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Photosystem II antenna modules CP43 and CP47 do not form a stable 'no reaction centre complex' in the cyanobacterium Synechocystis sp. PCC 6803

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    0561359 - MBÚ 2023 RIV NL eng J - Journal Article
    Bečková, Martina - Sobotka, Roman - Komenda, Josef
    Photosystem II antenna modules CP43 and CP47 do not form a stable 'no reaction centre complex' in the cyanobacterium Synechocystis sp. PCC 6803.
    Photosynthesis Research. Roč. 152, č. 3 (2022), s. 363-371. ISSN 0166-8595. E-ISSN 1573-5079
    R&D Projects: GA ČR(CZ) GX19-29225X
    EU Projects: European Commission(CZ) 854126 - PhotoRedesign
    Institutional support: RVO:61388971
    Keywords : Photosystem II * Photosynthesis * cp43 * cp47 * No reaction centre complex
    OECD category: Plant sciences, botany
    Impact factor: 3.7, year: 2022
    Method of publishing: Open access
    https://link.springer.com/article/10.1007/s11120-022-00896-w

    The repair of photosystem II is a key mechanism that keeps the light reactions of oxygenic photosynthesis functional. During this process, the PSII central subunit D1 is replaced with a newly synthesized copy while the neighbouring CP43 antenna with adjacent small subunits (CP43 module) is transiently detached. When the D2 protein is also damaged, it is degraded together with D1 leaving both the CP43 module and the second PSII antenna module CP47 unassembled. In the cyanobacterium Synechocystis sp. PCC 6803, the released CP43 and CP47 modules have been recently suggested to form a so-called no reaction centre complex (NRC). However, the data supporting the presence of NRC can also be interpreted as a co-migration of CP43 and CP47 modules during electrophoresis and ultracentrifugation without forming a mutual complex. To address the existence of NRC, we analysed Synechocystis PSII mutants accumulating one or both unassembled antenna modules as well as Synechocystis wild-type cells stressed with high light. The obtained results were not compatible with the existence of a stable NRC since each unassembled module was present as a separate protein complex with a mutually similar electrophoretic mobility regardless of the presence of the second module. The non-existence of NRC was further supported by isolation of the His-tagged CP43 and CP47 modules from strains lacking either D1 or D2 and their migration patterns on native gels.
    Permanent Link: https://hdl.handle.net/11104/0334050

     
     
Number of the records: 1  

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