title: N-terminal acetylation in paenibacillin, a novel lantibiotic.
abstract: N-terminal acetylation was uncovered in paenibacillin, a novel lantibiotic recently reported as a product of Paenibacillus polymyxa OSY-DF. This N-terminal modification is unprecedented among bacteria-derived antimicrobial peptides and further illustrates the broad range of modifications that can occur in lantibiotics. Additionally, the primary structure of paenibacillin has been finally determined unequivocally by the extensive NMR analysis taken together with previous MS/MS results. These analyses revealed the structure of paenibacillin as one of the most post-translationally modified lantibiotics.
authors.affiliation: Department of Food Science and Technology, The Ohio State University, 2015 Fyffe Road, Parker Food Science Building, Columbus, OH 43210, USA.
authors.forename: Zengguo
authors.initials: Z
authors.lastname: He
authors.forename: Chunhua
authors.initials: C
authors.lastname: Yuan
authors.forename: Liwen
authors.initials: L
authors.lastname: Zhang
authors.forename: Ahmed E
authors.initials: AE
authors.lastname: Yousef
mesh_terms: D000107:Acetylation; D000596:Amino Acids / Q000032:analysis; D001407:Bacillus / Q000378:metabolism*; D001430:Bacteriocins / Q000096:biosynthesis* / Q000737:chemistry* / Q000302:isolation & purification; D005285:Fermentation; D009682:Magnetic Resonance Spectroscopy
chemical_list: D000596:Amino Acids; D001430:Bacteriocins; C531362:paenibacillin protein, Paenibacillus polymyxa