Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
24313886
DOI
10.1111/tpj.12402
Knihovny.cz E-resources
- Keywords
- Hordeum vulgare, PSI-NDH supercomplex, clear native electrophoresis, cyclic electron transport, single particle electron microscopy,
- MeSH
- Microscopy, Electron MeSH
- Ferredoxins metabolism MeSH
- Photosystem I Protein Complex chemistry isolation & purification metabolism MeSH
- Hordeum chemistry enzymology radiation effects MeSH
- Plant Leaves chemistry enzymology radiation effects MeSH
- Models, Molecular MeSH
- NAD metabolism MeSH
- NADPH Dehydrogenase chemistry isolation & purification metabolism MeSH
- Native Polyacrylamide Gel Electrophoresis MeSH
- Oxidation-Reduction MeSH
- Light MeSH
- Light-Harvesting Protein Complexes chemistry isolation & purification metabolism MeSH
- Electron Transport MeSH
- Thylakoids metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Ferredoxins MeSH
- Photosystem I Protein Complex MeSH
- NAD MeSH
- NADPH Dehydrogenase MeSH
- Light-Harvesting Protein Complexes 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.
References provided by Crossref.org
Unique structural attributes of the PSI-NDH supercomplex in Physcomitrium patens
PSI of the Colonial Alga Botryococcus braunii Has an Unusually Large Antenna Size
Unique organization of photosystem II supercomplexes and megacomplexes in Norway spruce
