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Applied and Environmental Microbiology, March 2007, p. 1792-1796, Vol. 73, No. 6
0099-2240/07/$08.00+0     doi:10.1128/AEM.02350-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Production of Dehydroamino Acid-Containing Peptides by Lactococcus lactis{triangledown}

Rick Rink,1 Jenny Wierenga,1 Anneke Kuipers,1 Leon D. Kluskens,1 Arnold J. M. Driessen,2 Oscar P. Kuipers,3 and Gert N. Moll1*

BiOMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands,1 Department of Microbiology,2 Department of Molecular Genetics, Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, Groningen, The Netherlands3

Received 5 October 2006/ Accepted 9 January 2007

Nisin is a pentacyclic peptide antibiotic produced by some Lactococcus lactis strains. Nisin contains dehydroresidues and thioether rings that are posttranslationally introduced by a membrane-associated enzyme complex, composed of a serine and threonine dehydratase NisB and the cyclase NisC. In addition, the transporter NisT is necessary for export of the modified peptide. We studied the potential of L. lactis expressing NisB and NisT to produce peptides whose serines and threonines are dehydrated. L. lactis containing the nisBT genes and a plasmid coding for a specific leader peptide fusion construct efficiently produced peptides with a series of non-naturally occurring multiple flanking dehydrobutyrines. We demonstrated NisB-mediated dehydration of serines and threonines in a C-terminal nisin(1-14) extension of nisin, which implies that also residues more distant from the leader peptide than those occurring in prenisin or any other lantibiotic can be modified. Furthermore, the feasibility and efficiency of generating a library of peptides containing dehydroresidues were demonstrated. In view of the particular shape and reactivity of dehydroamino acids, such a library provides a novel source for screening for peptides with desired biological and physicochemical properties.

* Corresponding author. Mailing address: BiOMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands. Phone: 31 50 3638070. Fax: 31 50 3634429. E-mail: moll{at}biomade.nl.

{triangledown} Published ahead of print on 19 January 2007.

Applied and Environmental Microbiology, March 2007, p. 1792-1796, Vol. 73, No. 6
0099-2240/07/$08.00+0     doi:10.1128/AEM.02350-06
Copyright © 2007, 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]  
  • Kuipers, A., Meijer-Wierenga, J., Rink, R., Kluskens, L. D., Moll, G. N. (2008). Mechanistic Dissection of the Enzyme Complexes Involved in Biosynthesis of Lacticin 3147 and Nisin. Appl. Environ. Microbiol. 74: 6591-6597 [Abstract] [Full Text]  
  • van den Berg van Saparoea, H. B., Bakkes, P. J., Moll, G. N., Driessen, A. J. M. (2008). Distinct Contributions of the Nisin Biosynthesis Enzymes NisB and NisC and Transporter NisT to Prenisin Production by Lactococcus lactis. Appl. Environ. Microbiol. 74: 5541-5548 [Abstract] [Full Text]  
  • Lubelski, J., Overkamp, W., Kluskens, L. D., Moll, G. N., Kuipers, O. P. (2008). Influence of Shifting Positions of Ser, Thr, and Cys Residues in Prenisin on the Efficiency of Modification Reactions and on the Antimicrobial Activities of the Modified Prepeptides. Appl. Environ. Microbiol. 74: 4680-4685 [Abstract] [Full Text]  


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