Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis

C Herranz; AJM Driessen

doi:10.1128/AEM.71.4.1959-1963.2005

Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis

C Herranz, AJM Driessen^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

38 Citations (Scopus)

292 Downloads (Pure)

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 See translocase.

Original language	English
Pages (from-to)	1959-1963
Number of pages	5
Journal	Applied and environmental microbiology
Volume	71
Issue number	4
DOIs	https://doi.org/10.1128/AEM.71.4.1959-1963.2005
Publication status	Published - Apr-2005

Keywords

ACID BACTERIA
ESCHERICHIA-COLI
SIGNAL PEPTIDE
DEPENDENT BACTERIOCIN
PROTEIN EXPORT
FOOD SAFETY
EXPRESSION
PLASMID
MEMBRANE
SPECTRUM

Access to Document

10.1128/AEM.71.4.1959-1963.2005

2005ApplEnvirMicrobiolHerranz.pdfFinal publisher's version, 148 KB

Handle.net

Persistent link

Cite this

@article{fd5f0ccc750f45fda4dd3e213badaa19,

title = "Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis",

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 See translocase.",

keywords = "ACID BACTERIA, ESCHERICHIA-COLI, SIGNAL PEPTIDE, DEPENDENT BACTERIOCIN, PROTEIN EXPORT, FOOD SAFETY, EXPRESSION, PLASMID, MEMBRANE, SPECTRUM",

author = "C Herranz and AJM Driessen",

year = "2005",

month = apr,

doi = "10.1128/AEM.71.4.1959-1963.2005",

language = "English",

volume = "71",

pages = "1959--1963",

journal = "Applied and environmental microbiology",

issn = "0099-2240",

publisher = "AMER SOC MICROBIOLOGY",

number = "4",

}

TY - JOUR

T1 - Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis

AU - Herranz, C

AU - Driessen, AJM

PY - 2005/4

Y1 - 2005/4

N2 - 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 See translocase.

AB - 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 See translocase.

KW - ACID BACTERIA

KW - ESCHERICHIA-COLI

KW - SIGNAL PEPTIDE

KW - DEPENDENT BACTERIOCIN

KW - PROTEIN EXPORT

KW - FOOD SAFETY

KW - EXPRESSION

KW - PLASMID

KW - MEMBRANE

KW - SPECTRUM

U2 - 10.1128/AEM.71.4.1959-1963.2005

DO - 10.1128/AEM.71.4.1959-1963.2005

M3 - Article

SN - 0099-2240

VL - 71

SP - 1959

EP - 1963

JO - Applied and environmental microbiology

JF - Applied and environmental microbiology

IS - 4

ER -

Sec-mediated secretion of bacteriocin enterocin P by Lactococcus lactis

Abstract

Keywords

Access to Document

Handle.net

Fingerprint

Cite this