ArticleNature structural & molecular biology2015
HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
What it found
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Who cites it
68 citing papers in PubMed, 99 citations in OpenAlex.
- Article
- Activation of the antibiotic resistance factor WhiB7 can stimulate aggregate biofilm formation in stationary phaseJournal of bacteriology · 2026Article
- Regulation of ribosome hibernation controlsmBio · 2026Article
- HflX mediates rifampicin resistance inFrontiers in microbiology · 2026Article
- The OsRqc1-OsVms1 module regulates the temperature threshold in thermo-sensitive genic male-sterile rice lines.Science China. Life sciences · 2025Article
- 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
- Plant MutS2 proteins function in plastid ribosome quality control.bioRxiv : the preprint server for biology · 2025Article
- Multifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance.Biochemical Society transactions · 2025Article
- A PDMS-based Microfluidic Chip Assembly for Time-Resolved Cryo-EM (TRCEM) Sample Preparation.Bio-protocol · 2025Article
- tRNA selectivity during ribosome-associated quality control regulates the critical sterility-inducing temperature in two-line hybrid rice.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- HflX-mediated drug resistance through ribosome splitting and rRNA disordering in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Time-resolved cryo-EM (TRCEM) sample preparation using a PDMS-based microfluidic chip assembly.bioRxiv : the preprint server for biology · 2024Article
- Unraveling the roles and mechanisms of mitochondrial translation in normal and malignant hematopoiesis.Journal of hematology & oncology · 2024Review
- RqcH supports survival in the absence of non-stop ribosome rescue factors.bioRxiv : the preprint server for biology · 2024Article
- Drug resistance through ribosome splitting and rRNA disordering in mycobacteria.bioRxiv : the preprint server for biology · 2024Article
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- Article
- Insights into the function of the chloroplastic ribosome-associated GTPase high frequency of lysogenization X inPlant direct · 2024Article
- Ancestors in the Extreme: A Genomics View of Microbial Diversity in Hypersaline Aquatic Environments.Results and problems in cell differentiation · 2024Article
- 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
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adverse cellular conditions often lead to nonproductive translational stalling and arrest of ribosomes on mRNAs. Here, we used fast kinetics and cryo-EM to characterize Escherichia coli HflX, a GTPase with unknown function. Our data reveal that HflX is a heat shock-induced ribosome-splitting factor capable of dissociating vacant as well as mRNA-associated ribosomes with deacylated tRNA in the peptidyl site. Structural data demonstrate that the N-terminal effector domain of HflX binds to the peptidyl transferase center in a strikingly similar manner as that of the class I release factors and induces dramatic conformational changes in central intersubunit bridges, thus promoting subunit dissociation. Accordingly, loss of HflX results in an increase in stalled ribosomes upon heat shock. These results suggest a primary role of HflX in rescuing translationally arrested ribosomes under stress conditions.
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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.