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

Détails

ID Serval
serval:BIB_BD93AB5E0046
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
A putative amino acid transporter determines sensitivity to the two-peptide bacteriocin plantaricin JK.
Périodique
Microbiologyopen
Auteur⸱e⸱s
Oppegård C., Kjos M., Veening J.W., Nissen-Meyer J., Kristensen T.
ISSN
2045-8827 (Electronic)
ISSN-L
2045-8827
Statut éditorial
Publié
Date de publication
2016
Volume
5
Numéro
4
Pages
700-708
Langue
anglais
Résumé
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.
Mots-clé
Antibacterial activity, bacteriocins, membrane proteins, mode of action
Pubmed
Web of science
Open Access
Oui
Création de la notice
11/10/2016 15:37
Dernière modification de la notice
20/08/2019 15:31
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