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Ssr2998 of Synechocystis sp. PCC 6803 is involved in regulation of cyanobacterial electron transport and associated with the cytochrome b6f complex.
Volkmer, Thomas; Schneider, Dirk; Bernát, Gábor; Kirchhoff, Helmut; Wenk, Stephan-Olav; Rögner, Matthias.
Afiliación
  • Volkmer T; Biochemie der Pflanzen, Ruhr-Universität Bochum, Universitätsstrasse 150, 44780 Bochum, Germany.
J Biol Chem ; 282(6): 3730-7, 2007 Feb 09.
Article en En | MEDLINE | ID: mdl-17166849
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.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Secuencias Repetitivas de Ácidos Nucleicos / Sistemas de Lectura Abierta / Complejo de Citocromo b6f / Synechocystis Tipo de estudio: Risk_factors_studies Idioma: En Revista: J Biol Chem Año: 2007 Tipo del documento: Article País de afiliación: Alemania
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Secuencias Repetitivas de Ácidos Nucleicos / Sistemas de Lectura Abierta / Complejo de Citocromo b6f / Synechocystis Tipo de estudio: Risk_factors_studies Idioma: En Revista: J Biol Chem Año: 2007 Tipo del documento: Article País de afiliación: Alemania
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