La maladie de Parkinson en France (serveur d'exploration)

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Identification of Lethal Mutations in Yeast Threonyl-tRNA Synthetase Revealing Critical Residues in Its Human Homolog*

Identifieur interne : 001574 ( Ncbi/Curation ); précédent : 001573; suivant : 001575

Identification of Lethal Mutations in Yeast Threonyl-tRNA Synthetase Revealing Critical Residues in Its Human Homolog*

Auteurs : Zhi-Rong Ruan ; Zhi-Peng Fang ; Qing Ye ; Hui-Yan Lei ; Gilbert Eriani [France] ; Xiao-Long Zhou ; En-Duo Wang

Source :

RBID : PMC:4340410

Abstract

Background: Eukaryotic ThrRSs exhibit four structural domains similar to bacterial ThrRSs and evolve a eukaryote-specific N-terminal extension domain.

Results: Essential roles of 12 crucial residues in aminoacylation and editing reactions were revealed.

Conclusion: The identified critical residues affected activities of ThrRS in various manners.

Significance: We elucidated the synthetic and editing functions of selected residues and confirmed the functional consistency between yeast and human ThrRSs.


Url:
DOI: 10.1074/jbc.M114.599886
PubMed: 25416776
PubMed Central: 4340410

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PMC:4340410

Le document en format XML

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<bold>Background:</bold>
Eukaryotic ThrRSs exhibit four structural domains similar to bacterial ThrRSs and evolve a eukaryote-specific N-terminal extension domain.</p>
<p>
<bold>Results:</bold>
Essential roles of 12 crucial residues in aminoacylation and editing reactions were revealed.</p>
<p>
<bold>Conclusion:</bold>
The identified critical residues affected activities of ThrRS in various manners.</p>
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<bold>Significance:</bold>
We elucidated the synthetic and editing functions of selected residues and confirmed the functional consistency between yeast and human ThrRSs.</p>
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