A putative amino acid transporter determines sensitivity to the two-peptide bacteriocin plantaricin JK.

Details

Serval ID
serval:BIB_BD93AB5E0046
Type
Article: article from journal or magazin.
Collection
Publications
Title
A putative amino acid transporter determines sensitivity to the two-peptide bacteriocin plantaricin JK.
Journal
Microbiologyopen
Author(s)
Oppegård C., Kjos M., Veening J.W., Nissen-Meyer J., Kristensen T.
ISSN
2045-8827 (Electronic)
ISSN-L
2045-8827
Publication state
Published
Issued date
2016
Volume
5
Number
4
Pages
700-708
Language
english
Abstract
Lactobacillus plantarum produces a number of antimicrobial peptides (bacteriocins) that mostly target closely related bacteria. Although bacteriocins are important for the ecology of these bacteria, very little is known about how the peptides target sensitive cells. In this work, a putative membrane protein receptor of the two-peptide bacteriocin plantaricin JK was identified by comparing Illumina sequence reads from plantaricin JK-resistant mutants to a crude assembly of the sensitive wild-type Weissella viridescens genome using the polymorphism discovery tool VAAL. Ten resistant mutants harbored altogether seven independent mutations in a gene encoding an APC superfamily protein with 12 transmembrane helices. The APC superfamily transporter thus is likely to serve as a target for plantaricin JK on sensitive cells.
Keywords
Antibacterial activity, bacteriocins, membrane proteins, mode of action
Pubmed
Web of science
Open Access
Yes
Create date
11/10/2016 16:37
Last modification date
20/08/2019 16:31
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