ArticleThe Journal of biological chemistry2010
Identification of eukaryotic and prokaryotic methylthiotransferase for biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers, 1 of them a synthesis that pooled it.
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Who cites it
78 citing papers in PubMed, 1 synthesis or guideline pooled it, 136 citations in OpenAlex.
- Genome-wide meta-analysis identifies five new susceptibility loci for cutaneous malignant melanoma.Nature genetics · 2015Pooled it
- tRNA modifications in cancer: from molecular mechanisms to clinical translation.Biomarker research · 2026Review
- Integrated multi-omics reveals coordinatedmSystems · 2026Article
- Disruption of tRNA threonylation triggers RIG-I mediated anti-tumour immune response.Nature communications · 2026Article
- Client recruitment mechanism of the cytosolic Fe-S cluster assembly targeting complex.The EMBO journal · 2026Article
- Eperisone Analogs, Rescuers ofACS medicinal chemistry letters · 2025Article
- Mitochonic acid 5 mitigates age-related hearing loss progression by targeting defective 2-methylthiolation in mitochondrial transfer RNAs.Frontiers in cellular neuroscience · 2025Article
- Linalool exhibit antimicrobial ability againstCurrent research in microbial sciences · 2025Article
- OSGEP regulates islet β-cell function by modulating proinsulin translation and maintaining ER stress homeostasis in mice.Nature communications · 2024Article
- tRNA expression and modification landscapes, and their dynamics during zebrafish embryo development.Nucleic acids research · 2024Article
- Hepatic Transcriptome and Its Regulation Following Soluble Epoxide Hydrolase Inhibition in Alcohol-Associated Liver Disease.The American journal of pathology · 2024Article
- Escherichia coli tRNA (Gm18) methyltransferase (TrmH) requires the correct localization of its methylation site (G18) in the D-loop for efficient methylation.Journal of biochemistry · 2023Article
- Mitochondrial alterations in the cochlea of Cdk5rap1-knockout mice with age-related hearing loss.FEBS open bio · 2023Article
- CDKAL1 Drives the Maintenance of Cancer Stem-Like Cells by Assembling the eIF4F Translation Initiation Complex.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Molecular Genetics of Abnormal Redox Homeostasis in Type 2 Diabetes Mellitus.International journal of molecular sciences · 2023Review
- Biochemical and genetic studies define the functions of methylthiotransferases in methanogenic and methanotrophic archaea.Frontiers in microbiology · 2023Article
- tRNA Modifications and Modifying Enzymes in Disease, the Potential Therapeutic Targets.International journal of biological sciences · 2023Review
- Metabolic Analysis of Nucleosides/Bases in the Urine and Serum of Patients with Alcohol-Associated Liver Disease.Metabolites · 2022Article
- Conservation and Diversification of tRNA tInternational journal of molecular sciences · 2022Review
- Characterization of LipS1 and LipS2 fromACS bio & med chem Au · 2022Article
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial and eukaryotic transfer RNAs have been shown to contain hypermodified adenosine, 2-methylthio-N(6)-threonylcarbamoyladenosine, at position 37 (A(37)) adjacent to the 3'-end of the anticodon, which is essential for efficient and highly accurate protein translation by the ribosome. Using a combination of bioinformatic sequence analysis and in vivo assay coupled to HPLC/MS technique, we have identified, from distinct sequence signatures, two methylthiotransferase (MTTase) subfamilies, designated as MtaB in bacterial cells and e-MtaB in eukaryotic and archaeal cells. Both subfamilies are responsible for the transformation of N(6)-threonylcarbamoyladenosine into 2-methylthio-N(6)-threonylcarbamoyladenosine. Recently, a variant within the human CDKAL1 gene belonging to the e-MtaB subfamily was shown to predispose for type 2 diabetes. CDKAL1 is thus the first eukaryotic MTTase identified so far. Using purified preparations of Bacillus subtilis MtaB (YqeV), a CDKAL1 bacterial homolog, we demonstrate that YqeV/CDKAL1 enzymes, as the previously studied MTTases MiaB and RimO, contain two [4Fe-4S] clusters. This work lays the foundation for elucidating the function of CDKAL1.
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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.