ArticleNucleic acids research2016
The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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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
30 citing papers in PubMed, 44 citations in OpenAlex.
- HflX mediates rifampicin resistance inFrontiers in microbiology · 2026Article
- Defective Ribosome Recycling: A Bridge Between Translation Fidelity, Organelle Dysfunction, and Diseases: Exploring How Flawed Ribosome Recycling Factors Impact Ribosome Metabolism and Organelle Homeostasis, Leading to Human Diseases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- Article
- Application of bio-layer interferometry for the analysis of ribosome-protein interactions.Frontiers in molecular biosciences · 2024Article
- Insights into the function of the chloroplastic ribosome-associated GTPase high frequency of lysogenization X inPlant direct · 2024Article
- Phenomenological interpretations of the mechanism for the concentration-dependent positive effect of antibiotic lincomycin onApplied and environmental microbiology · 2023Article
- Time resolution in cryo-EM using a novel PDMS-based microfluidic chip assembly and its application to the study of HflX-mediated ribosome recycling.bioRxiv : the preprint server for biology · 2023Article
- At the Crossroad of Nucleotide Dynamics and Protein Synthesis in Bacteria.Microbiology and molecular biology reviews : MMBR · 2023Review
- Structure of Escherichia coli heat shock protein Hsp15 in complex with the ribosomal 50S subunit bearing peptidyl-tRNA.Nucleic acids research · 2022Article
- Structural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes.Nucleic acids research · 2022Article
- Mechanisms of ribosome recycling in bacteria and mitochondria: a structural perspective.RNA biology · 2022Review
- Human Mitoribosome Biogenesis and Its Emerging Links to Disease.International journal of molecular sciences · 2021Review
- HflX is a GTPase that controls hypoxia-induced replication arrest in slow-growing mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Dual function of GTPBP6 in biogenesis and recycling of human mitochondrial ribosomes.Nucleic acids research · 2020Article
- Functional Analysis of BipA in E. coli Reveals the Natural Plasticity of 50S Subunit Assembly.Journal of molecular biology · 2020Article
- The hibernating 100S complex is a target of ribosome-recycling factor and elongation factor G inThe Journal of biological chemistry · 2020Article
- The feather degradation mechanisms of a new Streptomyces sp. isolate SCUT-3.Communications biology · 2020Article
- Article
- Mycobacterial HflX is a ribosome splitting factor that mediates antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Using a combination of biochemical, structural probing and rapid kinetics techniques we reveal for the first time that the universally conserved translational GTPase (trGTPase) HflX binds to the E-site of the 70S ribosome and that its GTPase activity is modulated by peptidyl transferase centre (PTC) and peptide exit tunnel (PET) binding antibiotics, suggesting a previously undescribed mode of action for these antibiotics. Our rapid kinetics studies reveal that HflX functions as a ribosome splitting factor that disassembles the 70S ribosomes into its subunits in a nucleotide dependent manner. Furthermore, our probing and hydrolysis studies show that the ribosome is able to activate trGTPases bound to its E-site. This is, to our knowledge, the first case in which the hydrolytic activity of a translational GTPase is not activated by the GTPase activating centre (GAC) in the ribosomal A-site. Furthermore, we provide evidence that the bound state of the PTC is able to regulate the GTPase activity of E-site bound HflX.
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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.