title: Substrate selectivity of the sublancin S-glycosyltransferase.
abstract: SunS is a novel S-glycosyltransferase involved in the biosynthesis of the antimicrobial peptide sublancin. It selectively modifies Cys22 in a 56 amino acid peptide substrate SunA and can accept a variety of NDP sugars. This study reports the substrate selectivity with regard to the peptide substrate and the antimicrobial activity of the resulting sublancin analogues. The results suggest that SunS recognizes an α-helix N-terminal of the Cys to be glycosylated, which is present in a flexible linker. Interestingly, when Cys22 is mutated, sugar attachment is not required for sublancin antimicrobial activity. Furthermore, the sublancin-producing strain  Bacillus subtilis  168 also becomes susceptible to such mutants. These data suggest that S-glycosylation may be important for self-resistance.
authors.affiliation: Howard Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
authors.forename: Huan
authors.initials: H
authors.lastname: Wang
authors.forename: Wilfred A
authors.initials: WA
authors.lastname: van der Donk
mesh_terms: D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry / Q000494:pharmacology; D001412:Bacillus subtilis / Q000187:drug effects; D001430:Bacteriocins / Q000096:biosynthesis* / Q000737:chemistry / Q000494:pharmacology; D006020:Glycopeptides; D016695:Glycosyltransferases / Q000737:chemistry / Q000378:metabolism*; D008826:Microbial Sensitivity Tests; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D006020:Glycopeptides; D010455:Peptides; C114602:sublancin 168; D016695:Glycosyltransferases