ArticlePloS one2016
Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 52 citations in OpenAlex.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Pleiotropic roles of elongation factor P inMicrobiology spectrum · 2026Article
- Horizontal transfer of post-translational modifiers brings evolutionary opportunity and challenges to a conserved translation factor.BMC biology · 2026Article
- Constant trouble with prolines-navigating a global translation dilemma.Nucleic acids research · 2026Review
- YebC2 resolves ribosome stalling and increases fitness of cells lacking EF-P and the ABCF ATPase YfmR.PLoS genetics · 2025Article
- YebC2 resolves ribosome stalling at polyprolines independent of EF-P and the ABCF ATPase YfmR.bioRxiv : the preprint server for biology · 2024Article
- Resolution of ribosomal stalling by EF-P and ABCF ATPases YfmR and YkpA/YbiT.Nucleic acids research · 2024Article
- Horizontal Gene Transfer of a key Translation Factor and its Role in Polyproline Proteome Evolution.Molecular biology and evolution · 2024Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- 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
- Elongation factor P modulatesProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Rhamnose-Containing Compounds: Biosynthesis and Applications.Molecules (Basel, Switzerland) · 2022Review
- Translation stalling proline motifs are enriched in slow-growing, thermophilic, and multicellular bacteria.The ISME journal · 2022Article
- Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021Review
- A β-hairpin epitope as novel structural requirement for protein arginine rhamnosylation.Chemical science · 2020Article
- Translation elongation factor P (EF-P).FEMS microbiology reviews · 2020Review
- Bacteria-Catalyzed Arginine Glycosylation in Pathogens and Host.Frontiers in cellular and infection microbiology · 2020Review
- Complex Structure ofJournal of bacteriology · 2019Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation elongation factor P (EF-P), a ubiquitous protein over the entire range of bacterial species, rescues ribosomal stalling at consecutive prolines in proteins. In Escherichia coli and Salmonella enterica, the post-translational β-lysyl modification of Lys34 of EF-P is important for the EF-P activity. The β-lysyl EF-P modification pathway is conserved among only 26-28% of bacteria. Recently, it was found that the Shewanella oneidensis and Pseudomonas aeruginosa EF-P proteins, containing an Arg residue at position 32, are modified with rhamnose, which is a novel post-translational modification. In these bacteria, EF-P and its Arg modification are both dispensable for cell viability, similar to the E. coli and S. enterica EF-P proteins and their Lys34 modification. However, in the present study, we found that EF-P and Arg32 are essential for the viability of the human pathogen, Neisseria meningitidis. We therefore analyzed the modification of Arg32 in the N. meningitidis EF-P protein, and identified the same rhamnosyl modification as in the S. oneidensis and P. aeruginosa EF-P proteins. N. meningitidis also has the orthologue of the rhamnosyl modification enzyme (EarP) from S. oneidensis and P. aeruginosa. Therefore, EarP should be a promising target for antibacterial drug development specifically against N. meningitidis. The pair of genes encoding N. meningitidis EF-P and EarP suppressed the slow-growth phenotype of the EF-P-deficient mutant of E. coli, indicating that the activity of N. meningitidis rhamnosyl-EF-P for rescuing the stalled ribosomes at proline stretches is similar to that of E. coli β-lysyl-EF-P. The possible reasons for the unique requirement of rhamnosyl-EF-P for N. meningitidis cells are that more proline stretch-containing proteins are essential and/or the basal ribosomal activity to synthesize proline stretch-containing proteins in the absence of EF-P is lower in this bacterium than in others.
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