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Light affects the accessibility of the thylakoid light harvesting complex II (LHCII) phosphorylation site to the membrane protein kinase(s)
Department of Biological Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel.
Department of Biochemistry, Arrhenius Laboratories, Stockholm University, SE-106 91 Stockholm, Sweden.
Department of Biological Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel.
Institute of Botany, Ludwig Maximilians University, D-80638 Münich, Germany.
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2003 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 42, no 3, 728-738 p.Article in journal (Refereed) Published
Abstract [en]

Redox-controlled, reversible phosphorylation of the thylakoid light harvesting complex II (LHCII) regulates its association with photosystems (PS) I or II and thus, energy distribution between the two photosystems (state transition). Illumination of solubilized LHCII enhances exposure of the phosphorylation site at its N-terminal domain to protein kinase(s) and tryptic cleavage in vitro [Zer et al. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 8277-8282]. Here we report that short illumination (5-10 min, 15-30, µmol m-2 s-1) enhances the accessibility of LHCII phosphorylation site to kinase(s) activity also in isolated thylakoids. However, prolonged illumination or higher light intensities (30 min, 80-800 µmol m-2 s-1) prevent phosphorylation of LHCII in the isolated membranes as well as in vivo, although redox-dependent protein kinase activity persists in the illuminated thylakoids toward exogenous solubilized LHCII. This phenomenon, ascribed to light-induced inaccessibility of the phosphorylation site to the protein kinase(s), affects in a similar way the accessibility of thylakoid LHCII N-terminal domain to tryptic cleavage. The illumination effect is not redox related, decreases linearly with temperature from 25 to 5°C and may be ascribed to light-induced conformational changes in the complex causing lateral aggregation of dephosphorylated LHCII bound to and/or dissociated from PSII. The later state occurs under conditions allowing turnover of the phospho-LHCII phosphate. The light-induced inaccessibility of LHCII to the membrane-bound protein kinase reverses readily in darkness only if induced under LHCII-phosphate turnover conditions. Thus, phosphorylation prevents irreversible light-induced conformational changes in LHCII allowing lateral migration of the complex and the related state transition process.

Place, publisher, year, edition, pages
2003. Vol. 42, no 3, 728-738 p.
National Category
Natural Sciences
URN: urn:nbn:se:liu:diva-46746DOI: 10.1021/bi020451rOAI: diva2:267642
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2012-01-07

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Andersson, B.
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Department of Physics, Chemistry and BiologyThe Institute of Technology
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