Evidence map›Paper›PMID 18755686›Full record

ArticleThe Journal of biological chemistry2008

Promoting the formation of an active synthetase/tRNA complex by a nonspecific tRNA-binding domain.

Chia-Pei Chang, Grace Lin, Shun-Jia Chen, Wen-Chih Chiu, Wen-Heng Chen, Chien-Chia Wang

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In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Chia-Pei ChangDepartment of Life Science, National Central University, Jung-li, 32001 Taiwan.
Grace Lin
Shun-Jia Chen
Wen-Chih Chiu
Wen-Heng Chen
Chien-Chia Wang
National Central University · TWInstitute of Nuclear Energy Research · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous studies showed that valyl-tRNA synthetase of Saccharomyces cerevisiae contains an N-terminal polypeptide extension of 97 residues, which is absent from its bacterial relatives, but is conserved in its mammalian homologues. We showed herein that this appended domain and its human counterpart are both nonspecific tRNA-binding domains (K(d) approximately 0.5 microm). Deletion of the appended domain from the yeast enzyme severely impaired its tRNA binding, aminoacylation, and complementation activities. This N-domain-deleted yeast valyl-tRNA synthetase mutant could be rescued by fusion of the equivalent domain from its human homologue. Moreover, fusion of the N-domain of the yeast enzyme or its human counterpart to Escherichia coli glutaminyl-tRNA synthetase enabled the otherwise "inactive" prokaryotic enzyme to function as a yeast enzyme in vivo. Different from the native yeast enzyme, which showed different affinities toward mixed tRNA populations, the fusion enzyme exhibited similar binding affinities for all yeast tRNAs. These results not only underscore the significance of nonspecific tRNA binding in aminoacylation, but also provide insights into the mechanism of the formation of aminoacyl-tRNAs.

Indexed as

Amino Acyl-tRNA SynthetasesEscherichia coliEscherichia coli ProteinsHumansProtein BindingProtein Structure, TertiaryRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTransfer RNA AminoacylationValine-tRNA LigaseAmino Acyl-tRNA SynthetasesEscherichia coli Proteinsglutaminyl-tRNA synthetaseRNA, TransferSaccharomyces cerevisiae ProteinsValine-tRNA Ligase

Identifiers

PMID18755686
PMCPMC2662155
OpenAlexW2032866042

What OpenQuestion holds

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Registered trials

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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.