bacteriocinsribosomally

Bacteriocins that are ribosomally synthesized are antimicrobial peptides produced by bacteria and archaea. They are encoded by gene clusters and are initially produced as precursor peptides that carry an amino-terminal leader sequence. After export or at the membrane, the leader is removed and, in many cases, the core peptide is post-translationally modified to yield a mature active molecule. These ribosomally derived bacteriocins include the broader class known as ribosomally synthesized and post-translationally modified peptides (RiPPs), such as lantibiotics that contain unusual amino acids like lanthionine, as well as other small peptides that may be unmodified or lightly modified.

Bacteriocin gene clusters typically encode not only the structural gene but also enzymes responsible for modifications, export systems, and self-immunity proteins that protect the producer. The peptide's antibacterial activity is often narrow and targeted toward closely related strains, although some members exhibit broader spectra. Mechanisms of action vary but commonly involve disruption of cellular membranes, pore formation, or inhibition of cell wall synthesis. Nisin, a well-known lantibiotic, exemplifies membrane targeting via interactions with lipid II.

Applications include food preservation, where safe bacteriocins such as nisin are used to inhibit spoilage and pathogenic bacteria, and ongoing exploration of therapeutic and agricultural uses. Challenges include the potential for resistance development, stability under diverse conditions, and regulatory considerations. Research continues to expand understanding of biosynthesis, immunity, and practical deployment of ribosomally produced bacteriocins.