ArticleNucleic acids research2014
Molecular evolution of protein-RNA mimicry as a mechanism for translational control.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Expression of translation elongation factor P in Kocuria rhizophila is regulated by an inducible weak promoter.BMC microbiology · 2026Article
- TAR RNA Mimicry of INI1 and Its Influence on Non-Integration Function of HIV-1 Integrase.Viruses · 2025Review
- YebC2 resolves ribosome stalling at polyprolines independent of EF-P and the ABCF ATPase YfmR.bioRxiv : the preprint server for biology · 2024Article
- Expression of Staphylococcus aureus translation elongation factor P is regulated by a stress-inducible promotor.Antonie van Leeuwenhoek · 2024Article
- INI1/SMARCB1 Rpt1 domain mimics TAR RNA in binding to integrase to facilitate HIV-1 replication.Nature communications · 2021Article
- How Signaling Games Explain Mimicry at Many Levels: From Viral Epidemiology to Human Sociology.Research square · 2020Article
- Translation elongation factor P (EF-P).FEMS microbiology reviews · 2020Review
- Switching the Post-translational Modification of Translation Elongation Factor EF-P.Frontiers in microbiology · 2019Article
- Origin of biomolecular games: deception and molecular evolution.Journal of the Royal Society, Interface · 2018Article
- Carbonyl reduction by YmfI in Bacillus subtilis prevents accumulation of an inhibitory EF-P modification state.Molecular microbiology · 2017Article
- Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P.mBio · 2017Article
- Mg2+ regulates transcription of mgtA in Salmonella Typhimurium via translation of proline codons during synthesis of the MgtL peptide.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Non-canonical roles of tRNAs and tRNA mimics in bacterial cell biology.Molecular microbiology · 2016Review
- Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability.PloS one · 2016Article
- Finding optimal interaction interface alignments between biological complexes.Bioinformatics (Oxford, England) · 2015Article
- Mechanisms of ribosome rescue in bacteria.Nature reviews. Microbiology · 2015Review
- The non-canonical hydroxylase structure of YfcM reveals a metal ion-coordination motif required for EF-P hydroxylation.Nucleic acids research · 2014Article
- Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Elongation factor P (EF-P) is a conserved ribosome-binding protein that structurally mimics tRNA to enable the synthesis of peptides containing motifs that otherwise would induce translational stalling, including polyproline. In many bacteria, EF-P function requires post-translational modification with (R)-β-lysine by the lysyl-tRNA synthetase paralog PoxA. To investigate how recognition of EF-P by PoxA evolved from tRNA recognition by aminoacyl-tRNA synthetases, we compared the roles of EF-P/PoxA polar contacts with analogous interactions in a closely related tRNA/synthetase complex. PoxA was found to recognize EF-P solely via identity elements in the acceptor loop, the domain of the protein that interacts with the ribosome peptidyl transferase center and mimics the 3'-acceptor stem of tRNA. Although the EF-P acceptor loop residues required for PoxA recognition are highly conserved, their conservation was found to be independent of the phylogenetic distribution of PoxA. This suggests EF-P first evolved tRNA mimicry to optimize interactions with the ribosome, with PoxA-catalyzed aminoacylation evolving later as a secondary mechanism to further improve ribosome binding and translation control.
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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.