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Published online 22 January 2004

Nucleic Acids Research, 2004, Vol. 32, No. 2 465-476
© 2004 Oxford University Press

A primordial RNA modification enzyme: the case of tRNA (m1A) methyltransferase

Martine Roovers1, Johan Wouters2, Janusz M. Bujnicki3, Catherine Tricot2, Victor Stalon1,2, Henri Grosjean4 and Louis Droogmans*,1,5

1 Laboratoire de Microbiologie, Université Libre de Bruxelles, 2 Institut de Recherches Microbiologiques Jean-Marie Wiame, Avenue E. Gryson 1, B-1070 Bruxelles, Belgium, 3 Bioinformatics Laboratory, International Institute of Molecular and Cell Biology, ul. ks. Trojdena 4, 02-109 Warsaw, Poland, 4 Laboratoire d‘Enzymologie et Biochimie Structurales, CNRS, Avenue de la Terrasse 1, F-91198 Gif-sur-Yvette, France and 5 Laboratoire de Génétique des Procaryotes, Université Libre de Bruxelles, Institut de Biologies Moléculaire et Médicale, rue des Professeurs Jeener et Brachet 12, B-6041 Gosselies, Belgium

*To whom correspondence should be addressed at Laboratoire de Microbiologie, Université Libre de Bruxelles, Institut de Recherches Microbiologiques Jean-Marie Wiame, Avenue E. Gryson 1, B-1070 Bruxelles, Belgium. Tel: +32 2 526 7254; Fax: +32 2 526 7273; Email: ldroogma{at}ulb.ac.be
The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors

The modified nucleoside 1-methyladenosine (m1A) is found in the T-loop of many tRNAs from organisms belonging to the three domains of life (Eukaryota, Bacteria, Archaea). In the T-loop of eukaryotic and bacterial tRNAs, m1A is present at position 58, whereas in archaeal tRNAs it is present at position(s) 58 and/or 57, m1A57 being the obligatory intermediate in the biosynthesis of 1-methylinosine (m1I57). In yeast, the formation of m1A58 is catalysed by the essential tRNA (m1A58) methyltransferase (MTase), a tetrameric enzyme that is composed of two types of subunits (Gcd14p and Gcd10p), whereas in the bacterium Thermus thermophilus the enzyme is a homotetramer of the TrmI polypeptide. Here, we report that the TrmI enzyme from the archaeon Pyrococcus abyssi is also a homotetramer. However, unlike the bacterial site-specific TrmI MTase, the P.abyssi enzyme is region-specific and catalyses the formation of m1A at two adjacent positions (57 and 58) in the T-loop of certain tRNAs. The stabilisation of P.abyssi TrmI at extreme temperatures involves intersubunit disulphide bridges that reinforce the tetrameric oligomerisation, as revealed by biochemical and crystallographic evidences. The origin and evolution of m1A MTases is discussed in the context of different hypotheses of the tree of life.


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