Identification of an apparent aminoacyl-tRNA synthetase activator factor as tRNA nucleotidyltransferase.
作者信息
del Rio J M, Heredia C F
出版信息
Mol Cell Biochem. 1983;50(2):101-6. doi: 10.1007/BF00285636.
PMID:6855746
Abstract
The ability of yeast extracts to aminoacylate crude yeast tRNA with leucine and other amino acids is largely lost after chromatography of the extracts in DEAE-Sephadex. The original aminoacylating ability is restored by combining protein fractions from the DEAE-chromatogram. The characteristics of this reactivation are very similar to the activation, by protein factors, of certain aminoacyl-tRNA synthetases reported by others. The results in this work indicate that the apparent aminoacyl-tRNA synthetase activator factor is the tRNA nucleotidyltransferase and that the restoration of the original tRNA aminoacylating ability is a consequence of the repairing of the 3' end of incomplete tRNA chains.
摘要
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