Structural characterization of a complex of photosystem I and light-harvesting complex II of Arabidopsis thaliana

被引:150
作者
Kouril, R
Zygadlo, A
Arteni, AA
de Wit, CD
Dekker, JP
Jensen, PE
Scheller, HV
Boekema, EJ
机构
[1] Univ Groningen, GBB, Dept Biophys Chem, NL-9747 AG Groningen, Netherlands
[2] Royal Vet & Agr Univ, Dept Plant Biol, Plant Biol Lab, DK-1871 Frederiksberg, Denmark
[3] Vrije Univ Amsterdam, Fac Sci, Div Phys & Astron, NL-1081 HV Amsterdam, Netherlands
关键词
D O I
10.1021/bi051097a
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
Chloroplasts are central to the provision of energy for green plants. Their photosynthetic membrane consists of two major complexes converting sunlight: photosystem I (PSI) and photosystent 11 (PSII). The energy flow toward both photosystems is regulated by light-harvesting complex 11 (LHCII), which after phosphorylation can move from PSIT to PSI in the so-called state I to state 2 transition and can move back to PSII after dephosphorylation. To investigate the changes of PSI and PSII during state transitions, we studied the structures and frequencies of all major membrane complexes from Arabidopsis thaliana chloroplasts at conditions favoring either state 1 or state 2. We solubilized thylakoid membranes with digitonin and analyzed the complete set of complexes immediately after solubilization by electron microscopy and image analysis. Classification indicated the presence of a PSI-LHCII supercomplex consisting of one PSI-LHCI complex and one LHCII trimer, which was more abundant in state 2 conditions. The presence of LHCII was confirmed by excitation spectra of the PSI emission of membranes in state I or state 2. The PSI-LHCII complex could be averaged with a resolution of 16 A, showing that LHCII has a specific binding site at the PSI-A, -H, -L, and -K subunits.
引用
收藏
页码:10935 / 10940
页数:6
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