The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination

Dasgupta, Saumya ; Saha, Rajesh ; Dey, Chiranjeeb ; Banerjee, Rajat ; Roy, Siddhartha ; Basu, Gautam (2009) The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination FEBS Letters, 583 (12). pp. 2114-2120. ISSN 0014-5793

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.febslet.2009.05.041

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.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Glutamyl-tRNA Synthetase; tRNAGln; tRNA-discrimination; Glutamylation; Escherichia coli
ID Code:43165
Deposited On:10 Jun 2011 07:07
Last Modified:10 Jun 2011 07:08

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