title: Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus.
abstract: Post-transcriptional and post-translational modifications are very important for the control and optimal efficiency of messenger RNA (mRNA) translation. Among these, methylation is the most widespread modification, as it is found in all domains of life. These methyl groups can be grafted either on nucleic acids (transfer RNA (tRNA), ribosomal RNA (rRNA), mRNA, etc.) or on protein translation factors. This review focuses on Trm112, a small protein interacting with and activating at least four different eukaryotic methyltransferase (MTase) enzymes modifying factors involved in translation. The Trm112-Trm9 and Trm112-Trm11 complexes modify tRNAs, while the Trm112-Mtq2 complex targets translation termination factor eRF1, which is a tRNA mimic. The last complex formed between Trm112 and Bud23 proteins modifies 18S rRNA and participates in the 40S biogenesis pathway. In this review, we present the functions of these eukaryotic Trm112-MTase complexes, the molecular bases responsible for complex formation and substrate recognition, as well as their implications in human diseases. Moreover, as Trm112 orthologs are found in bacterial and archaeal genomes, the conservation of this Trm112 network beyond eukaryotic organisms is also discussed.
authors.affiliation: Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, 91128 Palaiseau CEDEX, France. gabrielle.bourgeois@polytechnique.edu.
authors.forename: Gabrielle
authors.initials: G
authors.lastname: Bourgeois
authors.affiliation: Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, 91128 Palaiseau CEDEX, France. juliette.letoquart@uclouvain.be.|De Duve Institute, Université Catholique de Louvain, avenue Hippocrate 75, 1200 Brussels, Belgium. juliette.letoquart@uclouvain.be.
authors.forename: Juliette
authors.initials: J
authors.lastname: Létoquart
authors.affiliation: Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, 91128 Palaiseau CEDEX, France. nhan.tran-van@polytechnique.edu.
authors.forename: Nhan
authors.initials: N
authors.lastname: van Tran
authors.affiliation: Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, 91128 Palaiseau CEDEX, France. marc.graille@polytechnique.edu.
authors.forename: Marc
authors.initials: M
authors.lastname: Graille
mesh_terms: D000595:Amino Acid Sequence; D005057:Eukaryotic Cells / Q000201:enzymology*; D008780:Methyltransferases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011387:Prokaryotic Cells / Q000201:enzymology; D014176:Protein Biosynthesis
chemical_list: D008780:Methyltransferases
keywords: RNA modifying enzyme; S-adenosyl-l-methionine; methyltransferase; post-transcriptional modification; translation