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Dephosphorylation of photosystem II core proteins is light‐regulated in vivo.
Author(s) -
Elich T.D.,
Edelman M.,
Mattoo A.K.
Publication year - 1993
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1993.tb06175.x
Subject(s) - dephosphorylation , cytochrome b6f complex , biology , photosystem ii , photosystem i , biophysics , in vivo , phosphorylation , thylakoid , biochemistry , chloroplast , phosphatase , photosynthesis , microbiology and biotechnology , gene
A number of photosystem II (PSII)‐associated proteins, including D1, D2, CP43 and LHCII, are phosphorylated post‐translationally by a membrane‐bound, redox‐regulated kinase activity. In vitro studies have demonstrated that these proteins can be dephosphorylated by membrane‐bound phosphatase activity, reportedly insensitive to light or redox control. We demonstrate here that the PSII core proteins, D1, D2 and CP43, undergo light‐stimulated, linear electron‐transport‐independent dephosphorylation in vivo. The in vivo dephosphorylation of D1 was characterized further and shown to depend upon light intensity, and to occur throughout the visible light spectrum with characteristics most consistent with light absorption by chlorophyll. PSII core protein dephosphorylation in vivo was stimulated by photosystem I (PSI)‐specific far‐red light, and inhibited by 2,5‐dibromo‐3‐methyl‐6‐isopropyl‐p‐benzoquinone, an inhibitor of plastoquinol oxidation by the cytochrome b6f complex. Based on these findings, we propose that PSI excitation is involved in regulating dephosphorylation of PSII core proteins in vivo.