title: Lantibiotic biosynthesis: interactions between prelacticin 481 and its putative modification enzyme, LctM.
abstract: Class AII and AIII lantibiotics and mersacidin are antibacterial peptides containing unusual residues obtained by posttranslational modifications of prepeptides, presumably catalyzed by LanM. LctM, the LanM for lacticin 481, is essential for the production of this class AII lantibiotic. Using the yeast two-hybrid system, we showed direct contact between the prelacticin 481 and LctM, supporting the proposed LctM function. Sixteen domains are conserved between the 10 known LanM proteins, whereas three additional domains were found only in class AII LanM proteins and in MrsM, the LanM for mersacidin. All the truncated LctM proteins that we tested presented impaired LctA-binding activity.
authors.affiliation: Laboratoire de Biologie et Chimie Moléculaires, Université de Bretagne Sud, Vannes, France.
authors.forename: P
authors.initials: P
authors.lastname: Uguen
authors.forename: J P
authors.initials: JP
authors.lastname: Le Pennec
authors.forename: A
authors.initials: A
authors.lastname: Dufour
mesh_terms: D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001430:Bacteriocins / Q000096:biosynthesis; D001665:Binding Sites; D003001:Cloning, Molecular; D017124:Conserved Sequence; D013294:Lactococcus lactis / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D009876:Operon; D010455:Peptides; D011498:Protein Precursors / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D001430:Bacteriocins; C413468:LtcM protein, Lactococcus lactis; D010455:Peptides; D011498:Protein Precursors; C413459:prelacticin 481; C082508:lacticin 481