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Molecular and Cellular Biology, June 2005, p. 4359-4370, Vol. 25, No. 11
0270-7306/05/$08.00+0 doi:10.1128/MCB.25.11.4359-4370.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Centre de Recherche de Biochimie Macromoléculaire du CNRS, 34293 Montpellier, France,1 International Institute of Molecular and Cell Biology, Warsaw, Poland,2 Laboratoire d'Enzymologie et Biochimie Structurales, Gif sur Yvette, France3
Received 18 November 2004/ Returned for modification 14 December 2004/ Accepted 1 March 2005
N2-Monomethylguanosine-10 (m2G10) and N2,N2-dimethylguanosine-26 (m22G26) are the only two guanosine modifications that have been detected in tRNA from nearly all archaea and eukaryotes but not in bacteria. In Saccharomyces cerevisiae, formation of m22G26 is catalyzed by Trm1p, and we report here the identification of the enzymatic activity that catalyzes the formation of m2G10 in yeast tRNA. It is composed of at least two subunits that are associated in vivo: Trm11p (Yol124c), which is the catalytic subunit, and Trm112p (Ynr046w), a putative zinc-binding protein. While deletion of TRM11 has no detectable phenotype under laboratory conditions, deletion of TRM112 leads to a severe growth defect, suggesting that it has additional functions in the cell. Indeed, Trm112p is associated with at least four proteins: two tRNA methyltransferases (Trm9p and Trm11p), one putative protein methyltransferase (Mtc6p/Ydr140w), and one protein with a Rossmann fold dehydrogenase domain (Lys9p/Ynr050c). In addition, TRM11 interacts genetically with TRM1, thus suggesting that the absence of m2G10 and m22G26 affects tRNA metabolism or functioning.
Supplemental material for this article may be found at http://mcb.asm.org/.
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