Absence of the psbH gene product destabilizes photosystem II complex and bicarbonate binding on its acceptor side in Synechocystis PCC 6803
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
11856320
DOI
10.1046/j.0014-2956.2001.02693.x
PII: 2693
Knihovny.cz E-zdroje
- MeSH
- fosfoproteiny genetika MeSH
- fosforylace MeSH
- fotosyntetická reakční centra (proteinové komplexy) genetika metabolismus MeSH
- fotosystém II (proteinový komplex) * MeSH
- hydrogenuhličitany metabolismus MeSH
- oxidační stres MeSH
- sinice genetika metabolismus MeSH
- trypsin metabolismus MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- fosfoproteiny MeSH
- fotosyntetická reakční centra (proteinové komplexy) MeSH
- fotosystém II (proteinový komplex) * MeSH
- hydrogenuhličitany MeSH
- photosystem II, psbH subunit MeSH Prohlížeč
- trypsin MeSH
The PsbH protein, a small subunit of the photosystem II complex (PSII), was identified as a 6-kDa protein band in the PSII core and subcore (CP47-D1-D2-cyt b-559) from the wild-type strain of the cyanobacterium Synechocystis PCC 6803. The protein was missing in the D1-D2-cytochrome b-559 complex and also in all PSII complexes isolated from IC7, a mutant lacking the psbH gene. The following properties of PSII in the mutant contrasted with those in wild-type: (a) CP47 was released during nondenaturing electrophoresis of the PSII core isolated from IC7; (b) depletion of CO2 resulted in a reversible decrease of the QA- reoxidation rate in the IC7 cells; (c) light-induced decrease in PSII activity, measured as 2,5-dimethyl-benzoquinone-supported Hill reaction, was strongly dependent on the HCO3- concentration in the IC7 cells; and (d) illumination of the IC7 cells lead to an extensive oxidation, fragmentation and cross-linking of the D1 protein. We did not find any evidence for phosphorylation of the PsbH protein in the wild-type strain. The results showed that in the PSII complex of Synechocystis attachment of CP47 to the D1-D2 heterodimer appears weakened and binding of bicarbonate on the PSII acceptor side is destabilized in the absence of the PsbH protein.
Citace poskytuje Crossref.org
Electron microscopy in structural studies of Photosystem II