ArticleJournal of bacteriology2012
Loss of elongation factor P disrupts bacterial outer membrane integrity.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 48 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 74 citations in OpenAlex.
- The RpfF Acyl-ACP thioesterase of major rice pathogen Xanthomonas oryzae pv. oryzae is essential for maintenance of membrane function and virulence.PLoS pathogens · 2026Article
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Pleiotropic roles of elongation factor P inMicrobiology spectrum · 2026Article
- Expression of Staphylococcus aureus translation elongation factor P is regulated by a stress-inducible promotor.Antonie van Leeuwenhoek · 2024Article
- Review
- YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- YfmR is a translation factor that prevents ribosome stalling and cell death in the absence of EF-P.bioRxiv : the preprint server for biology · 2023Article
- Translation factor accelerating peptide bond formation on the ribosome: EF-P and eIF5A as entropic catalysts and a potential drug targets.BBA advances · 2023Article
- Bacterial Ribosome Rescue Systems.Microorganisms · 2022Review
- The diffusible signal factor synthase, RpfF, in Xanthomonas oryzae pv. oryzae is required for the maintenance of membrane integrity and virulence.Molecular plant pathology · 2022Article
- A stress-induced block in dicarboxylate uptake and utilization inJournal of bacteriology · 2021Article
- Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021Review
- Non-invasive single-cell morphometry in living bacterial biofilms.Nature communications · 2020Article
- TheInfection and immunity · 2020Article
- Translation elongation factor P (EF-P).FEMS microbiology reviews · 2020Review
- Article
- Bacteria-Catalyzed Arginine Glycosylation in Pathogens and Host.Frontiers in cellular and infection microbiology · 2020Review
- Translational control of antibiotic resistance.Open biology · 2019Review
- Extragenic Suppression of Elongation Factor P Gene Mutant Phenotypes in Erwinia amylovora.Journal of bacteriology · 2019Article
- Sugar and iron: Toward understanding the antibacterial effect of ciclopirox in Escherichia coli.PloS one · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.