ReviewBiomolecules2017
Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus.
Review in Biomolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 66 citations in OpenAlex.
- Guanosine 10 methylation by TRMT11-TRMT112 optimizes human mitochondrial tRNAs for efficient translation.Nucleic acids research · 2026Article
- TRMT112 drives a tumor growth and metastasis-promoting program in triple-negative breast cancer.Cell death and differentiation · 2026Article
- HemK class methyltransferase, a protein translation regulator: role in growth, development and phenotypic diversity.Molecular biology reports · 2025Review
- The Greatwall-Endosulfine-PP2A/B55 pathway regulates entry into quiescence by enhancing translation of Elongator-tunable transcripts.Nature communications · 2024Article
- THUMPD2 catalyzes the N2-methylation of U6 snRNA of the spliceosome catalytic center and regulates pre-mRNA splicing and retinal degeneration.Nucleic acids research · 2024Article
- Rapamycin-sensitive mechanisms confine the growth of fission yeast below the temperatures detrimental to cell physiology.iScience · 2024Article
- Fecal microbiota transplantation from female donors restores gut permeability and reduces liver injury and inflammation in middle-aged male mice exposed to alcohol.Frontiers in nutrition · 2024Article
- The Greatwall-Endosulfine-PP2A/B55 pathway controls entry into quiescence by promoting translation of Elongator-tuneable transcripts.Research square · 2023Article
- N 2-methylguanosine modifications on human tRNAs and snRNA U6 are important for cell proliferation, protein translation and pre-mRNA splicing.Nucleic acids research · 2023Article
- Coordination of RNA modifications in the brain and beyond.Molecular psychiatry · 2023Review
- Review
- Overexpression of 18S rRNA methyltransferase CrBUD23 enhances biomass and lutein content inFrontiers in bioengineering and biotechnology · 2023Article
- The inhibitory effect of KIAA1456 on the proliferation and metastasis of epithelial ovarian cancer through SSX1 and AKT signaling pathway.Journal of Cancer · 2023Article
- Dysfunctional tRNA reprogramming and codon-biased translation in cancer.Trends in molecular medicine · 2022Review
- Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-International journal of molecular sciences · 2022Article
- Pan-Cancer Analysis Reveals the Relation between TRMT112 and Tumor Microenvironment.Journal of oncology · 2022Article
- Human TRMT112-Methyltransferase Network Consists of Seven Partners Interacting with a Common Co-Factor.International journal of molecular sciences · 2021Article
- THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of tRNA substrates.Nucleic acids research · 2021Article
- The Importance of the Epi-Transcriptome in Translation Fidelity.Non-coding RNA · 2021Review
- A comprehensive review of m6A/m6Am RNA methyltransferase structures.Nucleic acids research · 2021Review
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.