Loss of Elongation Factor P Disrupts Bacterial Outer Membrane Integrity

Author:

Zou S. Betty1,Hersch Steven J.1,Roy Hervé2,Wiggers J. Brad1,Leung Andrea S.1,Buranyi Stephen1,Xie Jinglin Lucy1,Dare Kiley2,Ibba Michael2,Navarre William Wiley1

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

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