ArticleNucleic acids research2018
Antibiotic resistance ABCF proteins reset the peptidyl transferase centre of the ribosome to counter translational arrest.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 83 citations in OpenAlex.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- Enhancing ribosomal translation of backbone-altering nonproteinogenic amino acids via YebC and YeeN.Nucleic acids research · 2026Article
- The Alteromonas macleodii ribosome enables consecutive incorporation of bulky D-amino acids into peptides.Nucleic acids research · 2026Article
- Ribosomal protection as a linezolid resistance mechanism inAntimicrobial agents and chemotherapy · 2026Article
- Ribosomal protection as a linezolid resistance mechanism inbioRxiv : the preprint server for biology · 2025Article
- Article
- Multifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance.Biochemical Society transactions · 2025Article
- Promoting ribosomal incorporation of backbone-modifying nonproteinogenic amino acids into nascent peptides by ATP-binding cassette family-F proteins and EF-P.Nucleic acids research · 2025Article
- Discovery of a fluorinated macrobicyclic antibiotic through chemical synthesis.Nature chemistry · 2025Article
- YebC2 resolves ribosome stalling and increases fitness of cells lacking EF-P and the ABCF ATPase YfmR.PLoS genetics · 2025Article
- Analysis of vaginal microbiota during postpartum and postmenopausal periods based on metagenomics.BMC microbiology · 2024Article
- 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
- Clindamycin: A Comprehensive Status Report with Emphasis on Use in Dermatology.The Journal of clinical and aesthetic dermatology · 2024Review
- Global regulation via modulation of ribosome pausing by the ABC-F protein EttA.Nature communications · 2024Article
- The ABCF proteins in Escherichia coli individually cope with 'hard-to-translate' nascent peptide sequences.Nucleic acids research · 2024Article
- Scientific Rationale and Clinical Basis for Clindamycin Use in the Treatment of Dermatologic Disease.Antibiotics (Basel, Switzerland) · 2024Review
- An antibiotic preorganized for ribosomal binding overcomes antimicrobial resistance.Science (New York, N.Y.) · 2024Article
- Phenomenological interpretations of the mechanism for the concentration-dependent positive effect of antibiotic lincomycin onApplied and environmental microbiology · 2023Article
- Genome-encoded ABCF factors implicated in intrinsic antibiotic resistance in Gram-positive bacteria: VmlR2, Ard1 and CplR.Nucleic acids research · 2023Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several ATPases in the ATP-binding cassette F (ABCF) family confer resistance to macrolides, lincosamides and streptogramins (MLS) antibiotics. MLS are structurally distinct classes, but inhibit a common target: the peptidyl transferase (PTC) active site of the ribosome. Antibiotic resistance (ARE) ABCFs have recently been shown to operate through direct ribosomal protection, but the mechanistic details of this resistance mechanism are lacking. Using a reconstituted translational system, we dissect the molecular mechanism of Staphylococcus haemolyticus VgaALC and Enterococcus faecalis LsaA on the ribosome. We demonstrate that VgaALC is an NTPase that operates as a molecular machine strictly requiring NTP hydrolysis (not just NTP binding) for antibiotic protection. Moreover, when bound to the ribosome in the NTP-bound form, hydrolytically inactive EQ2 ABCF ARE mutants inhibit peptidyl transferase activity, suggesting a direct interaction between the ABCF ARE and the PTC. The likely structural candidate responsible for antibiotic displacement by wild type ABCF AREs, and PTC inhibition by the EQ2 mutant, is the extended inter-ABC domain linker region. Deletion of the linker region renders wild type VgaALC inactive in antibiotic protection and the EQ2 mutant inactive in PTC inhibition.
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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.