Evidence map›Paper›PMID 34117118›Full record

ArticleRNA (New York, N.Y.)2021

Perturbation of ribosomal subunit dynamics by inhibitors of tRNA translocation.

Riccardo Belardinelli, Heena Sharma, Frank Peske, Marina V Rodnina

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Mechanism of read-through enhancement by aminoglycosides and mefloquine.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. The role of GTP hydrolysis by EF-G in ribosomal translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Review
  8. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Riccardo BelardinelliDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.ORCID 0000-0002-3333-0466
Heena SharmaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.
Frank PeskeDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.
Marina V RodninaDepartment of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.ORCID 0000-0003-0105-3879
Max Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many antibiotics that bind to the ribosome inhibit translation by blocking the movement of tRNAs and mRNA or interfering with ribosome dynamics, which impairs the formation of essential translocation intermediates. Here we show how translocation inhibitors viomycin (Vio), neomycin (Neo), paromomycin (Par), kanamycin (Kan), spectinomycin (Spc), hygromycin B (HygB), and streptomycin (Str, an antibiotic that does not inhibit tRNA movement), affect principal motions of the small ribosomal subunits (SSU) during EF-G-promoted translocation. Using ensemble kinetics, we studied the SSU body domain rotation and SSU head domain swiveling in real time. We show that although antibiotics binding to the ribosome can favor a particular ribosome conformation in the absence of EF-G, their kinetic effect on the EF-G-induced transition to the rotated/swiveled state of the SSU is moderate. The antibiotics mostly inhibit backward movements of the SSU body and/or the head domains. Vio, Spc, and high concentrations of Neo completely inhibit the backward movements of the SSU body and head domain. Kan, Par, HygB, and low concentrations of Neo slow down both movements, but their sequence and coordination are retained. Finally, Str has very little effect on the backward rotation of the SSU body domain, but retards the SSU head movement. The data underscore the importance of ribosome dynamics for tRNA-mRNA translocation and provide new insights into the mechanism of antibiotic action.

Indexed as

Anti-Bacterial AgentsBiological TransportCinnamatesEscherichia coliHygromycin BKanamycinKineticsNeomycinParomomycinPeptide Elongation Factor GProtein BiosynthesisRibosome SubunitsRNA, MessengerRNA, TransferSpectinomycinStreptomycinAnti-Bacterial AgentsCinnamateshygromycin AHygromycin BKanamycinNeomycinParomomycinPeptide Elongation Factor GRNA, MessengerRNA, TransferSpectinomycinStreptomycinViomycinantibioticsEF-Grapid kineticsribosome head domain swivelingribosome subunit rotationtranslation elongation

Identifiers

PMID34117118
PMCPMC8370747
OpenAlexW3136050798

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.