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Applied and Environmental Microbiology, April 2005, p. 1959-1963, Vol. 71, No. 4
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.4.1959-1963.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Sec-Mediated Secretion of Bacteriocin Enterocin P by Lactococcus lactis

Carmen Herranz and Arnold J. M. Driessen*

Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands

Received 16 July 2004/ Accepted 9 November 2004

Most lactic acid bacterium bacteriocins utilize specific leader peptides and dedicated machineries for secretion. In contrast, the enterococcal bacteriocin enterocin P (EntP) contains a typical signal peptide that directs its secretion when heterologously expressed in Lactococcus lactis. Signal peptide mutations and the SecA inhibitor azide blocked secretion. These observations demonstrate that EntP is secreted by the Sec translocase.

* 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.

Applied and Environmental Microbiology, April 2005, p. 1959-1963, Vol. 71, No. 4
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.4.1959-1963.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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