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Inactivation of colicin Y by intramembrane helix-helix interaction with its immunity protein

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dc.title Inactivation of colicin Y by intramembrane helix-helix interaction with its immunity protein en
dc.contributor.author Šmajs, David
dc.contributor.author Doležalová, Magda
dc.contributor.author Macek, Pavel
dc.contributor.author Žídek, Lukáš
dc.relation.ispartof Febs Journal
dc.identifier.issn 1742-464X Scopus Sources, Sherpa/RoMEO, JCR
dc.date.issued 2008-11
utb.relation.volume 275
utb.relation.issue 21
dc.citation.spage 5325
dc.citation.epage 5331
dc.type article
dc.language.iso en
dc.publisher Blackwell Publishing, Inc. en
dc.identifier.doi 10.1111/j.1742-4658.2008.06662.x
dc.relation.uri http://onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2008.06662.x/abstract
dc.subject colicin immunity en
dc.subject colicin Y en
dc.subject helix-helix interaction en
dc.subject pore-forming colicin en
dc.subject site-directed mutagenesis en
dc.description.abstract The construction of hybrids between colicins U and Y and the mutagenesis of the colicin Y gene (cya) have 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 Escherichia coli strain with cloned colicin Y immunity gene (cyi) inactivated this mutant, but not the wild-type 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. en
utb.faculty Faculty of Technology
dc.identifier.uri http://hdl.handle.net/10563/1002127
utb.identifier.obdid 43857843
utb.identifier.scopus 2-s2.0-53849089923
utb.identifier.wok 000260010600008
utb.identifier.pubmed 18803667
utb.source j-wok
dc.date.accessioned 2011-08-16T15:06:32Z
dc.date.available 2011-08-16T15:06:32Z
utb.contributor.internalauthor Doležalová, Magda
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