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Nucleic Acids Research, 2003, Vol. 31, No. 8 2148-2156
© 2003 Oxford University Press

Cloning and characterization of tRNA (m1A58) methyltransferase (TrmI) from Thermus thermophilus HB27, a protein required for cell growth at extreme temperatures

Louis Droogmans1, Martine Roovers1, Janusz M. Bujnicki2, Catherine Tricot3, Thomas Hartsch4, Victor Stalon1,3 and Henri Grosjean5

1 Laboratoire de Microbiologie, Université Libre de Bruxelles, Institut de Recherches Microbiologiques Jean-Marie Wiame, Avenue E. Gryson 1, B-1070 Bruxelles, Belgium, 2 Bioinformatics Laboratory, International Institute of Molecular and Cell Biology, ul. ks. Trojdena 4, 02-109 Warsaw, Poland, 3 Institut de Recherches Microbiologiques Jean-Marie Wiame, Avenue E. Gryson 1, B-1070 Bruxelles, Belgium, 4 Göttingen Genomics Laboratory, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Griesebachstrasse 8, D-37077 Göttingen, Germany and 5 Laboratoire d’Enzymologie et Biochimie Structurales, CNRS, Bld 34, Avenue de la Terrasse 1, F-91198 Gif-sur-Yvette, France

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors

N1-methyladenosine (m1A) is found at position 58 in the T-loop of many tRNAs. In yeast, the formation of this modified nucleoside is catalyzed by the essential tRNA (m1A58) methyltransferase, a tetrameric enzyme that is composed of two types of subunits (Gcd14p and Gcd10p). In this report we describe the cloning, expression and characterization of a Gcd14p homolog from the hyperthermophilic bacterium Thermus thermophilus. The purified recombinant enzyme behaves as a homotetramer of ~150 kDa by gel filtration and catalyzes the site- specific formation of m1A at position 58 of the T-loop of tRNA in the absence of any other complementary protein. S-adenosylmethionine is used as donor of the methyl group. Thus, we propose to name the bacterial enzyme TrmI and accordingly its structural gene trmI. These results provide a key evolutionary link between the functionally characterized two-component eukaryotic enzyme and the recently described crystal structure of an uncharacterized, putative homotetrameric methyltransferase Rv2118c from Mycobacterium tuberculosis. Interest ingly, inactivation of the T.thermophilus trmI gene results in a thermosensitive phenotype (growth defect at 80°C), which suggests a role of the N1-methylation of tRNA adenosine-58 in adaptation of life to extreme temperatures.


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