|Title||Recognition of pore-forming colicin Y by its cognate immunity protein.|
|Publication Type||Journal Article|
|Year of Publication||2006|
|Authors||Smajs, D, Matejková, P, Weinstock, GM|
|Journal||FEMS Microbiol Lett|
|Date Published||2006 May|
|Keywords||Amino Acid Sequence, Bacterial Proteins, Colicins, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Structure, Secondary, Structure-Activity Relationship|
Construction of hybrid immunity genes between colicin U (cui) and Y (cyi) immunity genes and site-directed mutagenesis of cyi were used to identify amino-acid residues of the colicin Y immunity protein (Cyi) involved in recognition of colicin Y. These amino-acid residues were localized close to the cytoplasmic site of the Cyi transmembrane helices T3 (S104, S107, F110, A112) and T4 (A159). Mutations in cui, which converted Cui sequence to Cyi sequence in positions 104, 107, 110, 112 and 159, resulted in an immunity gene that also conferred (besides immunity to colicin U) a high degree of immunity to colicin Y.
|Alternate Journal||FEMS Microbiol Lett|
Recognition of pore-forming colicin Y by its cognate immunity protein.
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