An aminoacyl tRNA synthetase whose sequence fits into neither of the two known classes
Article Abstract:
Research into aminoacyl transfer RNA synthetases is described. It is shown that MJ1477 and its homologues are the first tRNA synthases whose sequences do not fit into the two known classes of synthases.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2001
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Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
Article Abstract:
The mouse sticky mutation, which causes cerebellar Purkinje cell loss and ataxia, is a missense mutation in the editing domain of the alanyl-transfer RNAs (tRNAs) is reported. The results have shown that disruption of translational fidelity in terminally differentiated neurons have led to the accumulation of misfolded proteins and cell death, and have provided a novel mechanism underlying neurodegeneration.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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Distinct domains of tRNA synthetase recognize the same base pair
Article Abstract:
The prevention of the synthesis of proteins with errors by the aminoacyl transfer RNA synthetases is discussed. The analysis shows that the same base pair is recognized by the different domains of a tRNA synthetase.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2008
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