Evidence map›Paper›PMID 21622559›Full record

ArticleThe Journal of biological chemistry2011

Helix 69 is key for uniformity during substrate selection on the ribosome.

Rodrigo F Ortiz-Meoz, Rachel Green

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Disruption of evolutionarily correlated tRNA elements impairs accurate decoding.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  6. 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
  7. Article
  8. Intersubunit Bridges of the Bacterial Ribosome.Journal of molecular biology · 2016
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Allosteric control of the ribosome by small-molecule antibiotics.Nature structural & molecular biology · 2012
    Article
  16. Article
  17. Article
  18. 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.

Rodrigo F Ortiz-MeozHoward Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Rachel Green

Funding

Molecular mechanisms of ribosome pausing and the cellular responseR37GM059425 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 2014 to 2023
$3.5M
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 GM059425NIGMS NIH HHS R01 GM059425NIGMS NIH HHS R37 GM059425
6 · The paper itself

Abstract

Structural studies of ribosome complexes with bound tRNAs and release factors show considerable contacts between these factors and helix 69 (H69) of 23 S rRNA. Although biochemical and genetic studies have provided some general insights into the role of H69 in tRNA and RF selection, a detailed understanding of these contributions remains elusive. Here, we present a pre- steady-state kinetic analysis establishing that two distinct regions of H69 make critical contributions to substrate selection. The loop of H69 (A1913) forms contacts necessary for the efficient accommodation of a subset of natural tRNA species, whereas the base of the stem (G1922) is specifically critical for UGA codon recognition by the class 1 release factor RF2. These data define a broad and critical role for this centrally located intersubunit helix (H69) in accurate and efficient substrate recognition by the ribosome.

Indexed as

Nucleic Acid ConformationCodon, TerminatorEscherichia coliEscherichia coli ProteinsKineticsModels, MolecularMutationPeptide Termination FactorsProtein BiosynthesisProtein ConformationRibosomesRNA, BacterialRNA, Ribosomal, 23SRNA, TransferSubstrate SpecificityCodon, TerminatorEscherichia coli ProteinsPeptide Termination FactorsprfB protein, E coliRNA, BacterialRNA, Ribosomal, 23SRNA, Transfer

Identifiers

PMID21622559
PMCPMC3138323

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.