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J. Biol. Chem., Vol. 282, Issue 26, 18711-18721, June 29, 2007

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Archease from Pyrococcus abyssi Improves Substrate Specificity and Solubility of a tRNA m⁵C Methyltransferase^*

Sylvie Auxilien¹, Fatima El Khadali², Anette Rasmussen, Stephen Douthwaite³, and Henri Grosjean³⁴

From the Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France and the Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark

Members of the archease superfamily of proteins are represented in all three domains of life. Archease genes are generally located adjacent to genes encoding proteins involved in DNA or RNA processing. Archease have therefore been predicted to play a modulator or chaperone role in selected steps of DNA or RNA metabolism, although the roles of archeases remain to be established experimentally. Here we report the function of one of these archeases from the hyperthermophile Pyrococcus abyssi. The corresponding gene (PAB1946) is located in a bicistronic operon immediately upstream from a second open reading frame (PAB1947), which is shown here to encode a tRNA m⁵C methyltransferase. In vitro, the purified recombinant methyltransferase catalyzes m⁵C formation at several cytosines within tRNAs with preference for C49. The specificity of the methyltransferase is increased by the archease. In solution, the archease exists as a monomer, trimer, and hexamer. Only the oligomeric states bind the methyltransferase and prevent its aggregation, in addition to hindering dimerization of the methyltransferase-tRNA complex. This P. abyssi system possibly reflects the general function of archeases in preventing protein aggregation and modulating the function of their accompanying proteins.

Received for publication, August 4, 2006 , and in revised form, April 27, 2007.

^* This work was supported by grants from CNRS (Programme Interdépartemental de Géomicrobiologie des Environnements Extrêmes GEOMEX) (to H. G.) and Grant FNU-Rammebevilling 21-04-0520 from the Danish Research Agency, and the Nucleic Acid Center (to S. D.). 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 supplemental Figs. S1 and S2 and two references.

² Present address: Structural Motility, Institut Curie, CNRS, 26 Rue d'Ulm, 75248 Paris, France.

³ Both authors contributed equally to this work.

⁴ Present address: Institut de Génétique et Microbiologie, Université Paris-Sud, CNRS, 91405 Orsay, France.

¹ To whom correspondence should be addressed: LEBS, CNRS, Bât. 34, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France. Tel.: 33-1-69-82-34-98; Fax: 33-1-69-82-31-29; E-mail: Sylvie.Auxilien{at}lebs.cnrs-gif.fr.

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