IDENTIFICATION OF POTENTIAL AMINO-ACID-RESIDUES SUPPORTING ANTICODON RECOGNITION IN YEAST METHIONYL-TRANSFER RNA-SYNTHETASE

被引：10

作者：

DESPONS, L ^{[1
]}

WALTER, P ^{[1
]}

SENGER, B ^{[1
]}

EBEL, JP ^{[1
]}

FASIOLO, F ^{[1
]}

机构：

[1] CNRS,INST BIOL MOLEC & CELLULAIRE,15 RUE RENE DESCARTES,F-67084 STRASBOURG,FRANCE

来源：

FEBS LETTERS | 1991年 / 289卷 / 02期

关键词：

METHIONYL-TRANSFER RNA SYNTHETASE; SITE-DIRECTED MUTAGENESIS; ANTICODON BINDING REGION;

D O I：

10.1016/0014-5793(91)81073-H

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：

Sequence comparisons among methionyl-tRNA synthetases from different organisms reveal only one block of homology beyond the last beta-strand of the mononucleotide fold. We have introduced a series of semi-conservative amino acid replacements in the conserved motif of yeast methionyl-tRNA synthetase. The results indicate that replacements of two polar residues (Asn584 and Arg588) affected specifically the aminoacylation reaction. The location of these residues in the tertiary structure of the enzyme is compatible with a direct interaction of the amino acid side-chains with the tRNA anticodon.

引用

页码：217 / 220

页数：4

共 14 条

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