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A mechanism for regulation of chloroplast LHC II kinase by plastoquinol and thioredoxin
Author(s) -
Puthiyaveetil Sujith
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.04.076
Subject(s) - plastoquinone , chloroplast , photosystem , photosystem ii , biophysics , photosystem i , photosynthesis , chemistry , thioredoxin , protein kinase a , microbiology and biotechnology , phosphorylation , biochemistry , biology , enzyme , thylakoid , gene
State transitions are acclimatory responses to changes in light quality in photosynthesis. They involve the redistribution of absorbed excitation energy between photosystems I and II. In plants and green algae, this redistribution is produced by reversible phosphorylation of the chloroplast light harvesting complex II (LHC II). The LHC II kinase is activated by reduced plastoquinone (PQ) in photosystem II‐specific low light. In high light, when PQ is also reduced, LHC II kinase becomes inactivated by thioredoxin. Based on newly identified amino acid sequence features of LHC II kinase and other considerations, a mechanism is suggested for its redox regulation.