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Structural and mutational analysis of band 7 proteins in the cyanobacterium Synechocystis sp. strain PCC 6803
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SYSNO ASEP 0334815 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Structural and mutational analysis of band 7 proteins in the cyanobacterium Synechocystis sp. strain PCC 6803 Title Strukturní a mutační analýza proteinů pásu 7 v sinici Synechocystis sp. strain PCC 6803 Author(s) Boehm, M. (GB)
Nield, J. (GB)
Zhang, P. (FI)
Aro, E.-M. (FI)
Komenda, Josef (MBU-M) RID, ORCID
Nixon, P. J. (GB)Source Title Journal of Bacteriology. - : American Society for Microbiology - ISSN 0021-9193
Roč. 191, č. 20 (2009), s. 6425-6435Number of pages 11 s. Language eng - English Country US - United States Keywords BLUE NATIVE ELECTROPHORESIS ; PHOTOSYSTEM-II COMPLEX ; COLI PLASMA-MEMBRANE Subject RIV EE - Microbiology, Virology R&D Projects IAA400200801 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000270227500027 DOI 10.1128/JB.00644-09 Annotation Band 7 proteins are integral membrane proteins that play important physiological roles in eukaryotes but are poorly characterized in bacteria. The study of these proteins in the cyanobacterium Synechocystis sp. strain PCC 6803 revealed that none of the five band 7 proteins (Slr1106, Slr1128, Slr1768, Sll0815, and Sll1021) was essential for growth under a range of conditions. Accumulation of the major photosynthetic complexes in the thylakoid membrane and repair of the photosystem II complex were similar in the wild type and in a quadruple mutant. All band 7 proteins were detected in the form of large complexes and protein Slr1128has a ring-like structure with an approximate diameter of 16 nm when visualized by negative stain electron microscopy Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2010
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