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Alexander V. Vener Linköping University
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aleve{at}ibk.liu.se Alexander V. Vener
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Response to the letter by D. Leister The research works cited in the references 11-15 represent solid data obtained by diverse experimental techniques and demonstrating involvement of protein phosphorylation in regulation of PSII repair cycle. The paper published in October 2005 (Nature 437:1179-1182)claims the opposite on the basis of the the authors suggestion that PSII proteins are not phosphotylated in Arabidopsis mutants lacking STN7 and STN8 protein kinases. However, such a suggestion can not be right because D1, D2, CP43 and PsbH proteins of PSII have been found phosphorylated in vivo in the STN7 and STN8 deficient mutants by immunological and mass spectrometric methods (Bellafiore et al. Nature 2005, 433, 892-895; Vainonen et al. JBC 2005, 280, 33679-33686). Alexander V. Vener |
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Dario Leister, Professor of Botany University of Munich, Paolo Pesaresi, Vera Bonardi
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leister{at}lrz.uni-muenchen.de Dario Leister, et al.
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It was recently shown and published in October 2005 (Nature 437:1179- 1182) that reversible D1 protein phosphorylation is not essential for PSII repair in the flowering plant Arabidopsis thaliana. In this context (see critical passages of this MCP paper by Turkina et al. below) one would wish a better knowledge of the literature by the authors, as well as by the involved editor(s) and reviewers. On behalf of Paolo Pesaresi, Vera Bonardi and myself Dario Leister Introduction: Reversible phosphorylation of the PSII reaction center proteins has been found essential for the maintenance of active PSII under high light stress (11-13). Particularly, dephosphorylation of the lightdamaged D1 protein, a central functional subunit of the PSII reaction center, is required for its degradation and replacement (13-15). Discussion: The repair cycle of plant PSII under high light includes lateral membrane migration of phosphorylated PSII dimers from granal to stromal thylakoids, their dissociation and stepwise dephosphorylation of CP43, D2 and D1, resulting in exposure of photodamaged D1 for digestion by proteases (12, 13). Dephosphorylation of the lightdamaged D1 protein controls its degradation and substitution by a newly synthesized polypeptide (13-15). |
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