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Cyanobacterial thylakoid membrane proteins are reversibly phosphorylated under plastoquinone‐reducing conditions in vitro
Author(s) -
Harrison Michael A.,
Tsinoremas Nicholas F.,
Allen John F.
Publication year - 1991
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 - 10.1016/0014-5793(91)80499-s
Subject(s) - plastoquinone , thylakoid , phosphorylation , in vitro , chemistry , biophysics , photosystem ii , biochemistry , cyanobacteria , protein phosphorylation , membrane , microbiology and biotechnology , chloroplast , biology , photosynthesis , bacteria , genetics , protein kinase a , gene
Reversible, light‐dependent protein phosphorylation was observed in isolated thylakoid membranes of the cyanobacterium Synechococcus 6301. A polypeptide of 15 kDA in particular was phosphorylated under plastoquinone‐reducing conditions and was not phosphorylated under plastoquinone‐oxidising conditions. Phosphorylation and dephosphorylation reactions involving this and several other membrane polypeptides showed sensitivity to inhibitors of protein kinases and phosphatases. Changes in phosphorylation state correlated with changes in low temperature fluorescence emission characteristic or changes in excitation energy distribution between the photosystems. The 15 kDa phosphopolypeptide is likely to be involved directly in light state adaptations in cyanobacteria.