Journal
NUCLEIC ACIDS RESEARCH
Volume 39, Issue 14, Pages 6249-6259Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkr176
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Funding
- Agence Nationale pour la Recherche [ANR-06-BLAN-0075-02, ANR-07-JCJC-0105]
- Centre National pour la Recherche Scientifique
- Human Frontier Science Program organism [RGP0018/2009-C]
- EU [LSHG-CT-2005-512028]
- Universite Paris-Sud 11
- Agence Nationale de la Recherche (ANR) [ANR-06-BLAN-0075, ANR-07-JCJC-0105] Funding Source: Agence Nationale de la Recherche (ANR)
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Methylation is a common modification encountered in DNA, RNA and proteins. It plays a central role in gene expression, protein function and mRNA translation. Prokaryotic and eukaryotic class I translation termination factors are methylated on the glutamine of the essential and universally conserved GGQ motif, in line with an important cellular role. In eukaryotes, this modification is performed by the Mtq2-Trm112 holoenzyme. Trm112 activates not only the Mtq2 catalytic subunit but also two other tRNA methyltransferases (Trm9 and Trm11). To understand the molecular mechanisms underlying methyltransferase activation by Trm112, we have determined the 3D structure of the Mtq2-Trm112 complex and mapped its active site. Using site-directed mutagenesis and in vivo functional experiments, we show that this structure can also serve as a model for the Trm9-Trm112 complex, supporting our hypothesis that Trm112 uses a common strategy to activate these three methyltransferases.
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