The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination
- PMID: 19481543
- DOI: 10.1016/j.febslet.2009.05.041
The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination
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.
Similar articles
-
A chimaeric glutamyl:glutaminyl-tRNA synthetase: implications for evolution.Biochem J. 2009 Jan 15;417(2):449-55. doi: 10.1042/BJ20080747. Biochem J. 2009. PMID: 18817520
-
Growth inhibition of Escherichia coli during heterologous expression of Bacillus subtilis glutamyl-tRNA synthetase that catalyzes the formation of mischarged glutamyl-tRNA1 Gln.J Microbiol. 2004 Jun;42(2):111-6. J Microbiol. 2004. PMID: 15357304
-
Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase.Nat Struct Biol. 2001 Mar;8(3):203-6. doi: 10.1038/84927. Nat Struct Biol. 2001. PMID: 11224561
-
Glutamyl-tRNA sythetase.Biol Chem. 1997 Nov;378(11):1313-29. Biol Chem. 1997. PMID: 9426192 Review.
-
Substrate selection by aminoacyl-tRNA synthetases.Nucleic Acids Symp Ser. 1995;(33):40-2. Nucleic Acids Symp Ser. 1995. PMID: 8643392 Review.
Cited by
-
Fusion with anticodon binding domain of GluRS is not sufficient to alter the substrate specificity of a chimeric Glu-Q-RS.Protein J. 2014 Feb;33(1):48-60. doi: 10.1007/s10930-013-9537-7. Protein J. 2014. PMID: 24374508
-
Critical role of zinc ion on E. coli glutamyl-queuosine-tRNA(Asp) synthetase (Glu-Q-RS) structure and function.Protein J. 2014 Apr;33(2):143-9. doi: 10.1007/s10930-014-9546-1. Protein J. 2014. PMID: 24505021
-
Evolutionary insights about bacterial GlxRS from whole genome analyses: is GluRS2 a chimera?BMC Evol Biol. 2014 Feb 12;14:26. doi: 10.1186/1471-2148-14-26. BMC Evol Biol. 2014. PMID: 24521160 Free PMC article.
-
Rational design of an evolutionary precursor of glutaminyl-tRNA synthetase.Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20485-90. doi: 10.1073/pnas.1117294108. Epub 2011 Dec 7. Proc Natl Acad Sci U S A. 2011. PMID: 22158897 Free PMC article.
-
Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase.Biosci Rep. 2015 Mar 31;35(2):e00184. doi: 10.1042/BSR20150005. Biosci Rep. 2015. PMID: 25686371 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases