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MBE Advance Access originally published online on November 26, 2008
Molecular Biology and Evolution 2009 26(2):445-450; doi:10.1093/molbev/msn267
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© The Author 2008. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Research Articles

No Rosetta Stone for a Sense–Antisense Origin of Aminoacyl tRNA Synthetase Classes

Tom A. Williams, Kenneth H. Wolfe and Mario A. Fares

Department of Genetics, Smurfit Institute of Genetics, University of Dublin, Trinity College, Dublin, Ireland

E-mail: faresm{at}tcd.ie.

Accepted for publication November 15, 2008.

Aminoacyl tRNA synthetases (aaRS) are crucial enzymes that join amino acids to their cognate tRNAs, thereby implementing the genetic code. These enzymes fall into two unrelated structural classes whose evolution has not been explained. The leading hypothesis, proposed by Rodin and Ohno, is that the two classes originated as a pair of sense–antisense genes encoded on opposite strands of a single DNA molecule. This unusual idea obtained its main support from reports of a "Rosetta stone": a locus where genes for heat shock protein 70 (HSP70) and an Nicotinamide adenine dinulecotide-specific glutamate dehydrogenase (NAD-GDH), which are structurally homologous to the two classes of aaRS, overlap extensively on complementary DNA strands. This remarkable locus was first characterized in the oomycete Achlya klebsiana and has since been reported in many other species. Here we present evidence that the open reading frames on the antisense strand of HSP70 genes are spurious, and we identify a more probable candidate for the gene encoding the oomycete NAD-GDH enzyme. These results cast extensive doubt on the Rosetta Stone argument.

Key Words: Rosetta Stone • Aminoacyl tRNA Synthetase • Hsp70

Michele Vendruscolo, Associate Editor


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