SELECTION OF SUPPRESSOR METHIONYL-TRANSFER-RNA SYNTHETASES - MAPPING THE TRANSFER-RNA ANTICODON BINDING-SITE

被引：86

作者：

MEINNEL, T ^{[1
]}

MECHULAM, Y ^{[1
]}

LECORRE, D ^{[1
]}

PANVERT, M ^{[1
]}

BLANQUET, S ^{[1
]}

FAYAT, G ^{[1
]}

机构：

[1] ECOLE POLYTECH, BIOCHIM LAB, CNRS, UA 240, F-91128 PALAISEAU, FRANCE

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 01期

关键词：

AMINOACYL-TRANSFER-RNA SYNTHETASE; PROTEIN NUCLEIC ACID INTERACTIONS; TRANSFER-RNA DISCRIMINATION; SITE-DIRECTED MUTAGENESIS;

D O I：

10.1073/pnas.88.1.291

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Accurate aminoacylation of a tRNA by Escherichia coli methionyl-tRNA synthetase (MYS) is specified by the CAU anticodon. A genetic screening procedure was designed to isolate MTS mutants able to aminoacylate a methionine amber tRNA (CUA anticodon). Selected suppressor MTS enzymes all possess one or several mutations in the vicinity of Trp-461, a residue that is the major contributor to the stability of complexes formed with tRNAs having the cognate CAu anticodon. Analysis of catalytic properties of purified suppressor enzymes shows that they have acquired an additional specificity toward the amber anticodon without complete disruption of the methionine anticodon site. It is concluded that both positive and negative discrimination toward the binding of tRNA anticodon sequences is restricted to a limited region of the synthetase, residues 451-467.

引用

页码：291 / 295

页数：5

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