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    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/27758


    Title: Evolutionary Basis of Converting a Bacterial tRNA Synthetase into a Yeast Cytoplasmic or Mitochondrial Enzyme
    Authors: Chiu,WC;Chang,CP;Wang,CC
    Contributors: 生命科學研究所
    Keywords: METHIONYL-TRANSFER-RNA;ELONGATION FACTOR-I;SACCHAROMYCES-CEREVISIAE;BINDING DOMAIN;MULTISYNTHETASE COMPLEX;RABBIT LIVER;GENE ENCODES;AMINOACYLATION;TRANSLATION;FEATURES
    Date: 2009
    Issue Date: 2010-06-29 19:28:57 (UTC+8)
    Publisher: 中央大學
    Abstract: Previous studies showed that cytoplasmic and mitochondrial forms of yeast valyl-tRNA synthetase (ValRS) are specified by the VAS1 gene through alternative initiation of translation. Sequence comparison suggests that the yeast cytoplasmic (or mature mitochondrial) ValRS contains an N-terminal appendage that acts in cis as a nonspecific tRNA-binding domain (TRBD) and is absent from its bacterial relatives. We show here that Escherichia coli ValRS can substitute for the mitochondrial and cytoplasmic functions of VAS1 by fusion of a mitochondrial targeting signal and a TRBD, respectively. In addition, the bacterial ValRS gene can be converted into a dual functional yeast gene encoding both cytoplasmic and mitochondrial activities by fusion of a DNA sequence specifying both the mitochondrial targeting signal and TRBD. In vitro assays suggested that fusion of a nonspecific TRBD to the bacterial enzyme significantly enhanced its yeast tRNA-binding and aminoacylation activities. These results not only underscore the necessity of retaining a TRBD for functioning of a tRNA synthetase in yeast cytoplasm, but also provide insights into the evolution of tRNA synthetase genes.
    Relation: JOURNAL OF BIOLOGICAL CHEMISTRY
    Appears in Collections:[生命科學研究所 ] 期刊論文

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