This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by van den Berg van Saparoea, H. B.
Right arrow Articles by Driessen, A. J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by van den Berg van Saparoea, H. B.
Right arrow Articles by Driessen, A. J. M.
Agricola
Right arrow Articles by van den Berg van Saparoea, H. B.
Right arrow Articles by Driessen, A. J. M.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, September 2008, p. 5541-5548, Vol. 74, No. 17
0099-2240/08/$08.00+0     doi:10.1128/AEM.00342-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Distinct Contributions of the Nisin Biosynthesis Enzymes NisB and NisC and Transporter NisT to Prenisin Production by Lactococcus lactis{triangledown}

H. Bart van den Berg van Saparoea,1,{dagger} Patrick J. Bakkes,1,{dagger} Gert N. Moll,2 and Arnold J. M. Driessen1*

Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, Zernike Institute for Advanced Materials and Kluyver Centre for the Genomics of Industrial Microorganisms, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands,1 BiOMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands2

Received 11 February 2008/ Accepted 6 July 2008

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 L. lactis NZ9700 demonstrated that the prenisin was released from the cell into the medium before the processing of the leader sequence occurred. Upon the deletion of nisC, the production of prenisin was reduced by 70%, while in the absence of nisB, the production of prenisin was nearly completely abolished. In cells lacking nisT, no secretion was observed, while the expression of nisABC in these cells resulted in 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.

* Corresponding author. Mailing address: Department of Microbiology, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands. Phone: 31-50-3632164. Fax: 31-50-3632154. E-mail: a.j.m.driessen{at}rug.nl

{triangledown} Published ahead of print on 11 July 2008.

{dagger} These authors contributed equally.

Applied and Environmental Microbiology, September 2008, p. 5541-5548, Vol. 74, No. 17
0099-2240/08/$08.00+0     doi:10.1128/AEM.00342-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Lubelski, J., Khusainov, R., Kuipers, O. P. (2009). Directionality and Coordination of Dehydration and Ring Formation during Biosynthesis of the Lantibiotic Nisin. J. Biol. Chem. 284: 25962-25972 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»