ArticleThe Journal of biological chemistry2012
Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P).
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 62 citations in OpenAlex.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Hitchhiking genes and boundaries of AmpC amplicons during amoxicillin resistance development in E. coli.BMC microbiology · 2025Article
- Phosphorylation of EF-P aggravates Streptococcus suis-induced blood-brain barrier damage by enhancing serine protease production.Veterinary research · 2025Article
- Kinetic mechanism and determinants of EF-P recruitment to translating ribosomes.Nucleic acids research · 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
- Elongation Factor P Modulates the Incorporation of Structurally Diverse Noncanonical Amino Acids intoJournal of the American Chemical Society · 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
- Genome-Wide Investigation of Pasteurella multocida Identifies the Stringent Response as a Negative Regulator of Hyaluronic Acid Capsule Production.Microbiology spectrum · 2022Article
- 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
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- Extragenic Suppression of Elongation Factor P Gene Mutant Phenotypes in Erwinia amylovora.Journal of bacteriology · 2019Article
- Disulfide Crosslinked Hydrogels Made From the Hydra Stinging Cell Protein, Minicollagen-1.Frontiers in chemistry · 2019Article
- A Survey of Pyridoxal 5'-Phosphate-Dependent Proteins in the Gram-Positive Model BacteriumFrontiers in molecular biosciences · 2019Review
- Hypusine, a polyamine-derived amino acid critical for eukaryotic translation.The Journal of biological chemistry · 2018Review
- Translation Elongation and Recoding in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- An Erwinia amylovora yjeK mutant exhibits reduced virulence, increased chemical sensitivity and numerous environmentally dependent proteomic alterations.Molecular plant pathology · 2018Article
- The role of polyproline motifs in the histidine kinase EnvZ.PloS one · 2018Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Bacterial elongation factor P (EF-P) is the ortholog of archaeal and eukaryotic initiation factor 5A (eIF5A). EF-P shares sequence homology and crystal structure with eIF5A, but unlike eIF5A, EF-P does not undergo hypusine modification. Recently, two bacterial genes, yjeA and yjeK, encoding truncated homologs of class II lysyl-tRNA synthetase and of lysine-2,3-aminomutase, respectively, have been implicated in the modification of EF-P to convert a specific lysine to a hypothetical β-lysyl-lysine. Here we present biochemical evidence for β-lysyl-lysine modification in Escherichia coli EF-P and for its role in EF-P activity by characterizing native and recombinant EF-P proteins for their modification status and activity in vitro. Mass spectrometric analyses confirmed the lysyl modification at lysine 34 in native and recombinant EF-P proteins. The β-lysyl-lysine isopeptide was identified in the exhaustive Pronase digests of native EF-P and recombinant EF-P isolated from E. coli coexpressing EF-P, YjeA, and YjeK but not in the digests of proteins derived from the vectors encoding EF-P alone or EF-P together with YjeA, indicating that both enzymes, YjeA and YjeK, are required for β-lysylation of EF-P. Endogenous EF-P as well as the recombinant EF-P preparation containing β-lysyl-EF-P stimulated N-formyl-methionyl-puromycin synthesis ∼4-fold over the preparations containing unmodified EF-P and/or α-lysyl-EF-P. The mutant lacking the modification site lysine (K34A) was inactive. This is the first report of biochemical evidence for the β-lysylation of EF-P in vivo and the requirement for this modification for the activity of EF-P.
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