Posttranslationally modified bacteriocins--the lantibiotics.
Lantibiotics are a subgroup of bacteriocins that are characterized by the presence of the unusual thioether amino acids lanthionine and 3-methyllanthionine generated through posttranslational modification. The biosynthesis of lantibiotics follows a defined pathway comprising modifications of the prepeptide, proteolytic activation, and export. The genes encoding the biosynthesis apparatus and the lantibiotic prepeptide are organized in clusters, which also include information for proteins involved in regulation and producer self-protection. The elongated cationic lantibiotics primarily act through the formation of pores and recent progress with nisin and epidermin has shown that specific docking molecules such as lipid II play an essential role in this mechanism. Mersacidin and actagardine inhibit cell wall biosynthesis by complexing the precursor lipid II, whereas the cinnamycin-like peptides bind to phosphoethanolamine thus inhibiting phospholipase A2.
Guder
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Institut für Medizinische Mikrobiologie und Immunologie der Universität Bonn, Sigmund-Freud-Str. 25, D-53105 Bonn, Germany.
Wiedemann
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I
Sahl
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HG
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D000890:Anti-Infective Agents / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D001430:Bacteriocins / Q000737:chemistry / Q000235:genetics* / Q000494:pharmacology; D002463:Cell Membrane Permeability / Q000187:drug effects; D008969:Molecular Sequence Data; D010455:Peptides; D011499:Protein Processing, Post-Translational / Q000502:physiology*
D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D001430:Bacteriocins; D010455:Peptides