potential of the reaction center quinone Q_A^– and a decreased redox potential of Q_B^–. Analysis reveals that membrane integration of the D1 precursor protein is affected, leading to the accumulation of pD1 in the membrane phase. We show that Slr1471p interacts directly with the D1 protein and discuss why the accumulation of pD1 in two reaction center assembly intermediates is dependent on Slr1471p.

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