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PMID: 21478168 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein.

Nucleic acids research ·Vol. 39 ·No. 14 ·2011-08-00 ·Pages 6249-59

Liger D, Mora L, Lazar N, Figaro S, Henri J, Scrima N, Buckingham RH, van Tilbeurgh H, Heurgué-Hamard V, Graille M

Abstract

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.

MeSH Terms
Catalytic Domain Crystallography Enzyme Activation Fungal Proteins/chemistry Gene Deletion Models, Molecular Mutagenesis, Site-Directed Protein Binding Protein Biosynthesis Protein Methyltransferases/chemistry,genetics Protein Subunits/chemistry,genetics S-Adenosylmethionine/chemistry Saccharomyces cerevisiae Proteins/genetics tRNA Methyltransferases/genetics
Chemicals
Fungal Proteins Protein Subunits Saccharomyces cerevisiae Proteins S-Adenosylmethionine Protein Methyltransferases TRM9 protein, S cerevisiae tRNA Methyltransferases Trm112 protein, S cerevisiae
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Liger Dominique
Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, Université Paris-Sud, IFR115, CNRS UMR 8619, Orsay Cedex F-91405, France.
Mora Liliana
Lazar Noureddine
Figaro Sabine
Henri Julien
Scrima Nathalie
Buckingham Richard H
van Tilbeurgh Herman
Heurgué-Hamard Valérie
Graille Marc
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
1362-4962
Published
2011-08-00
Epub
2011-00-07
Pages
6249-59
Language
English
Region
England
NLM ID
0411011
PMCID
PMC3152332
Subset
IM
Corrections
ErratumIn
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