Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex

被引:73
作者
Kouril, Roman [1 ]
Strouhal, Ondrej [1 ]
Nosek, Lukas [1 ]
Lenobel, Rene [2 ]
Chamrad, Ivo [2 ]
Boekema, Egbert J. [3 ]
Sebela, Marek [2 ]
Ilik, Petr [1 ]
机构
[1] Palacky Univ, Fac Sci, Dept Biophys, Ctr Reg Hana Biotechnol & Agr Res, Olomouc 78371, Czech Republic
[2] Palacky Univ, Fac Sci, Ctr Reg Hana Biotechnol & Agr Res, Dept Prot Biochem & Prote, Olomouc 78371, Czech Republic
[3] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Electron Microscopy Grp, NL-9747 AG Groningen, Netherlands
关键词
clear native electrophoresis; Hordeum vulgare; single particle electron microscopy; PSI-NDH supercomplex; cyclic electron transport; CYCLIC ELECTRON FLOW; NADH DEHYDROGENASE; RESPIRATORY COMPLEX; NDHB GENE; TOBACCO; IDENTIFICATION; PHOTOSYNTHESIS; SEPARATION; BINDING; LHCA5;
D O I
10.1111/tpj.12402
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Cyclic electron transport (CET) around photosystem I (PSI) plays an important role in balancing the ATP/NADPH ratio and the photoprotection of plants. The NAD(P)H dehydrogenase complex (NDH) has a key function in one of the CET pathways. Current knowledge indicates that, in order to fulfill its role in CET, the NDH complex needs to be associated with PSI; however, until now there has been no direct structural information about such a supercomplex. Here we present structural data obtained for a plant PSI-NDH supercomplex. Electron microscopy analysis revealed that in this supercomplex two copies of PSI are attached to one NDH complex. A constructed pseudo-atomic model indicates asymmetric binding of two PSI complexes to NDH and suggests that the low-abundant Lhca5 and Lhca6 subunits mediate the binding of one of the PSI complexes to NDH. On the basis of our structural data, we propose a model of electron transport in the PSI-NDH supercomplex in which the association of PSI to NDH seems to be important for efficient trapping of reduced ferredoxin by NDH.
引用
收藏
页码:568 / 576
页数:9
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