Small CAB-like proteins prevent formation of singlet oxygen in the damaged photosystem II complex of the cyanobacterium Synechocystis sp. PCC 6803
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Bacterial Proteins metabolism MeSH
- Chlorophyll metabolism MeSH
- Cytochrome b Group metabolism MeSH
- Photosystem I Protein Complex physiology MeSH
- Photosystem II Protein Complex metabolism physiology MeSH
- Hydroxyl Radical metabolism MeSH
- Cold Temperature MeSH
- Oxidation-Reduction MeSH
- Oxidative Stress MeSH
- Reactive Oxygen Species metabolism MeSH
- Singlet Oxygen metabolism MeSH
- Light MeSH
- Synechocystis metabolism physiology radiation effects MeSH
- Thylakoids metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Chlorophyll MeSH
- cytochrome b559 MeSH Browser
- Cytochrome b Group MeSH
- Photosystem I Protein Complex MeSH
- Photosystem II Protein Complex MeSH
- Hydroxyl Radical MeSH
- Reactive Oxygen Species MeSH
- Singlet Oxygen MeSH
The cyanobacterial small CAB-like proteins (SCPs) are single-helix membrane proteins mostly associated with the photosystem II (PSII) complex that accumulate under stress conditions. Their function is still ambiguous although they are assumed to regulate chlorophyll (Chl) biosynthesis and/or to protect PSII against oxidative damage. In this study, the effect of SCPs on the PSII-specific light-induced damage and generation of singlet oxygen ((1)O(2)) was assessed in the strains of the cyanobacterium Synechocystis sp. PCC 6803 lacking PSI (PSI-less strain) or lacking PSI together with all SCPs (PSI-less/scpABCDE(-) strain). The light-induced oxidative modifications of the PSII D1 protein reflected by a mobility shift of the D1 protein and by generation of a D1-cytochrome b-559 adduct were more pronounced in the PSI-less/scpABCDE(-) strain. This increased protein oxidation correlated with a faster formation of (1)O(2) as detected by the green fluorescence of Singlet Oxygen Sensor Green assessed by a laser confocal scanning microscopy and by electron paramagnetic resonance spin-trapping technique using 2, 2, 6, 6-tetramethyl-4-piperidone (TEMPD) as a spin trap. In contrast, the formation of hydroxyl radicals was similar in both strains. Our results show that SCPs prevent (1)O(2) formation during PSII damage, most probably by the binding of free Chl released from the damaged PSII complexes.
References provided by Crossref.org
The biogenesis and maintenance of PSII: Recent advances and current challenges
Bcl-2△21 and Ac-DEVD-CHO Inhibit Death of Wheat Microspores
Making proteins green; biosynthesis of chlorophyll-binding proteins in cyanobacteria