Domains of phenylalanyl-tRNA synthetase from Thermus thermophilus required for aminoacylation

被引：12

作者：

Lechler, A ^{[1
]}

Kreutzer, R ^{[1
]}

机构：

[1] Univ Bayreuth, Biochem Lab, D-95447 Bayreuth, Germany

来源：

FEBS LETTERS | 1997年 / 420卷 / 2-3期

关键词：

phenylalanyl-tRNA synthetase; Thermus thermophilus; aminoacylation; tRNA(Phe); protein-RNA interaction;

D O I：

10.1016/S0014-5793(97)01504-4

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：

The contribution of entire domains or particular amino acid residues of the phenylalanyl-tRNA synthetase (FRS) from Thermus thermophilus to the interaction with tRNA(Phe) was studied, Removal of domain 8 of the beta subunit resulted in drastic reduction of the dissociation constant of the FRS.tRNA(Phe) complex. Neither the removal of arginine 2 of the beta subunit, ,which makes the only major contact between domains beta 1-5 and the tRNA, nor the replacement of the conserved proline 473 by glycine had an influence on the aminoacylation activity of the FRS. Thus, the body comprising domains 1-5 of the beta subunit may not be essential for efficient aminoacylation of tRNA(Phe) by the FRS and rather be involved in other functions. (C) 1997 Federation of European Biochemical Societies.

引用

页码：139 / 142

页数：4

共 25 条

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