The membrane topology of immunity proteins for the two-peptide bacteriocins carnobacteriocin XY, lactococcin G, and lactococcin MN shows structural diversity.

Autor: Britton AP; Department of Chemistry, The King's University, Edmonton, AB, Canada., van der Ende SR; Department of Chemistry, The King's University, Edmonton, AB, Canada., van Belkum MJ; Department of Chemistry, University of Alberta, Edmonton, AB, Canada., Martin-Visscher LA; Department of Chemistry, The King's University, Edmonton, AB, Canada.
Jazyk: angličtina
Zdroj: MicrobiologyOpen [Microbiologyopen] 2020 Jan; Vol. 9 (1), pp. e00957. Date of Electronic Publication: 2019 Oct 30.
DOI: 10.1002/mbo3.957
Abstrakt: The two-peptide bacteriocins produced by Gram-positive bacteria require two different peptides, present in equimolar amounts, to elicit optimal antimicrobial activity. Producer organisms are protected from their bacteriocin by a dedicated immunity protein. The immunity proteins for two-peptide bacteriocins contain putative transmembrane domains (TMDs) and might therefore be associated with the membrane. The immunity protein CbnZ for the two-peptide bacteriocin carnobacteriocin XY (CbnXY) was identified by heterologously expressing the cbnZ gene in sensitive host strains. Using protein topology prediction methods and the dual pho-lac reporter system, we mapped out the membrane topology of CbnZ, along with those of the immunity proteins LagC and LciM for the two-peptide bacteriocins lactococcin G and lactococcin MN, respectively. Our results reveal wide structural variety between these immunity proteins that can contain as little as one TMD or as many as four TMDs.
(© 2019 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.)
Databáze: MEDLINE
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