caa a22 4500 467894949 CHVBK 20180406152800.0 cr unu---uuuuu 170328e20061101xx s 000 0 eng 10.1007/s11103-006-9044-8 doi (NATIONALLICENCE)springer-10.1007/s11103-006-9044-8 State transitions revisited—a buffering system for dynamic low light acclimation of Arabidopsis [Elektronische Daten] [Tikkanen Mikko, Piippo Mirva, Suorsa Marjaana, Sirpiö Sari, Mulo Paula, Vainonen Julia, Vener Alexander V, Allahverdiyeva Yagut, Aro Eva-Mari] The mobile part of the light-harvesting chlorophyll (chl) a/b protein complex (LHCII), composed of the Lhcb1 and Lhcb2 proteins, is the basic unit of chloroplast state transitions—the short term tuning system in balancing the excitation energy between Photosystem (PS) II and PSI. State transitions are catalysed by the thylakoid associated STN7 kinase, and we show here that besides the phosphorylation of the Lhcb1 and Lhcb2 proteins, also the phosphorylation of Lhcb4.2 (CP29) is under the control of the STN7 kinase. Upon growth of Arabidopsis WT and stn7 mutant plants under low and moderate light conditions, the WT plants favoured state 2 whereas stn7 was locked in state 1. The lack of the STN7 kinase and state transitions in stn7 also modified the thylakoid protein contents upon long-term low light acclimation resulting, for example, in low Lhcb1 and in elevated Lhca1 and Lhca2 protein amounts as compared to WT. Adjustments of thylakoid protein contents probably occurred at post-transcriptional level since the DNA microarray experiments from each growth condition did not reveal any significant differences between stn7 and WT transcriptomes. The resulting high Lhcb2/Lhcb1 ratio in stn7 upon growth at low light was accompanied by lower capacity for NPQ than in WT. On the contrary, higher amounts of PsbS in stn7 under moderate and high light growth conditions resulted in higher NPQ compared to WT and consequently also in a protection of PSII against photoinhibition. STN7 kinase and the state transitions are suggested to have a physiological significance for dynamic acclimation to low but fluctuating growth light conditions. They are shown to function as a buffering system upon short high light illumination peaks by shifting the thylakoids from state 2 to state 1 and thereby down regulating the induction of stress-responsive genes, a likely result from transient over-reduction of PSI acceptors. Springer Science+Business Media B.V., 2006 Arabidopsis nationallicence Light acclimation nationallicence STN7 kinase nationallicence Thylakoid protein phosphorylation nationallicence chl : chlorophyll nationallicence F v/ F m : photochemical efficiency of PSII nationallicence HSP : heat shock protein nationallicence LHCII : light harvesting chlorophyll a/b protein complex nationallicence NPQ : non-photochemical energy quenching nationallicence PSI : photosystem I nationallicence PSII : photosystem II nationallicence Mikko Tikkanen Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut Mirva Piippo Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut Marjaana Suorsa Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut Sari Sirpiö Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut Paula Mulo Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut Julia Vainonen Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut Alexander V Vener Division of Cell Biology, Linkoping University, SE-581 85, Linkoping, Sweden aut Yagut Allahverdiyeva Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut Eva-Mari Aro Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut Plant Molecular Biology Kluwer Academic Publishers 62/4-5(2006-11-01), 779-793 0167-4412 62:4-5<779 2006 62 11103 https://doi.org/10.1007/s11103-006-9044-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11103-006-9044-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Mikko Tikkanen Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut NATIONALLICENCE 700 1- Mirva Piippo Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut NATIONALLICENCE 700 1- Marjaana Suorsa Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut NATIONALLICENCE 700 1- Sari Sirpiö Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut NATIONALLICENCE 700 1- Paula Mulo Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut NATIONALLICENCE 700 1- Julia Vainonen Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut NATIONALLICENCE 700 1- Alexander V Vener Division of Cell Biology, Linkoping University, SE-581 85, Linkoping, Sweden aut NATIONALLICENCE 700 1- Yagut Allahverdiyeva Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut NATIONALLICENCE 700 1- Eva-Mari Aro Plant Physiology and Molecular Biology, Department of Biology, University of Turku, FIN-20014, Turku, Finland aut NATIONALLICENCE 773 0- Plant Molecular Biology Kluwer Academic Publishers 62/4-5(2006-11-01), 779-793 0167-4412 62:4-5<779 2006 62 11103 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer