Isolation of a single polypeptide leucyl-tRNA synthetase from bakers' yeast1
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منابع مشابه
Cytoplasmic Methionyl - tRNA Synthetase from Bakers ’ Yeast
Methionyl-tRNA synthetase has been purified from a yeast strain carrying the MESl structural gene on a high copy number plasmid (pFL1). The purified enzyme is a monomer of M, = 85,000 in contrast to its counterpart from Escherichia coli which is a dimer made up of identical subunits (M, = 76,000; Dardel, F., Fayat, G., and Blanquet, S . (1984) J. Bucteriol. 160,1115-1122). The yeast enzyme was ...
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The specific activities of 15 aminoacyl-tRNA synthetases in Saccharomyces cerevisiae were measured after growth under a variety of conditions that produced a range of cell-doubling times. The specific activity of each synthetase increased as cell-doubling time decreased. Control experiments eliminate the possibility that these results are due to preferential recovery of synthetases, or to the p...
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The editing reactions catalyzed by aminoacyl-tRNA synthetases are critical for the faithful protein synthesis by correcting misactivated amino acids and misaminoacylated tRNAs. We report that the isolated editing domain of leucyl-tRNA synthetase from the deep-rooted bacterium Aquifex aeolicus (alphabeta-LeuRS) catalyzes the hydrolytic editing of both mischarged tRNA(Leu) and minihelix(Leu). Wit...
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Several aminoacyl-tRNA synthetases have been reported to be overexpressed for charging essential aminoacyl-tRNAs in many cancer types. In this study, we aimed to explore the potential role of leucyl-tRNA synthetase (LARS) as an anticancer target. MTT assay was performed to screen inhibitors to human LARS (hsLARS) from compounds AN2690 and its derivatives, compounds 1-6, in U2OS and SKOV3 cells....
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1979
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/6.11.3651