Evidence map›Paper›PMID 21378964›Full record

ArticleNature structural & molecular biology2011

How mutations in tRNA distant from the anticodon affect the fidelity of decoding.

T Martin Schmeing, Rebecca M Voorhees, Ann C Kelley, V Ramakrishnan

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

85 citing papers in PubMed, 137 citations in OpenAlex.

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  14. Tuning tRNAs for improved translation.Frontiers in genetics · 2024
    Review
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  17. Genes · 2023
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25 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

T Martin SchmeingMRC Laboratory of Molecular Biology, Cambridge, UK. martin.schmeing@mcgill.ca
Rebecca M Voorhees
Ann C Kelley
V Ramakrishnan
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184332Medical Research Council U.1051.04.018(78935)Wellcome Trust 082086
6 · The paper itself

Abstract

The ribosome converts genetic information into protein by selecting aminoacyl tRNAs whose anticodons base-pair to an mRNA codon. Mutations in the tRNA body can perturb this process and affect fidelity. The Hirsh suppressor is a well-studied tRNA(Trp) harboring a G24A mutation that allows readthrough of UGA stop codons. Here we present crystal structures of the 70S ribosome complexed with EF-Tu and aminoacyl tRNA (native tRNA(Trp), G24A tRNA(Trp) or the miscoding A9C tRNA(Trp)) bound to cognate UGG or near-cognate UGA codons, determined at 3.2-Å resolution. The A9C and G24A mutations lead to miscoding by facilitating the distortion of tRNA required for decoding. A9C accomplishes this by increasing tRNA flexibility, whereas G24A allows the formation of an additional hydrogen bond that stabilizes the distortion. Our results also suggest that each native tRNA will adopt a unique conformation when delivered to the ribosome that allows accurate decoding.

Indexed as

AnticodonMutationBase SequenceCodonCrystallography, X-RayModels, MolecularNucleic Acid ConformationRNA, TransferAnticodonCodonRNA, Transfer

Identifiers

PMID21378964
PMCPMC3072312
OpenAlexW2156400868

What OpenQuestion holds

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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.