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J. Biol. Chem., Vol. 279, Issue 35, 37142-37152, August 27, 2004

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N²-Methylation of Guanosine at Position 10 in tRNA Is Catalyzed by a THUMP Domain-containing, S-Adenosylmethionine-dependent Methyltransferase, Conserved in Archaea and Eukaryota^*

Jean Armengaud, Jaunius Urbonaviius¶||, Bernard Fernandez, Guylaine Chaussinand, Janusz M. Bujnicki**, and Henri Grosjean¶

From the Commissariat à l'Energie Atomique VALRHO, DSV-DIEP-SBTN, Service de Biochimie Post-génomique & Toxicologie Nucléaire, F-30207 Bagnols-sur-Cèze, France, ^¶Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Bld. 34, 1 Avenue de la Terrasse, F-91198 Gif-sur-Yvette, France, and ^**International Institute of Molecular and Cell Biology, Trojdena 4, Warsaw 02-109, Poland

In sequenced genomes, genes belonging to the cluster of orthologous group COG1041 are exclusively, and almost ubiquitously, found in Eukaryota and Archaea but never in Bacteria. The corresponding gene products exhibit a characteristic Rossmann fold, S-adenosylmethionine-dependent methyltransferase domain in the C terminus and a predicted RNA-binding THUMP (thiouridine synthases, RNA methyltransferases, and pseudouridine synthases) domain in the N terminus. Recombinant PAB1283 protein from the archaeon Pyrococcus abyssi GE5, a member of COG1041, was purified and shown to behave as a monomeric 39-kDa entity. This protein (EC 2.1.1.32), now renamed _PabTrm-G10, which is extremely thermostable, forms a 1:1 complex with tRNA and catalyzes the adenosylmethionine-dependent methylation of the exocyclic amino group (N²) of guanosine located at position 10. Depending on the experimental conditions used, as well as the tRNA substrate tested, the enzymatic reaction leads to the formation of either N²-monomethyl (m²G) or N²-dimethylguanosine (m²₂G). Interestingly, _PabTrm-G10 exhibits different domain organization and different catalytic site architecture from another, earlier characterized, tRNA-dimethyltransferase from Pyrococcus furiosus (_PfuTrm-G26, also known as _PfuTrm1, a member of COG1867) that catalyzes an identical two-step dimethylation of guanosine but at position 26 in tRNAs and is also conserved among all sequenced Eukaryota and Archaea. The co-occurrence of these two guanosine dimethyltransferases in both Archaea and Eukaryota but not in Bacteria is a hallmark of distinct tRNAs maturation strategies between these domains of life.

Received for publication, April 7, 2004 , and in revised form, May 28, 2004.

^* This work was supported in part by a grant from the Centre National de la Recherche Scientifique (Geomex program, 2002-2004) (to H. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains two additional figures.

^|| Supported by a postdoctoral FEBS fellowship.

Supported by the EMBO/HHMI Young Investigator Program and by a fellowship from the Foundation for Polish Science.

To whom correspondence should be addressed. Tel.: 33-4-66-79-68-02; Fax: 33-4-66-79-19-05; E-mail: armengaud{at}cea.fr.

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