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Supercomplexes of plant photosystem I with cytochrome b6f, light-harvesting complex II and NDH

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F17%3A73579337" target="_blank" >RIV/61989592:15310/17:73579337 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.sciencedirect.com/science/article/pii/S0005272816306491" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0005272816306491</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bbabio.2016.10.006" target="_blank" >10.1016/j.bbabio.2016.10.006</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Supercomplexes of plant photosystem I with cytochrome b6f, light-harvesting complex II and NDH

  • Original language description

    Photosystem I (PSI) is a pigment-protein complex required for the light-dependent reactions of photosynthesis and participates in light-harvesting and redox-driven chloroplast metabolism. Assembly of PSI into supercomplexes with light harvesting complex (LHC) II, cytochrome b6f (Cytb6f) or NAD(P)H dehydrogenase complex (NDH) has been proposed as a means for regulating photosynthesis. However, structural details about the binding positions in plant PSI are lacking. We analyzed large data sets of electron microscopy single particle projections of supercomplexes obtained from the stroma membrane of Arabidopsis thaliana. By single particle analysis, we established the binding position of Cytb6f at the antenna side of PSI. The rectangularshaped Cytb6f dimer binds at the side where Lhca1 is located. The complex binds with its short side rather than its long side to PSI,which may explainwhy these supercomplexes are difficult to purify and easily disrupted. Refined analysis of the interaction between PSI and the NDH complex indicates that in total up to 6 copies of PSI can arrangewith one NDH complex. Most PSI-NDH supercomplexes appeared to have 1–3 PSI copies associated. Finally, the PSI-LHCII supercomplex was found to bind an additional LHCII trimer at two positions on the LHCI side in Arabidopsis. The organization of PSI, either in a complexwith NDHor with Cytb6f,may improve regulation of electron transport by the control of binding partners and distances in small domains.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

    <a href="/en/project/LO1204" target="_blank" >LO1204: Sustainable development of research in the Centre of the Region Haná</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2017

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biochimica et Biophysica Acta - Bioenergetics

  • ISSN

    0005-2728

  • e-ISSN

  • Volume of the periodical

    1858

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    9

  • Pages from-to

    12-20

  • UT code for WoS article

    000390626500003

  • EID of the result in the Scopus database