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Plant Physiol. 2011 Dec;157(4):2102-7. doi: 10.1104/pp.111.187328. Epub 2011 Oct 5.

The phosphorylation status of the chloroplast protein kinase STN7 of Arabidopsis affects its turnover.

Author information

1
Department of Molecular Biology, University of Geneva, 1211 Geneva, Switzerland.

Abstract

The chloroplast serine-threonine protein kinase STN7 of Arabidopsis (Arabidopsis thaliana) is required for the phosphorylation of the light-harvesting system of photosystem II and for state transitions, a process that allows the photosynthetic machinery to balance the light excitation energy between photosystem II and photosystem I and thereby to optimize the photosynthetic yield. Because the STN7 protein kinase of Arabidopsis is known to be phosphorylated at four serine-threonine residues, we have changed these residues by site-directed mutagenesis to alanine (STN7-4A) or aspartic acid (STN7-4D) to assess the role of these phosphorylation events. The corresponding mutants were still able to phosphorylate the light-harvesting system of photosystem II and to perform state transitions. Moreover, we noticed a marked decrease in the level of the STN7 kinase in the wild-type strain under prolonged state 1 conditions that no longer occurs in the STN7-4D mutant. The results suggest a possible role of phosphorylation of the STN7 kinase in regulating its turnover.

PMID:
21976483
PMCID:
PMC3327173
DOI:
10.1104/pp.111.187328
[Indexed for MEDLINE]
Free PMC Article

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