Details
| Original language | English |
|---|---|
| Pages (from-to) | 1179-82 |
| Number of pages | 4 |
| Journal | NATURE |
| Volume | 437 |
| Issue number | 7062 |
| Publication status | Published - 20 Oct 2005 |
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 turnover, whereas LHCII phosphorylation is associated with the relocation of LHCII and the redistribution of excitation energy (state transitions) between photosystems. In the long term, imbalances in energy distribution between photosystems are counteracted by adjusting photosystem stoichiometry. In the green alga Chlamydomonas and the plant Arabidopsis, state transitions require the orthologous protein kinases STT7 and STN7, respectively. 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.
Keywords
- Acclimatization/physiology, Arabidopsis/enzymology, Arabidopsis Proteins/genetics, Light-Harvesting Protein Complexes/metabolism, Mutation/genetics, Phosphorylation, Photosynthesis/physiology, Photosystem II Protein Complex/genetics, Protein Kinases/genetics, Protein-Serine-Threonine Kinases
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In: NATURE, Vol. 437, No. 7062, 20.10.2005, p. 1179-82.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases
AU - Bonardi, Vera
AU - Pesaresi, Paolo
AU - Becker, Thomas
AU - Schleiff, Enrico
AU - Wagner, Raik
AU - Pfannschmidt, Thomas
AU - Jahns, Peter
AU - Leister, Dario
N1 - Funding information: 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.
PY - 2005/10/20
Y1 - 2005/10/20
N2 - 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 turnover, whereas LHCII phosphorylation is associated with the relocation of LHCII and the redistribution of excitation energy (state transitions) between photosystems. In the long term, imbalances in energy distribution between photosystems are counteracted by adjusting photosystem stoichiometry. In the green alga Chlamydomonas and the plant Arabidopsis, state transitions require the orthologous protein kinases STT7 and STN7, respectively. 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.
AB - 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 turnover, whereas LHCII phosphorylation is associated with the relocation of LHCII and the redistribution of excitation energy (state transitions) between photosystems. In the long term, imbalances in energy distribution between photosystems are counteracted by adjusting photosystem stoichiometry. In the green alga Chlamydomonas and the plant Arabidopsis, state transitions require the orthologous protein kinases STT7 and STN7, respectively. 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.
KW - Acclimatization/physiology
KW - Arabidopsis/enzymology
KW - Arabidopsis Proteins/genetics
KW - Light-Harvesting Protein Complexes/metabolism
KW - Mutation/genetics
KW - Phosphorylation
KW - Photosynthesis/physiology
KW - Photosystem II Protein Complex/genetics
KW - Protein Kinases/genetics
KW - Protein-Serine-Threonine Kinases
U2 - 10.1038/nature04016
DO - 10.1038/nature04016
M3 - Article
C2 - 16237446
VL - 437
SP - 1179
EP - 1182
JO - NATURE
JF - NATURE
SN - 0028-0836
IS - 7062
ER -