Literature DB >> 15812026

Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis.

Carmen Herranz1, Arnold J M Driessen.   

Abstract

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.

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Year:  2005        PMID: 15812026      PMCID: PMC1082533          DOI: 10.1128/AEM.71.4.1959-1963.2005

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  36 in total

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2.  Restrictive use of detergents in the functional reconstitution of the secondary multidrug transporter LmrP.

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4.  Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum.

Authors:  L M Cintas; P Casaus; L S Håvarstein; P E Hernández; I F Nes
Journal:  Appl Environ Microbiol       Date:  1997-11       Impact factor: 4.792

Review 5.  Potential of bacteriocin-producing lactic acid bacteria for improvements in food safety and quality.

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3.  Sec-mediated transport of posttranslationally dehydrated peptides in Lactococcus lactis.

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