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Glycine-rich loop of mitochondrial processing peptidase ?-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F10%3A00340832" target="_blank" >RIV/61388971:_____/10:00340832 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Glycine-rich loop of mitochondrial processing peptidase ?-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20

  • Original language description

    Tryptophan fluorescence measurements were used to characterize the local dynamics of the highly conserved glycine-rich loop (GRL) of the mitochondrial processing peptidase (MPP) subunit in the presence of the substrate precursor. Reporter tryptophan residue was introduced into the GRL of the yeast MPP (Y299W) or at a proximal site (Y303W). Timeresolved and steady-state fluorescence spectroscopy demonstrated that for Trp299, the primary contact with the yeast malate dehydrogenase precursor evokes a change of the local GRL mobility. Moreover, time-resolved measurements showed that a functionless MPP with a single-residue deletion in the loop (Y303W/G292) is defective particularly in the primary contact with substrate

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/IAA501110631" target="_blank" >IAA501110631: Evolution and biogenesis of mitochondria-related organelles: hydrogenosomes and mitosomes</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2010

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Molecular Biology

  • ISSN

    0022-2836

  • e-ISSN

  • Volume of the periodical

    396

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    14

  • Pages from-to

  • UT code for WoS article

    000275691500002

  • EID of the result in the Scopus database