Evidence map›Paper›PMID 22921065›Full record

ArticleChemistry & biology2012

A Role for the 2' OH of peptidyl-tRNA substrate in peptide release on the ribosome revealed through RF-mediated rescue.

Jeffrey J Shaw, Stefan Trobro, Shan L He, Johan Åqvist, Rachel Green

Abstract read
In one paragraph

Article in Chemistry & biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Metabolic stress promotes stop-codon readthrough and phenotypic heterogeneity.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Review
  8. Ribosome Structure, Function, and Early Evolution.International journal of molecular sciences · 2018
    Review
  9. Decoding on the ribosome depends on the structure of the mRNA phosphodiester backbone.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Article
  11. Review
  12. Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Review
  14. 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

5 authors at 3 institutions in 2 countries.

Jeffrey J ShawDepartment of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Stefan Trobro
Shan L He
Johan Åqvist
Rachel Green
Howard Hughes Medical Institute · USUppsala University · SEJohns Hopkins University · US

Funding

The role played by the RNAs and tRNAs in translationR01GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1999 to 2013
$3.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM059425NIGMS NIH HHS R01GM059425
6 · The paper itself

Abstract

The 2' OH of the peptidyl-tRNA substrate is thought to be important for catalysis of both peptide bond formation and peptide release in the ribosomal active site. The release reaction also specifically depends on a release factor protein (RF) to hydrolyze the ester linkage of the peptidyl-tRNA upon recognition of stop codons in the A site. Here, we demonstrate that certain amino acid substitutions (in particular those containing hydroxyl or thiol groups) in the conserved GGQ glutamine of release factor RF1 can rescue defects in the release reaction associated with peptidyl-tRNA substrates lacking a 2' OH. We explored this rescue effect through biochemical and computational approaches that support a model where the 2' OH of the P-site substrate is critical for orienting the nucleophile in a hydrogen-bonding network productive for catalysis.

Indexed as

Amino Acid SubstitutionBiocatalysisCatalytic DomainCodon, TerminatorHydrogen BondingHydrogen-Ion ConcentrationHydroxidesMolecular Dynamics SimulationPeptidesPeptide Termination FactorsRibosomesRNA, Transfer, Amino AcylSolventsSubstrate SpecificityCodon, TerminatorHydroxidesPeptidesPeptide Termination FactorsRNA, Transfer, Amino AcylSolventstRNA, peptidyl-

Identifiers

PMID22921065
PMCPMC3487719
OpenAlexW2018865499

What OpenQuestion holds

Textmetadata
LicenceTDM
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.