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Nucleic Acids Research Advance Access originally published online on September 15, 2009
Nucleic Acids Research 2009 37(20):6942-6949; doi:10.1093/nar/gkp754
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Nucleic Acids Research, 2009, Vol. 37, No. 20 6942-6949
© The Author(s) 2009. Published by Oxford University Press.
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Recognition of tRNAGln by Helicobacter pylori GluRS2—a tRNAGln-specific glutamyl-tRNA synthetase

Keng-Ming Chang1,2 and Tamara L. Hendrickson1,*

1Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, MI 48202 and 2Department of Chemistry, Johns Hopkins University, 3400 North Charles St, Baltimore, MD 21218, USA

*To whom correspondence should be addressed. Tel: +1 313 577 6914; Fax: +1 313 577 8822; Email: tamara.hendrickson{at}chem.wayne.edu

Received July 6, 2009. Revised August 27, 2009. Accepted August 27, 2009.

Accurate aminoacylation of tRNAs by the aminoacyl-tRNA synthetases (aaRSs) plays a critical role in protein translation. However, some of the aaRSs are missing in many microorganisms. Helicobacter pylori does not have a glutaminyl-tRNA synthetase (GlnRS) but has two divergent glutamyl-tRNA synthetases: GluRS1 and GluRS2. Like a canonical GluRS, GluRS1 aminoacylates tRNAGlu1 and tRNAGlu2. In contrast, GluRS2 only misacylates tRNAGln to form Glu-tRNAGln. It is not clear how GluRS2 achieves specific recognition of tRNAGln while rejecting the two H. pylori tRNAGlu isoacceptors. Here, we show that GluRS2 recognizes major identity elements clustered in the tRNAGln acceptor stem. Mutations in the tRNA anticodon or at the discriminator base had little to no impact on enzyme specificity and activity.


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