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The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination
S DASGUPTA, R SAHA, C DEY, , S ROY, G BASU
Published in -
2009
Volume: 583
   
Issue: 12
Pages: 2114 - 2120
Abstract
Discrimination of tRNAGln is an integral function of several bacterial glutamyl-tRNA synthetases (GluRS). The origin of the discrimination is thought to arise from unfavorable interactions between tRNAGln and the anticodon-binding domain of GluRS. From experiments on an anticodon-binding domain truncated Escherichia coli (E. coli) GluRS (catalytic domain) and a chimeric protein, constructed from the catalytic domain of E. coli GluRS and the anticodon-binding domain of E. coli glutaminyl-tRNA synthetase (GlnRS), we show that both proteins discriminate against E. coli tRNAGln. Our results demonstrate that in addition to the anticodon-binding domain, tRNAGln discriminatory elements may be present in the catalytic domain in E. coli GluRS as well. © 2009 Federation of European Biochemical Societies.
About the journal
JournalFEBS Letters
Publisher-
ISSN0014-5793