Biosynthesis of Lantibiotic Nisin: POSTTRANSLATIONAL MODIFICATION OF ITS PREPEPTIDE OCCURS AT A MULTIMERIC MEMBRANE-ASSOCIATED LANTHIONINE SYNTHETASE COMPLEX

摘要: The lantibiotic nisin of Lactococcus lactis is matured from a ribosomally synthesized prepeptide by post-translational modification. Genetic and biochemical evidence suggests that genes nisB nisC the gene cluster encode proteins necessary for prenisin Inactivation both resulted in complete loss production. preparation membrane vesicles revealed NisB NisC are attached to cellular membrane, co-immunoprecipitation experiments showed they associated with each other. By using yeast two-hybrid system, which highly sensitive method unravel protein-protein interactions, we could show physically interacts protein, suggesting contains binding site prenisin. This was also confirmed protein NisA antibodies directed against leader sequence prepeptide. analysis interaction between as well NisT ABC transporter. A minor indicated protein. Furthermore, investigations at least two molecules part modification transport complex. Our results suggest maturation secretion occur membrane-associated multimeric lanthionine synthetase complex consisting NisB, NisC, transporter NisT.