Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases

Vera Bonardi, Paolo Pesaresi, Thomas Becker, Enrico Schleiff, Raik Wagner, Thomas Pfannschmidt, Peter Jahns and Dario Leister ()
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Vera Bonardi: Ludwig-Maximilians-Universität
Paolo Pesaresi: Max-Planck-Institut für Züchtungsforschung
Thomas Becker: Ludwig-Maximilians-Universität
Enrico Schleiff: Ludwig-Maximilians-Universität
Raik Wagner: Friedrich-Schiller-Universität Jena
Thomas Pfannschmidt: Friedrich-Schiller-Universität Jena
Peter Jahns: Heinrich-Heine-Universität Düsseldorf
Dario Leister: Ludwig-Maximilians-Universität

Nature, 2005, vol. 437, issue 7062, 1179-1182

Abstract: Abstract Illumination changes elicit modifications of thylakoid proteins and reorganization of the photosynthetic machinery. This involves, in the short term, phosphorylation of photosystem II (PSII) and light-harvesting (LHCII) proteins. PSII phosphorylation is thought to be relevant for PSII turnover1,2, whereas LHCII phosphorylation is associated with the relocation of LHCII and the redistribution of excitation energy (state transitions) between photosystems3,4. In the long term, imbalances in energy distribution between photosystems are counteracted by adjusting photosystem stoichiometry5,6. In the green alga Chlamydomonas and the plant Arabidopsis, state transitions require the orthologous protein kinases STT7 and STN7, respectively7,8. Here we show that in Arabidopsis a second protein kinase, STN8, is required for the quantitative phosphorylation of PSII core proteins. However, PSII activity under high-intensity light is affected only slightly in stn8 mutants, and D1 turnover is indistinguishable from the wild type, implying that reversible protein phosphorylation is not essential for PSII repair. Acclimation to changes in light quality is defective in stn7 but not in stn8 mutants, indicating that short-term and long-term photosynthetic adaptations are coupled. Therefore the phosphorylation of LHCII, or of an unknown substrate of STN7, is also crucial for the control of photosynthetic gene expression.

Date: 2005
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DOI: 10.1038/nature04016

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