Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus
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 n...
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| Format: | Article |
| Language: | English |
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MDPI AG
2017-01-01
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| Series: | Biomolecules |
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| Online Access: | http://www.mdpi.com/2218-273X/7/1/7 |
| _version_ | 1818511100017115136 |
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| author | Gabrielle Bourgeois Juliette Létoquart Nhan van Tran Marc Graille |
| author_facet | Gabrielle Bourgeois Juliette Létoquart Nhan van Tran Marc Graille |
| author_sort | Gabrielle Bourgeois |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-10T23:28:54Z |
| format | Article |
| id | doaj.art-6c834670354347f4a4a2217ea5909dca |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-12-10T23:28:54Z |
| publishDate | 2017-01-01 |
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| series | Biomolecules |
| spelling | doaj.art-6c834670354347f4a4a2217ea5909dca2022-12-22T01:29:27ZengMDPI AGBiomolecules2218-273X2017-01-0171710.3390/biom7010007biom7010007Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational ApparatusGabrielle Bourgeois0Juliette Létoquart1Nhan van Tran2Marc Graille3Laboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, 91128 Palaiseau CEDEX, FranceLaboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, 91128 Palaiseau CEDEX, FranceLaboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, 91128 Palaiseau CEDEX, FranceLaboratoire de Biochimie, Ecole polytechnique, CNRS, Université Paris-Saclay, 91128 Palaiseau CEDEX, FrancePost-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.http://www.mdpi.com/2218-273X/7/1/7post-transcriptional modificationRNA modifying enzymemethyltransferaseS-adenosyl-l-methioninetranslation |
| spellingShingle | Gabrielle Bourgeois Juliette Létoquart Nhan van Tran Marc Graille Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus Biomolecules post-transcriptional modification RNA modifying enzyme methyltransferase S-adenosyl-l-methionine translation |
| title | Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus |
| title_full | Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus |
| title_fullStr | Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus |
| title_full_unstemmed | Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus |
| title_short | Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus |
| title_sort | trm112 a protein activator of methyltransferases modifying actors of the eukaryotic translational apparatus |
| topic | post-transcriptional modification RNA modifying enzyme methyltransferase S-adenosyl-l-methionine translation |
| url | http://www.mdpi.com/2218-273X/7/1/7 |
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