Evidence map›Paper›PMID 25085895›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

The ribosome uses cooperative conformational changes to maximize and regulate the efficiency of translation.

Wei Ning, Jingyi Fei, Ruben L Gonzalez

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Partial spontaneous intersubunit rotations in pretranslocation ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  2. Article
  3. Entropic control of the free-energy landscape of an archetypal biomolecular machine.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Three tRNAs on the ribosome slow translation elongation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. Article
  16. Structural insights into ribosome translocation.Wiley interdisciplinary reviews. RNA · 2016
    Review
  17. Elongation factor G initiates translocation through a power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Intersubunit Bridges of the Bacterial Ribosome.Journal of molecular biology · 2016
    Review
  19. Review
  20. Molecular mechanism of viomycin inhibition of peptide elongation in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

3 authors at 1 institution in 1 country.

Wei NingDepartment of Chemistry, Columbia University, New York, NY 10027.
Jingyi FeiDepartment of Chemistry, Columbia University, New York, NY 10027.
Ruben L GonzalezDepartment of Chemistry, Columbia University, New York, NY 10027 rlg2118@columbia.edu.
Columbia University · US

Funding

The Structural Dynamics of Translation InitiationR01GM084288 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI GONZALEZ, RUBEN L · 2009 to 2022
$4.4M
NIGMS NIH HHS GM 084288NIGMS NIH HHS R01 GM084288
6 · The paper itself

Abstract

One of the most challenging unanswered questions regarding the structural biology of biomolecular machines such as the two-subunit ribosome is whether and how these machines coordinate seemingly independent and random conformational fluctuations to maximize and regulate their functional efficiencies. To address this question, we have used ribosome mutagenesis or a ribosome-targeting antibiotic to predictably perturb the dynamics of intersubunit rotation, a structural rearrangement of the ribosome that is essential for the translocation and ejection of ribosome-bound tRNAs during translation. Concomitantly, we have used single-molecule fluorescence resonance energy transfer (smFRET) to characterize the effects of these perturbations on the dynamics of ribosomal L1 stalk movements and ribosome-bound tRNA reconfigurations, conformational changes that are likewise essential for the translocation and ejection of tRNAs during translation. Together with the results of complementary biochemical studies, our smFRET studies demonstrate that the ribosome uses cooperative conformational changes to maximize and regulate the efficiency with which it translocates and ejects tRNAs during translation. We propose that the ribosome employs cooperative conformational changes to efficiently populate global conformational states that are productive for translation, that translation factors exploit this cooperativity as part of their mechanisms of action, and that antibiotics exploit it to maximize the potency with which they inhibit translation. It is likely that similar cooperative conformational changes underlie the function and regulation of other biomolecular machines.

Indexed as

Protein BiosynthesisFluorescence Resonance Energy TransferNucleic Acid ConformationRibosomesRNA, TransferStatic ElectricityRNA, Transfer

Identifiers

PMID25085895
PMCPMC4143051
OpenAlexW2105162317

What OpenQuestion holds

Textmetadata
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.