RECOGNITION OF YEAST TRANSFER RNA(PHE) BY ITS COGNATE YEAST PHENYLALANYL-TRANSFER RNA-SYNTHETASE - AN ANALYSIS OF SPECIFICITY

被引：53

作者：

SAMPSON, JR ^{[1
]}

BEHLEN, LS ^{[1
]}

DIRENZO, AB ^{[1
]}

UHLENBECK, OC ^{[1
]}

机构：

[1] UNIV COLORADO, DEPT CHEM & BIOCHEM, BOULDER, CO 80309 USA

来源：

BIOCHEMISTRY | 1992年 / 31卷 / 17期

关键词：

D O I：

10.1021/bi00132a002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A kinetic analysis of aminoacylation of mutant yeast tRNA(Phe) transcripts by its cognate yeast phenylalanyl-tRNA synthetase (FRS) reveals five nucleotides in tRNA(Phe) as major recognition sites for FRS. The aminoacylation kinetics for two double mutants suggest that each of the five recognition sites contributes independently to k(cat)/K(M). Measured kinetic values for the mutants presented here and those reported previously were then used to calculate the predicted k(cat)/K(M)of misacylation for a number of noncognate tRNAs. The predicted k(cat)/K(M) values are consistent with values measured by other investigators and thus support the five-nucleotide recognition model. The k(cat)/K(M) of misacylation for all known yeast tRNAs has been calculated on the basis of this model, and the specificity of FRS for tRNA(Phe) in yeast is discussed.

引用

页码：4161 / 4167

页数：7

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