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Appl. Environ. Microbiol. doi:10.1128/AEM.00342-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Distinct contributions of the nisin biosynthesis enzymes NisB, NisC and the transporter NisT to prenisin production by Lactococcus lactis

Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, the Zernike Institute for Advanced Materials, and the Kluyver Centre for the Genomics of Industrial Microorganisms, University of Groningen, Kerklaan 30, NL-9751 NN Haren, The Netherlands; and BiOMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands

^* To whom correspondence should be addressed. Email: a.j.m.driessen{at}rug.nl.

	Abstract

Several Lactococcus lactis strains produce the lantibiotic nisin. The dedicated enzymes NisB and NisC, and the transporter NisT modify and secrete the ribosomally synthesized nisin precursor peptide. NisB can function in the absence of the cyclase NisC yielding the dehydrated prenisin that lacks the thioether rings. A kinetic analysis of nisin production by the L. lactis NZ9700 demonstrates that the prenisin is released from the cell into the medium before processing of the leader sequence occurs. Upon the deletion of nisC, production of prenisin is reduced by 70 %, while in the absence of nisB production of prenisin is nearly completely abolished. In cells lacking nisT, no secretion was observed while the expression of nisABC in these cells resulted in a considerable growth rate inhibition caused by the intracellular accumulation of active nisin. Overall, these data indicate that the efficiency of prenisin transport by NisT is markedly enhanced by NisB suggesting a channeling mechanism of prenisin transfer between the nisin modification enzymes and the transporter.