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Philos Trans R Soc Lond B Biol Sci. 2012 Dec 19;367(1608):3466-74. doi: 10.1098/rstb.2012.0064.

Protein kinases and phosphatases involved in the acclimation of the photosynthetic apparatus to a changing light environment.

Author information

1
Departments of Molecular Biology and Plant Biology, University of Geneva, 30 Quai Ernest Ansermet, Geneva 4, Switzerland. jean-david.rochaix@unige.ch

Abstract

Photosynthetic organisms are subjected to frequent changes in light quality and quantity and need to respond accordingly. These acclimatory processes are mediated to a large extent through thylakoid protein phosphorylation. Recently, two major thylakoid protein kinases have been identified and characterized. The Stt7/STN7 kinase is mainly involved in the phosphorylation of the LHCII antenna proteins and is required for state transitions. It is firmly associated with the cytochrome b(6)f complex, and its activity is regulated by the redox state of the plastoquinone pool. The other kinase, Stl1/STN8, is responsible for the phosphorylation of the PSII core proteins. Using a reverse genetics approach, we have recently identified the chloroplast PPH1/TAP38 and PBPC protein phosphatases, which counteract the activity of STN7 and STN8 kinases, respectively. They belong to the PP2C-type phosphatase family and are conserved in land plants and algae. The picture that emerges from these studies is that of a complex regulatory network of chloroplast protein kinases and phosphatases that is involved in light acclimation, in maintenance of the plastoquinone redox poise under fluctuating light and in the adjustment to metabolic needs.

PMID:
23148273
PMCID:
PMC3497069
DOI:
10.1098/rstb.2012.0064
[Indexed for MEDLINE]
Free PMC Article

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