The cyanobacterial homologue of HCF136/YCF48 is a component of an early photosystem II assembly complex and is important for both the efficient assembly and repair of photosystem II in Synechocystis sp. PCC 6803
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
Biotechnology and Biological Sciences Research Council - United Kingdom
PubMed
18550538
DOI
10.1074/jbc.m801917200
PII: S0021-9258(20)74771-X
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins genetics physiology MeSH
- Cysteine metabolism MeSH
- Cytochrome b Group genetics isolation & purification MeSH
- Photosystem II Protein Complex genetics isolation & purification physiology MeSH
- Membrane Proteins genetics physiology MeSH
- Methionine metabolism MeSH
- Polarography MeSH
- Polymerase Chain Reaction MeSH
- Sulfur Radioisotopes MeSH
- Cyanobacteria physiology MeSH
- Synechocystis physiology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Cysteine MeSH
- cytochrome b559 MeSH Browser
- Cytochrome b Group MeSH
- Photosystem II Protein Complex MeSH
- Membrane Proteins MeSH
- Methionine MeSH
- Sulfur Radioisotopes MeSH
The role of the slr2034 (ycf48) gene product in the assembly and repair of photosystem II (PSII) has been studied in the cyanobacterium Synechocystis PCC 6803. YCF48 (HCF136) is involved in the assembly of Arabidopsis thaliana PSII reaction center (RC) complexes but its mode of action is unclear. We show here that YCF48 is a component of two cyanobacterial PSII RC-like complexes in vivo and is absent in larger PSII core complexes. Interruption of ycf48 slowed the formation of PSII complexes in wild type, as judged from pulse-labeling experiments, and caused a decrease in the final level of PSII core complexes in wild type and a marked reduction in the levels of PSII assembly complexes in strains lacking either CP43 or CP47. Absence of YCF48 also led to a dramatic decrease in the levels of the COOH-terminal precursor (pD1) and the partially processed form, iD1, in a variety of PSII mutants and only low levels of unassembled mature D1 were observed. Yeast two-hybrid analyses using the split ubiquitin system showed an interaction of YCF48 with unassembled pD1 and, to a lesser extent, unassembled iD1, but not with unassembled mature D1 or D2. Overall our results indicate a role for YCF48 in the stabilization of newly synthesized pD1 and in its subsequent binding to a D2-cytochrome b559 pre-complex, also identified in this study. Besides a role in assembly, we show for the first time that YCF48 also functions in the selective replacement of photodamaged D1 during PSII repair.
References provided by Crossref.org
The biogenesis and maintenance of PSII: Recent advances and current challenges
High-light-inducible proteins HliA and HliB: pigment binding and protein-protein interactions
Chlorophyll f synthesis by a super-rogue photosystem II complex