TAILIEUCHUNG - Báo cáo khoa học: Inactivation of colicin Y by intramembrane helix–helix interaction with its immunity protein

Daptomycin and A21987C antibiotics are branched, cyclic, nonribosomally assembled acidic lipodepsipeptides produced byStreptomyces roseosporus. The antibacterial activity of daptomycin against Gram-positive bacteria strongly depends on the nature of the N-terminal fatty acid moiety. | ỊFEBS Journal Inactivation of colicin Y by intramembrane helix-helix interaction with its immunity protein David Smajs1 Magda DoleZalova1 2 Pavel Macek3 4 and Lukas Zidek3 1 Department of Biology Faculty of Medicine Masaryk University Brno Czech Republic 2 Department of Food Engineering Faculty of Technology Tomas Bata University Zlin Czech Republic 3 National centre for Biomolecular Research Faculty of Science Masaryk University Brno Czech Republic 4 Institute of Microbiology Academy of Sciences of the Czech Republic Prague Czech Republic Keywords colicin immunity colicin Y helix-helix interaction pore-forming colicin site-directed mutagenesis Correspondence D. Smajs Department of Biology Faculty of Medicine Masaryk University Kamenice 5 Building A6 625 00 Brno Czech Republic Fax 420 549 491 327 Tel 420 549 497 496 E-mail dsmajs@ Received 22 May 2008 revised 4 August 2008 accepted 29 August 2008 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. doi Colicin Y Cya belongs to the group of ion channelforming colicins 1 having a high sequence homology to colicin U 2 . A

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