"000330907900007" . "clear native electrophoresis, Hordeum vulgare, single particle electron microscopy, PSI-NDH supercomplex, cyclic electron transport"@en . "Kou\u0159il, Roman" . . . "15310" . . "Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex"@en . "Plant Journal" . "Il\u00EDk, Petr" . . "Lenobel, Ren\u00E9" . "7"^^ . "GB - Spojen\u00E9 kr\u00E1lovstv\u00ED Velk\u00E9 Brit\u00E1nie a Severn\u00EDho Irska" . . "47848" . "8"^^ . "77" . . "Strouhal, Ond\u0159ej" . "[BCB2F93D7528]" . "10.1111/tpj.12402" . "4" . . "Boekema, Egbert" . "0960-7412" . . . . "Chamr\u00E1d, Ivo" . . "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." . "Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex" . "Nosek, Luk\u00E1\u0161" . . . "http://onlinelibrary.wiley.com/doi/10.1111/tpj.12402/pdf" . "RIV/61989592:15310/14:33150462" . "9"^^ . "RIV/61989592:15310/14:33150462!RIV15-MSM-15310___" . "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."@en . . . . "Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex"@en . . . "P(EE2.3.20.0057), P(GA13-28093S), P(LO1204), S" . . . . "\u0160ebela, Marek" . . . "Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex" . . . .