Affiliation:
1. Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada
2. Department of Microbiology, The Ohio State University, Columbus, Ohio, USA
Abstract
ABSTRACT
Elongation factor P (EF-P) is posttranslationally modified at a conserved lysyl residue by the coordinated action of two enzymes, PoxA and YjeK. We have previously established the importance of this modification in
Salmonella
stress resistance. Here we report that, like
poxA
and
yjeK
mutants,
Salmonella
strains lacking EF-P display increased susceptibility to hypoosmotic conditions, antibiotics, and detergents and enhanced resistance to the compound
S
-nitrosoglutathione. The susceptibility phenotypes are largely explained by the enhanced membrane permeability of the
efp
mutant, which exhibits increased uptake of the hydrophobic dye 1-
N
-phenylnaphthylamine (NPN). Analysis of the membrane proteomes of wild-type and
efp
mutant
Salmonella
strains reveals few changes, including the prominent overexpression of a single porin, KdgM, in the
efp
mutant outer membrane. Removal of KdgM in the
efp
mutant background ameliorates the detergent, antibiotic, and osmosensitivity phenotypes and restores wild-type permeability to NPN. Our data support a role for EF-P in the translational regulation of a limited number of proteins that, when perturbed, renders the cell susceptible to stress by the adventitious overexpression of an outer membrane porin.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
65 articles.
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