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REVIEW article
Front. RNA Res.
Sec. RNA Processing and Regulation
Volume 3 - 2025 | doi: 10.3389/frnar.2025.1556979
This article is part of the Research Topic RNA Methylation: Detection, Deposition, and Functions View all 5 articles
TRMT112, a master activator of several methyltransferases modifying factors involved in RNA maturation and translation
Provisionally accepted- Laboratory of Structural Cell Biology (BIOC), Institut Polytechnique de Paris (IP Paris), Palaiseau, France
Most RNAs and many protein factors involved in mRNA maturation and translation are decorated by numerous and diverse chemical modifications, which contribute to the efficiency, fidelity and regulation of these complexes and to essential cellular processes. Among those modifications, methylation catalyzed mainly by S-adenosyl-L-methionine (SAM) dependent methyltransferases (MTases) is the most common one. TRMT112 is a small protein acting as an allosteric regulator of several MTases. Initial studies focusing on TRMT112 and its associated MTases were performed in Saccharomyces cerevisiae whereas only few were expanded to human cells, leading to the identification and characterization of four TRMT112 partners in yeast (Trm11, Bud23, Mtq2 and Trm9) and five in human cells (TRMT11, BUD23, MTQ2/HemK2 and two Trm9 orthologues ALKBH8 and TRMT9B). Recent studies have identified several novel MTase partners of human TRMT112, namely METTL5, THUMPD2 and THUMPD3. Interestingly, all these TRMT112-MTase complexes modify factors (RNAs and proteins) involved in mRNA maturation and translation processes and growing evidence supports the importance of these MTases in cancer and correct brain development. In this review, we summarize the current knowledge on TRMT112 protein and its various MTase partners in eukaryotes and archaea.
Keywords: Epitranscriptomics, Heterodimeric methyltransferase, pre-mRNA splicing, mRNA translation, post-transcriptional, translational modifications
Received: 07 Jan 2025; Accepted: 26 Feb 2025.
Copyright: © 2025 Wang, Tay, Hu, Corre and GRAILLE. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence:
Marc GRAILLE, Laboratory of Structural Cell Biology (BIOC), Institut Polytechnique de Paris (IP Paris), Palaiseau, France
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