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• W213535818 abstract "Research Article1 December 1993free access Dephosphorylation of photosystem II core proteins is light-regulated in vivo. T.D. Elich T.D. Elich Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center-West, MD 20705-2350. Search for more papers by this author M. Edelman M. Edelman Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center-West, MD 20705-2350. Search for more papers by this author A.K. Mattoo A.K. Mattoo Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center-West, MD 20705-2350. Search for more papers by this author T.D. Elich T.D. Elich Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center-West, MD 20705-2350. Search for more papers by this author M. Edelman M. Edelman Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center-West, MD 20705-2350. Search for more papers by this author A.K. Mattoo A.K. Mattoo Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center-West, MD 20705-2350. Search for more papers by this author Author Information T.D. Elich1, M. Edelman1 and A.K. Mattoo1 1Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center-West, MD 20705-2350. The EMBO Journal (1993)12:4857-4862https://doi.org/10.1002/j.1460-2075.1993.tb06175.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info 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. Previous ArticleNext Article Volume 12Issue 121 December 1993In this issue RelatedDetailsLoading ..." @default.
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• W213535818 title "Dephosphorylation of photosystem II core proteins is light-regulated in vivo." @default.
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