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J. Biol. Chem., Vol. 282, Issue 6, 3730-3737, February 9, 2007
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1
From the
Biochemie der Pflanzen, Ruhr-Universität Bochum, Universitätsstrasse 150, 44780 Bochum, Germany,
Molekularbiologie und Biochemie, Zentrum für Biochemie und Molekulare Zellforschung, Albert-Ludwigs-Universität Freiburg, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany, and the ¶Institut für Botanik, Schlossgarten 3, 48149 Münster, Germany
To analyze the function of a protein encoded by the open reading frame ssr2998 in Synechocystis sp. PCC 6803, the corresponding gene was disrupted, and the generated mutant strain was analyzed. Loss of the 7.2-kDa protein severely reduced the growth of Synechocystis, especially under high light conditions, and appeared to impair the function of the cytochrome b6 f complex. This resulted in slower electron donation to cytochrome f and photosystem 1 and, concomitantly, over-reduction of the plastoquinone pool, which in turn had an impact on the photosystem 1 to photosystem 2 stoichiometry and state transition. Furthermore, a 7.2-kDa protein, encoded by the open reading frame ssr2998, was co-isolated with the cytochrome b6 f complex from the cyanobacterium Synechocystis sp. PCC 6803. ssr2998 seems to be structurally and functionally associated with the cytochrome b6 f complex from Synechocystis, and the protein could be involved in regulation of electron transfer processes in Synechocystis sp. PCC 6803.
Received for publication, May 23, 2006 , and in revised form, November 24, 2006.
* This work was supported by Deutsche Forschungsgemeinschaft SFB 480 projects C1 (to M. R.) and KI818/2 (to H. K.), by the Fonds der Chemischen Industrie, and by funds from the Landesstiftung Baden-Württemberg (to D. S.). 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 To whom correspondence should be addressed. E-mail: matthias.roegner{at}rub.de.
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