ArticleNucleic acids research2011
Mechanism of activation of methyltransferases involved in translation by the Trm112 'hub' protein.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 48 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
48 citing papers in PubMed, 77 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
- 2'-O-methylation-dependent installation of NNature communications · 2026Article
- Integrating natural language processing and genome analysis enables accurate bacterial phenotype prediction.NAR genomics and bioinformatics · 2025Article
- Refinement and curation of homologous groups facilitated by structure prediction.Protein science : a publication of the Protein Society · 2025Article
- The Greatwall-Endosulfine-PP2A/B55 pathway regulates entry into quiescence by enhancing translation of Elongator-tunable transcripts.Nature communications · 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
- The emerging importance of METTL5-mediated ribosomal RNA methylation.Experimental & molecular medicine · 2022Review
- Mammalian HEMK1 methylates glutamine residue of the GGQ motif of mitochondrial release factors.Scientific reports · 2022Article
- WBSCR22 and TRMT112 synergistically suppress cell proliferation, invasion and tumorigenesis in pancreatic cancer via transcriptional regulation of ISG15.International journal of oncology · 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
- The ribosome epitranscriptome: inert-or a platform for functional plasticity?RNA (New York, N.Y.) · 2021Review
- A comprehensive review of m6A/m6Am RNA methyltransferase structures.Nucleic acids research · 2021Review
- The catalytic activity of the translation termination factor methyltransferase Mtq2-Trm112 complex is required for large ribosomal subunit biogenesis.Nucleic acids research · 2020Article
- Structural and functional insights into Archaeoglobus fulgidus m2G10 tRNA methyltransferase Trm11 and its Trm112 activator.Nucleic acids research · 2020Article
- Identification of the 3-amino-3-carboxypropyl (acp) transferase enzyme responsible for acp3U formation at position 47 in Escherichia coli tRNAs.Nucleic acids research · 2020Article
- The human 18S rRNA m6A methyltransferase METTL5 is stabilized by TRMT112.Nucleic acids research · 2019Article
- The Common Partner of Several Methyltransferases TRMT112 Regulates the Expression of N6AMT1 Isoforms in Mammalian Cells.Biomolecules · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methylation is a common modification encountered in DNA, RNA and proteins. It plays a central role in gene expression, protein function and mRNA translation. Prokaryotic and eukaryotic class I translation termination factors are methylated on the glutamine of the essential and universally conserved GGQ motif, in line with an important cellular role. In eukaryotes, this modification is performed by the Mtq2-Trm112 holoenzyme. Trm112 activates not only the Mtq2 catalytic subunit but also two other tRNA methyltransferases (Trm9 and Trm11). To understand the molecular mechanisms underlying methyltransferase activation by Trm112, we have determined the 3D structure of the Mtq2-Trm112 complex and mapped its active site. Using site-directed mutagenesis and in vivo functional experiments, we show that this structure can also serve as a model for the Trm9-Trm112 complex, supporting our hypothesis that Trm112 uses a common strategy to activate these three methyltransferases.
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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.