Literature DB >> 19481543

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

Saumya Dasgupta1, Rajesh Saha, Chiranjeeb Dey, Rajat Banerjee, Siddhartha Roy, Gautam Basu.   

Abstract

Discrimination of tRNA(Gln) is an integral function of several bacterial glutamyl-tRNA synthetases (GluRS). The origin of the discrimination is thought to arise from unfavorable interactions between tRNA(Gln) 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 tRNA(Gln). Our results demonstrate that in addition to the anticodon-binding domain, tRNA(Gln) discriminatory elements may be present in the catalytic domain in E. coli GluRS as well.

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Year:  2009        PMID: 19481543     DOI: 10.1016/j.febslet.2009.05.041

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  6 in total

1.  Critical role of zinc ion on E. coli glutamyl-queuosine-tRNA(Asp) synthetase (Glu-Q-RS) structure and function.

Authors:  Sutapa Ray; Victor Banerjee; Mickael Blaise; Baisakhi Banerjee; Kali Pada Das; Daniel Kern; Rajat Banerjee
Journal:  Protein J       Date:  2014-04       Impact factor: 2.371

2.  Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase.

Authors:  Patrick O'Donoghue; Kelly Sheppard; Osamu Nureki; Dieter Söll
Journal:  Proc Natl Acad Sci U S A       Date:  2011-12-07       Impact factor: 11.205

3.  Preliminary X-ray crystallographic analysis of an engineered glutamyl-tRNA synthetase from Escherichia coli.

Authors:  Nipa Chongdar; Saumya Dasgupta; Ajit Bikram Datta; Gautam Basu
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2014-06-18       Impact factor: 1.056

4.  Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS.

Authors:  Sutapa Ray; Mickael Blaise; Bappaditya Roy; Saptaparni Ghosh; Daniel Kern; Rajat Banerjee
Journal:  Protein J       Date:  2014-02       Impact factor: 2.371

5.  Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase.

Authors:  Nipa Chongdar; Saumya Dasgupta; Ajit Bikram Datta; Gautam Basu
Journal:  Biosci Rep       Date:  2015-03-31       Impact factor: 3.840

6.  Evolutionary insights about bacterial GlxRS from whole genome analyses: is GluRS2 a chimera?

Authors:  Saumya Dasgupta; Gautam Basu
Journal:  BMC Evol Biol       Date:  2014-02-12       Impact factor: 3.260

  6 in total

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