Evidence map›Paper›PMID 36924943›Full record

ArticleThe Journal of biological chemistry2023

Structural basis for reduced ribosomal A-site fidelity in response to P-site codon-anticodon mismatches.

Ha An Nguyen, Eric D Hoffer, Crystal E Fagan, Tatsuya Maehigashi, Christine M Dunham

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ha An NguyenDepartment of Chemistry, Emory University, Atlanta, Georgia, USA; Emory Antibiotic Resistance Center (ARC), Emory University, Atlanta, Georgia, USA.
Eric D HofferEmory Antibiotic Resistance Center (ARC), Emory University, Atlanta, Georgia, USA; Biochemistry, Cell and Developmental Biology Graduate Program, Emory University, Atlanta, Georgia, USA.
Crystal E FaganEmory Antibiotic Resistance Center (ARC), Emory University, Atlanta, Georgia, USA; Biochemistry, Cell and Developmental Biology Graduate Program, Emory University, Atlanta, Georgia, USA.
Tatsuya MaehigashiDepartment of Chemistry, Emory University, Atlanta, Georgia, USA; Emory Antibiotic Resistance Center (ARC), Emory University, Atlanta, Georgia, USA.
Christine M DunhamDepartment of Chemistry, Emory University, Atlanta, Georgia, USA; Emory Antibiotic Resistance Center (ARC), Emory University, Atlanta, Georgia, USA. Electronic address: christine.m.dunham@emory.edu.
Emory University · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
Training Program in Biochemistry, Cell and Molecular BiologyT32GM008367 · NIGMS · EMORY UNIVERSITY · PI BOISE, LAWRENCE H., CORBETT, ANITA H. · 1990 to 2019
$5.6M
Structural Studies of Ribosome RegulationR01GM093278 · NIGMS · EMORY UNIVERSITY · PI DUNHAM, CHRISTINE M · 2010 to 2022
$4.6M
NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM093278NIGMS NIH HHS T32 GM008367
6 · The paper itself

Abstract

Rapid and accurate translation is essential in all organisms to produce properly folded and functional proteins. mRNA codons that define the protein-coding sequences are decoded by tRNAs on the ribosome in the aminoacyl (A) binding site. The mRNA codon and the tRNA anticodon interaction is extensively monitored by the ribosome to ensure accuracy in tRNA selection. While other polymerases that synthesize DNA and RNA can correct for misincorporations, the ribosome is unable to correct mistakes. Instead, when a misincorporation occurs, the mismatched tRNA-mRNA pair moves to the peptidyl (P) site and, from this location, causes a reduction in the fidelity at the A site, triggering post-peptidyl transfer quality control. This reduced fidelity allows for additional incorrect tRNAs to be accepted and for release factor 2 (RF2) to recognize sense codons, leading to hydrolysis of the aberrant peptide. Here, we present crystal structures of the ribosome containing a tRNA

Indexed as

AnticodonCodonRibosomesRNA, RibosomalBase Pair MismatchModels, MolecularNucleic Acid ConformationNucleotidesProtein BiosynthesisRNA, MessengerRNA, TransferAnticodonCodonNucleotidesRNA, MessengerRNA, RibosomalRNA, TransferfidelitymiscodingmRNAnear cognateribosometranslationtRNA

Identifiers

PMID36924943
PMCPMC10140155
OpenAlexW4324135199

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.