Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
24313886
DOI
10.1111/tpj.12402
Knihovny.cz E-zdroje
- Klíčová slova
- Hordeum vulgare, PSI-NDH supercomplex, clear native electrophoresis, cyclic electron transport, single particle electron microscopy,
- MeSH
- elektronová mikroskopie MeSH
- ferredoxiny metabolismus MeSH
- fotosystém I - proteinový komplex chemie izolace a purifikace metabolismus MeSH
- ječmen (rod) chemie enzymologie účinky záření MeSH
- listy rostlin chemie enzymologie účinky záření MeSH
- molekulární modely MeSH
- NAD metabolismus MeSH
- NADPH-dehydrogenasa chemie izolace a purifikace metabolismus MeSH
- nativní elektroforéza na polyakrylamidovém gelu MeSH
- oxidace-redukce MeSH
- světlo MeSH
- světlosběrné proteinové komplexy chemie izolace a purifikace metabolismus MeSH
- transport elektronů MeSH
- tylakoidy metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- ferredoxiny MeSH
- fotosystém I - proteinový komplex MeSH
- NAD MeSH
- NADPH-dehydrogenasa MeSH
- světlosběrné proteinové komplexy MeSH
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.
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