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.
Highlights
Gene expression is a finely-tuned process allowing a cell to adapt rapidly throughout the cell cycle or upon exposure to environmental cues
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
It is well known that DNA modifications and post-translational modifications of histone proteins participate in the epigenetic control of gene expression [1]
Summary
Gene expression is a finely-tuned process allowing a cell to adapt rapidly throughout the cell cycle or upon exposure to environmental cues. The activity of factors involved in translation is enhanced or regulated by post-transcriptional or post-translational modifications with methylation being the most prominent one in protein translation. This is the case for transfer RNAs (tRNA), which are heavily modified so as to improve their stability, as well as the efficiency and accuracy of translation [2]. We present the current knowledge on the Trm112 eukaryotic protein, which acts as an activating platform of four S-adenosyl-L-methionine (SAM)-dependent methyltransferases (MTases) modifying rRNA (Bud23), tRNAs (Trm and Trm11) or the eRF1 class I translation termination factor (Mtq2), perfectly illustrating the importance of methylation in protein synthesis.
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