Photosystem II antenna modules CP43 and CP47 do not form a stable 'no reaction centre complex' in the cyanobacterium Synechocystis sp. PCC 6803
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články
Grantová podpora
854126
European Research Council - International
61388971
Akademie Věd České Republiky
19-29225X
Grantová Agentura České Republiky
854126
European Research Council - International
PubMed
35015206
PubMed Central
PMC9458580
DOI
10.1007/s11120-022-00896-w
PII: 10.1007/s11120-022-00896-w
Knihovny.cz E-zdroje
- Klíčová slova
- CP43, CP47, No reaction centre complex, Photosynthesis, Photosystem II,
- MeSH
- bakteriální proteiny genetika metabolismus MeSH
- fotosystém II - proteinový komplex metabolismus MeSH
- kyslík metabolismus MeSH
- Synechocystis * genetika metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- fotosystém II - proteinový komplex MeSH
- kyslík MeSH
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.
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