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

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.

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Figure 1: Subcellular localization of STN8.
Figure 2: Phosphorylation of thylakoid proteins.
Figure 3: PSII activity and D1 turnover under high-intensity light.
Figure 4: Photosynthetic acclimation and mRNA expression.

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Acknowledgements

We thank A. Biehl, C. Noutsos, A. Dietzmann, B. Eilts and M. Brost for excellent technical assistance; F. Salamini, M. Koornneef and P. Hardy for critical comments on the manuscript; and the Salk Institute for making T-DNA insertion lines publicly available. This work was supported by the European Community (Human Potential Programme (PSICO)) and the Deutsche Forschungsgemeinschaft.

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Correspondence to Dario Leister.

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Complete data sets are deposited at GEO (http://www.ncbi.nlm.nih.gov/geo/) under accession numbers GSE2620–GSE2622. Reprints and permissions information is available at npg.nature.com/reprintsandpermissions. The authors declare no competing financial interests.

Supplementary information

Supplementary Figure 1

Mutations of STN7 and STN8 genes and their effects on transcript accumulation and growth. (PDF 67 kb)

Supplementary Figure 2

Coomassie-staining of a representative protein gel, from which immunoblots displayed in Fig. 2 were derived (PDF 33 kb)

Supplementary Figure 3

Immunoblot analysis of D1 protein upon exposure to high-intensity light. (PDF 48 kb)

Supplementary Figure 4

Phosphorylation of thylakoid proteins during photoinhibition and subsequent recovery. (PDF 36 kb)

Supplementary Figure 5

Quantitation of D1 labelling during pulse-chase measurement of D1 turnover. (PDF 23 kb)

Supplementary Table 1

Pigment composition of leaves from stn7, stn8 and stn7 stn8 plants compared to wild type. (PDF 17 kb)

Supplementary Table 2

Spectroscopic data measured from stn7, stn8, stn7 stn8 and wild-type leaves. (PDF 17 kb)

Supplementary Table 3

Photosynthetic genes with STN7-dependent differential expression in the stn8 mutant. (PDF 11 kb)

Supplementary Data

This file contains the Supplementary Methods and additional references. (DOC 37 kb)

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Bonardi, V., Pesaresi, P., Becker, T. et al. Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases. Nature 437, 1179–1182 (2005). https://doi.org/10.1038/nature04016

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