Evidence map›Paper›PMID 21768119›Full record

ArticleThe Journal of biological chemistry2011

Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons.

Byung Ran So, Songon An, Sandeep Kumar, Mom Das, Daniel A Turner, Christopher M Hadad, Karin Musier-Forsyth

Open access · hybridAbstract 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 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  6. Conformational and chemical selection by aProceedings of the National Academy of Sciences of the United States of America · 2017
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  11. Emergence and evolution.Topics in current chemistry · 2014
    Review
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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

7 authors at 2 institutions in 1 country.

Byung Ran SoDepartment of Chemistry, Ohio State University, Columbus, Ohio 43210, USA.
Songon An
Sandeep Kumar
Mom Das
Daniel A Turner
Christopher M Hadad
Karin Musier-Forsyth
The Ohio State University · USUniversity of Minnesota · US

Funding

CLASS II AMINOACYL-TRNA SYNTHETASE SUBSTRATE RECOGNITIONR01GM049928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUSIER-FORSYTH, KARIN M · 1996 to 2012
$4.0M
CLASS II AMINOACYL-TRNA SYNTHETASE SUBSTRATE RECOGNITIONR29GM049928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUSIER-FORSYTH, KARIN M · 1994 to 1996
–
CLASS II AMINOACYL-TRNA SYNTHETASE SUBSTRATE RECOGNITIONR55GM049928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUSIER-FORSYTH, KARIN M · 1993 to 1993
–
NIGMS NIH HHS GM049928NIGMS NIH HHS R01 GM049928
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases attach specific amino acids to cognate tRNAs. Prolyl-tRNA synthetases are known to mischarge tRNA(Pro) with the smaller amino acid alanine and with cysteine, which is the same size as proline. Quality control in proline codon translation is partly ensured by an editing domain (INS) present in most bacterial prolyl-tRNA synthetases that hydrolyzes smaller Ala-tRNA(Pro) and excludes Pro-tRNA(Pro). In contrast, Cys-tRNA(Pro) is cleared by a freestanding INS domain homolog, YbaK. Here, we have investigated the molecular mechanism of catalysis and substrate recognition by Hemophilus influenzae YbaK using site-directed mutagenesis, enzymatic assays of isosteric substrates and functional group analogs, and computational modeling. These studies together with mass spectrometric characterization of the YbaK-catalyzed reaction products support a novel substrate-assisted mechanism of Cys-tRNA(Pro) deacylation that prevents nonspecific Pro-tRNA(Pro) hydrolysis. Collectively, we propose that the INS and YbaK domains co-evolved distinct mechanisms involving steric exclusion and thiol-specific chemistry, respectively, to ensure accurate decoding of proline codons.

Indexed as

CodonProtein BiosynthesisAcylationAmino Acyl-tRNA SynthetasesBacterial ProteinsBiocatalysisCatalysisHaemophilus influenzaeHydrolysisMutagenesis, Site-DirectedProlineProtein Structure, TertiaryRNA, Transfer, Amino AcylSubstrate SpecificityAmino Acyl-tRNA SynthetasesBacterial ProteinsCodonProlineRNA, Transfer, Amino AcylYbaK protein, Haemophilus influenzae

Identifiers

PMID21768119
PMCPMC3173103
OpenAlexW2088459429

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.