Evidence map›Paper›PMID 38407413›Full record

ArticleNucleic acids research2024

Mechanistic insights into the alternative ribosome recycling by HflXr.

Savannah M Seely, Ritwika S Basu, Matthieu G Gagnon

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2024. 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 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. HflX mediates rifampicin resistance inFrontiers in microbiology · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. 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 · 2025
    Article
  9. Article
  10. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Savannah M SeelyDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Ritwika S BasuDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Matthieu G GagnonDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.ORCID 0000-0003-4516-604X
The University of Texas Medical Branch at Galveston · US

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
HOUSTON AREA MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008280 · NIGMS · RICE UNIVERSITY · PI WENSEL, THEODORE G · 1988 to 2023
$8.0M
Structural Basis for the Allosteric Mechanisms Regulating Ribosome FunctionR01GM136936 · NIGMS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI GAGNON, MATTHIEU · 2020 to 2024
$1.8M
NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R01 GM136936NIGMS NIH HHS T32 GM008280NIH HHS P41-GM103311NIH HHS R01-GM136936
6 · The paper itself

Abstract

During stress conditions such as heat shock and antibiotic exposure, ribosomes stall on messenger RNAs, leading to inhibition of protein synthesis. To remobilize ribosomes, bacteria use rescue factors such as HflXr, a homolog of the conserved housekeeping GTPase HflX that catalyzes the dissociation of translationally inactive ribosomes into individual subunits. Here we use time-resolved cryo-electron microscopy to elucidate the mechanism of ribosome recycling by Listeria monocytogenes HflXr. Within the 70S ribosome, HflXr displaces helix H69 of the 50S subunit and induces long-range movements of the platform domain of the 30S subunit, disrupting inter-subunit bridges B2b, B2c, B4, B7a and B7b. Our findings unveil a unique ribosome recycling strategy by HflXr which is distinct from that mediated by RRF and EF-G. The resemblance between HflXr and housekeeping HflX suggests that the alternative ribosome recycling mechanism reported here is universal in the prokaryotic kingdom.

Indexed as

Bacterial ProteinsCryoelectron MicroscopyListeria monocytogenesRibosomesModels, MolecularPeptide Elongation Factor GProtein BiosynthesisRibosomal ProteinsRibosome Subunits, Large, BacterialBacterial ProteinsPeptide Elongation Factor GRibosomal Proteins

Identifiers

PMID38407413
PMCPMC11040002
OpenAlexW4392168550

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.