During State 1 to State 2 Transition in Arabidopsis thaliana, the Photosystem II Supercomplex Gets Phosphorylated but Does Not Disassemble

被引:57
作者
Wientjes, Emilie [1 ]
Drop, Bartlomiej [1 ]
Kouril, Roman [2 ,3 ]
Boekema, Egbert J. [2 ]
Croce, Roberta [1 ]
机构
[1] Vrije Univ Amsterdam, Dept Phys & Astron, Fac Sci, NL-1081 HV Amsterdam, Netherlands
[2] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Fac Math & Nat Sci, NL-9747 AG Groningen, Netherlands
[3] Palacky Univ, Dept Biophys, Fac Sci, Ctr Reg Hana Biotechnol & Agr Res, Olomouc 78371, Czech Republic
基金
欧洲研究理事会;
关键词
Photosynthesis; Photosystem II; Plant; Plant Biochemistry; Protein Phosphorylation; State Transitions; Supramolecular Organization; LIGHT-HARVESTING COMPLEX; EXCITATION-ENERGY DISTRIBUTION; PROTEIN-PHOSPHORYLATION; MEMBRANE ORGANIZATION; CHARGE SEPARATION; QUANTUM YIELD; ANTENNA; PHOTOSYNTHESIS; FLUORESCENCE; DYNAMICS;
D O I
10.1074/jbc.M113.511691
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Background: State transition balances the excitation pressure between the two photosystems of plants. Results: The organization of photosystem II supercomplexes and megacomplexes is the same in state 1 and state 2. Conclusion: Phosphorylation is not sufficient to induce the disassembly of the supercomplexes. Significance: This work helps to understand how plants optimize light harvesting under ever changing light conditions. Plants are exposed to continuous changes in light quality and quantity that challenge the performance of the photosynthetic apparatus and have evolved a series of mechanisms to face this challenge. In this work, we have studied state transitions, the process that redistributes the excitation pressure between photosystems I and II (PSI/PSII) by the reversible association of LHCII, the major antenna complex of higher plants, with either one of them upon phosphorylation/dephosphorylation. By combining biochemical analysis and electron microscopy, we have studied the effect of state transitions on the composition and organization of photosystem II in Arabidopsis thaliana. Two LHCII trimers (called trimers M and S) are part of the PSII supercomplex, whereas up to two more are loosely associated with PSII in state 1 in higher plants (called extra trimers). Here, we show that the LHCII from the extra pool migrates to PSI in state 2, thus leaving the PSII supercomplex and the semicrystalline PSII arrays intact. In state 2, not only is the mobile LHCII phosphorylated, but also the LHCII in the PSII supercomplexes. This demonstrates that PSII phosphorylation is not sufficient for disconnecting LHCII trimers S and M from PSII and for their migration to PSI.
引用
收藏
页码:32821 / 32826
页数:6
相关论文
共 48 条
[1]  
Allen JF, 2000, PHILOS T R SOC B, V355, P1351, DOI 10.1098/rstb.2000.0697
[2]   HOW DOES PROTEIN-PHOSPHORYLATION REGULATE PHOTOSYNTHESIS [J].
ALLEN, JF .
TRENDS IN BIOCHEMICAL SCIENCES, 1992, 17 (01) :12-17
[3]   CHLOROPLAST PROTEIN-PHOSPHORYLATION COUPLES PLASTOQUINONE REDOX STATE TO DISTRIBUTION OF EXCITATION-ENERGY BETWEEN PHOTOSYSTEMS [J].
ALLEN, JF ;
BENNETT, J ;
STEINBACK, KE ;
ARNTZEN, CJ .
NATURE, 1981, 291 (5810) :25-29
[4]   Molecular recognition in thylakoid structure and function [J].
Allen, JF ;
Forsberg, J .
TRENDS IN PLANT SCIENCE, 2001, 6 (07) :317-326
[5]   PROTEIN-PHOSPHORYLATION IN REGULATION OF PHOTOSYNTHESIS [J].
ALLEN, JF .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1098 (03) :275-335
[6]   Discrete Redox Signaling Pathways Regulate Photosynthetic Light-Harvesting and Chloroplast Gene Transcription [J].
Allen, John F. ;
Santabarbara, Stefano ;
Allen, Carol A. ;
Puthiyaveetil, Sujith .
PLOS ONE, 2011, 6 (10)
[7]   CHANGES IN THE ORGANIZATION OF STROMA MEMBRANES INDUCED BY INVIVO STATE-1-STATE-2 TRANSITION [J].
BASSI, R ;
GIACOMETTI, GM ;
SIMPSON, DJ .
BIOCHIMICA ET BIOPHYSICA ACTA, 1988, 935 (02) :152-165
[8]   A SUPRAMOLECULAR LIGHT-HARVESTING COMPLEX FROM CHLOROPLAST PHOTOSYSTEM-II MEMBRANES [J].
BASSI, R ;
DAINESE, P .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 204 (01) :317-326
[9]   State transitions and light adaptation require chloroplast thylakoid protein kinase STN7 [J].
Bellafiore, S ;
Barneche, F ;
Peltier, G ;
Rochaix, JD .
NATURE, 2005, 433 (7028) :892-895
[10]   PROTEIN-PHOSPHORYLATION IN GREEN PLANT CHLOROPLASTS [J].
BENNETT, J .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1991, 42 :281-311