ArticleNature chemical biology2015
Arginine-rhamnosylation as new strategy to activate translation elongation factor P.
Article in Nature chemical biology, 2015. 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 68 papers.
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Who cites it
68 citing papers in PubMed, 135 citations in OpenAlex.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- 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
- Stepped collisional energy improves protein acylation identification by eliminating positional bias of cyclic immonium ions.Communications chemistry · 2025Article
- EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences.Nature communications · 2024Article
- Resolution of ribosomal stalling by EF-P and ABCF ATPases YfmR and YkpA/YbiT.Nucleic acids research · 2024Article
- The human mitochondrial translation factor TACO1 alleviates mitoribosome stalling at polyproline stretches.Nucleic acids research · 2024Article
- Horizontal Gene Transfer of a key Translation Factor and its Role in Polyproline Proteome Evolution.Molecular biology and evolution · 2024Article
- Article
- Elongation Factor P Modulates the Incorporation of Structurally Diverse Noncanonical Amino Acids intoJournal of the American Chemical Society · 2023Article
- CRISPRi-Mediated Silencing ofJournal of proteome research · 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
- Quantification of Protein Glycosylation Using Nanopores.Nano letters · 2022Article
- Translation stalling proline motifs are enriched in slow-growing, thermophilic, and multicellular bacteria.The ISME journal · 2022Article
- NleB/SseK-catalyzed arginine-glycosylation and enteropathogen virulence are finely tuned by a single variable position contiguous to the catalytic machinery.Chemical science · 2021Article
- Burkholderia PglL enzymes are Serine preferring oligosaccharyltransferases which target conserved proteins across the Burkholderia genus.Communications biology · 2021Article
- Two RmlC homologs catalyze dTDP-4-keto-6-deoxy-D-glucose epimerization in Pseudomonas putida KT2440.Scientific reports · 2021Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
13 authors at 6 institutions in 2 countries.
Funding
Abstract
Ribosome stalling at polyproline stretches is common and fundamental. In bacteria, translation elongation factor P (EF-P) rescues such stalled ribosomes, but only when it is post-translationally activated. In Escherichia coli, activation of EF-P is achieved by (R)-β-lysinylation and hydroxylation of a conserved lysine. Here we have unveiled a markedly different modification strategy in which a conserved arginine of EF-P is rhamnosylated by a glycosyltransferase (EarP) using dTDP-L-rhamnose as a substrate. This is to our knowledge the first report of N-linked protein glycosylation on arginine in bacteria and the first example in which a glycosylated side chain of a translation elongation factor is essential for function. Arginine-rhamnosylation of EF-P also occurs in clinically relevant bacteria such as Pseudomonas aeruginosa. We demonstrate that the modification is needed to develop pathogenicity, making EarP and dTDP-L-rhamnose-biosynthesizing enzymes ideal targets for antibiotic development.
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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.