Evolutionary Basis of Converting a Bacterial tRNA Synthetase into a Yeast Cytoplasmic or Mitochondrial Enzyme

NCU Institutional Repository > 生醫理工學院 > 生命科學研究所 > 期刊論文 > Item 987654321/27758

jsp.display-item.identifier=請使用永久網址來引用或連結此文件: http://ir.lib.ncu.edu.tw/handle/987654321/27758

题名:	Evolutionary Basis of Converting a Bacterial tRNA Synthetase into a Yeast Cytoplasmic or Mitochondrial Enzyme
作者:	Chiu,WC;Chang,CP;Wang,CC
贡献者:	生命科學研究所
关键词:	METHIONYL-TRANSFER-RNA;ELONGATION FACTOR-I;SACCHAROMYCES-CEREVISIAE;BINDING DOMAIN;MULTISYNTHETASE COMPLEX;RABBIT LIVER;GENE ENCODES;AMINOACYLATION;TRANSLATION;FEATURES
日期:	2009
上传时间:	2010-06-29 19:28:57 (UTC+8)
出版者:	中央大學
摘要:	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.
關聯:	JOURNAL OF BIOLOGICAL CHEMISTRY
显示于类别:	[生命科學研究所 ] 期刊論文

文件中的档案:

档案	描述	大小	格式	浏览次数
index.html		0Kb	HTML	1028	检视/开启

在NCUIR中所有的数据项都受到原著作权保护.

社群 sharing

数据加载中.....