Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase

Shun Ichi Sekine, Osamu Nureki, Atsushi Shimada, Dmitry G. Vassylyev, Shigeyuki Yokoyama

Research output: Contribution to journalArticle

91 Citations (Scopus)

Abstract

Glutamyl-tRNA synthetases (GluRSs) are divided into two distinct types, with regard to the presence or absence of glutaminyl-tRNA synthetase (GlnRS) in the genetic translation systems. In the original 19-synthetase systems lacking GlnRS, the 'non-discriminating' GluRS glutamylates both tRNAGlu and tRNAGln. In contrast, in the evolved 20-synthetase systems with GlnRS, the 'discriminating' GluRS aminoacylates only tRNAGlu. Here we report the 2.4 Å resolution crystal structure of a 'discriminating' GluRS · tRNAGlu complex from Thermus thermophilus. The GluRS recognizes the tRNAGlu anticodon bases via two α-helical domains, maintaining the base stacking. We show that the discrimination between the Glu and Gln anticodons (34YUC36 and 34YUG36, respectively) is achieved by a single aginine residue (Arg 358). The mutation of Arg 358 to Gln resulted in a GluRS that does not discriminate between the Glu and Gln anticodons. Tiffs change mimics the reverse course of GluRS evolution from anticodon 'non-discriminating' to 'discriminating'.

Original languageEnglish
Pages (from-to)203-206
Number of pages4
JournalNature Structural Biology
Volume8
Issue number3
DOIs
Publication statusPublished - Mar 10 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

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