Evidence map›Paper›PMID 20660012›Full record

ArticleNucleic acids research2010

A molecular clamp ensures allosteric coordination of peptidyltransfer and ligand binding to the ribosomal A-site.

Arturas Meskauskas, Jonathan D Dinman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

33 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Nervous-Like Circuits in the Ribosome Facts, Hypotheses and Perspectives.International journal of molecular sciences · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Article
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  20. 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

2 authors at 2 institutions in 2 countries.

Arturas MeskauskasDepartment of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA. artmeska@umd.edu
Jonathan D Dinman
University of Maryland, College Park · USVilnius University · LT

Funding

Translational Fidelity in EukaryotesR01GM058859 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI DINMAN, JONATHAN D · 1999 to 2011
$3.8M
NIGMS NIH HHS 5 R01 GM058859NIGMS NIH HHS R01 GM058859
6 · The paper itself

Abstract

Although the ribosome is mainly comprised of rRNA and many of its critical functions occur through RNA-RNA interactions, distinct domains of ribosomal proteins also participate in switching the ribosome between different conformational/functional states. Prior studies demonstrated that two extended domains of ribosomal protein L3 form an allosteric switch between the pre- and post-translocational states. Missing was an explanation for how the movements of these domains are communicated among the ribosome's functional centers. Here, a third domain of L3 called the basic thumb, that protrudes roughly perpendicular from the W-finger and is nestled in the center of a cagelike structure formed by elements from three separate domains of the large subunit rRNA is investigated. Mutagenesis of basically charged amino acids of the basic thumb to alanines followed by detailed analyses suggests that it acts as a molecular clamp, playing a role in allosterically communicating the ribosome's tRNA occupancy status to the elongation factor binding region and the peptidyltransferase center, facilitating coordination of their functions through the elongation cycle. The observation that these mutations affected translational fidelity, virus propagation and cell growth demonstrates how small structural changes at the atomic scale can propagate outward to broadly impact the biology of cell.

Indexed as

Allosteric RegulationBinding SitesFrameshifting, RibosomalLigandsModels, MolecularMutationPeptide Elongation Factor 2Peptidyl TransferasesRibosomal Protein L3Ribosomal ProteinsRibosomesRNA, RibosomalRNA, Transfer, Amino AcylYeastsLigandsPeptide Elongation Factor 2Peptidyl TransferasesRibosomal Protein L3Ribosomal ProteinsRNA, RibosomalRNA, ribosomal, 25SRNA, Transfer, Amino Acyl

Identifiers

PMID20660012
PMCPMC2995063
OpenAlexW1984878181

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.