| Literature DB >> 17166849 |
Thomas Volkmer1, Dirk Schneider, Gábor Bernát, Helmut Kirchhoff, Stephan-Olav Wenk, Matthias Rögner.
Abstract
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.Entities:
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Year: 2006 PMID: 17166849 DOI: 10.1074/jbc.M604948200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157