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Inactivation of colicin Y by intramembrane helixhelix interaction with its immunity protein

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F08%3A00027657" target="_blank" >RIV/00216224:14310/08:00027657 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388971:_____/08:00320823

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    Inactivation of colicin Y by intramembrane helixhelix interaction with its immunity protein

  • Original language description

    Construction of hybrids between colicins U and Y and mutagenesis of colicin Y gene (cya) revealed amino acid residues important for interactions between colicin Y and its cognate immunity protein (Cyi). Four such residues (I578, T582, Y586, and V590) were found in helices 8 and 9 of the colicin Y pore forming domain. To verify the importance of these residues, the corresponding amino acids in the colicin B protein were mutated to the residues present in colicin Y. An E. coli strain with cloned colicin Yimmunity gene (cyi) inactivated this mutant but not the wildtype colicin B. In addition, interacting amino acid pairs in Cya and Cyi were identified using a set of Cyi point mutant strains. These data are consistent with antiparallel helix-helix interactions between Cyi helix T3 and Cya helix 8 of the pore-forming domain as a molecular mechanism of colicin Y inactivation by its immunity protein.

  • Czech name

    Inaktivace kolicinu Y jeho imunitním proteinem

  • Czech description

    Je popsána inaktivace kolicinu Y jeho imunitním proteinem, predevším pak jde o identifikaci aminokyselinových zbyků, které se podílí na interakci mezi kolicinem a jeho imunitním proteinem.

Classification

  • Type

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

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

  • Continuities

    Z - Vyzkumny zamer (s odkazem do CEZ)

Others

  • Publication year

    2008

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    FEBS Journal

  • ISSN

    1742-464X

  • e-ISSN

  • Volume of the periodical

    275

  • Issue of the periodical within the volume

    21

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    7

  • Pages from-to

  • UT code for WoS article

    000260010600008

  • EID of the result in the Scopus database