The FtsH protease slr0228 is important for quality control of photosystem II in the thylakoid membrane of Synechocystis sp. PCC 6803
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
16286465
DOI
10.1074/jbc.m503852200
PII: S0021-9258(19)47558-3
Knihovny.cz E-resources
- MeSH
- Electrophoresis, Gel, Two-Dimensional MeSH
- Biochemical Phenomena MeSH
- Biochemistry MeSH
- Cell Membrane metabolism MeSH
- Time Factors MeSH
- Chloroplasts metabolism MeSH
- Cytoplasm metabolism MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Epitopes chemistry MeSH
- Photosystem II Protein Complex metabolism MeSH
- Genotype MeSH
- Immunoblotting MeSH
- Microscopy, Confocal MeSH
- Metalloendopeptidases chemistry physiology MeSH
- Mutation, Missense MeSH
- Mutation MeSH
- Plasmids metabolism MeSH
- Peptide Hydrolases chemistry MeSH
- Light MeSH
- Synechocystis metabolism MeSH
- Thylakoids metabolism MeSH
- Protein Binding MeSH
- Green Fluorescent Proteins chemistry metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Epitopes MeSH
- Photosystem II Protein Complex MeSH
- Metalloendopeptidases MeSH
- Peptide Hydrolases MeSH
- Green Fluorescent Proteins MeSH
The cyanobacterium Synechocystis sp. PCC 6803 contains four members of the FtsH protease family. One of these, FtsH (slr0228), has been implicated recently in the repair of photodamaged photosystem II (PSII) complexes. We have demonstrated here, using a combination of blue native PAGE, radiolabeling, and immunoblotting, that FtsH (slr0228) is required for selective replacement of the D1 reaction center subunit in both wild type PSII complexes and in PSII subcomplexes lacking the PSII chlorophyll a-binding subunit CP43. To test whether FtsH (slr0228) has a more general role in protein quality control in vivo, we have studied the synthesis and degradation of PSII subunits in wild type and in defined insertion and missense mutants incapable of proper assembly of the PSII holoenzyme. We discovered that, when the gene encoding FtsH (slr0228) was disrupted in these strains, the overall level of assembly intermediates and unassembled PSII proteins markedly increased. Pulse-chase experiments showed that this was due to reduced rates of degradation in vivo. Importantly, analysis of epitope-tagged and green fluorescent protein-tagged strains revealed that slr0228 was present in the thylakoid and not the cytoplasmic membrane. Overall, our results show that FtsH (slr0228) plays an important role in controlling the removal of PSII subunits from the thylakoid membrane and is not restricted to selective D1 turnover.
References provided by Crossref.org
The biogenesis and maintenance of PSII: Recent advances and current challenges
The Role of FtsH Complexes in the Response to Abiotic Stress in Cyanobacteria
