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The role of the catalytic domain of E. coli GluRS in tRNA discrimination |
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| Authors: | Saumya Dasgupta Chiranjeeb Dey Siddhartha Roy |
| Affiliation: | a Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VIIM, Kolkata 700 054, India b Indian Institute of Chemical Biology (CSIR), 4, Raja S.C. Mullick Road, Kolkata 700 032, India c Dr. B.C. Guha Centre for Genetic Engineering and Biotechnology, University of Calcutta, 35 Ballygunge Circular Road, Kolkata 700 019, India |
| 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. |
| Keywords: | GluRS, glutamyl-tRNA synthetase GlnRS, glutaminyl-tRNA synthetase NGluRS, N-terminal catalytic domain of GluRS CGluRS, C-terminal anticodon-binding domain of GluRS cGluGlnRS, chimera of NGluRS and the anticodon-binding domain of GlnRS ASA, solvent accessible surface area aaRS, aminoacyl-tRNA synthetase D-GluRS, discriminatory GluRS ND-GluRS, non-discriminatory GluRS |
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