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
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DOI - Digital Object Identifier
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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
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Result continuities
Project
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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
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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
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UT code for WoS article
000260010600008
EID of the result in the Scopus database
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