{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["18(12)"],"submitter":["Li H"],"pubmed_abstract":["Methylation is a common post-transcriptional modification of tRNAs, particularly in the anticodon loop region. The cytosine 38 (C38) in tRNAs, such as tRNA<sup>Asp-GUC</sup>, tRNA<sup>Gly-GCC</sup>, tRNA<sup>Val-AAC</sup>, and tRNA<sup>Glu-CUC</sup>, can be methylated by human DNMT2/TRDMT1 and some homologs found in bacteria, plants, and animals. However, the substrate properties and recognition mechanism of DNMT2/TRDMT1 remain to be explored. Here, taking into consideration common features of the four known substrate tRNAs, we investigated methylation activities of DNMT2/TRDMT1 on the tRNA<sup>Gly-GCC</sup> truncation and point mutants, and conformational changes of mutants. The results demonstrated that human DNMT2/TRDMT1 preferred substrate tRNA<sup>Gly-GCC</sup> in vitro. L-shaped conf"],"journal":["RNA biology"],"pagination":["2531-2545"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8632113"],"repository":["biostudies-literature"],"pubmed_title":["New substrates and determinants for tRNA recognition of RNA methyltransferase DNMT2/TRDMT1."],"pmcid":["PMC8632113"],"pubmed_authors":["Li H","Wu J","Cai C","Qin M","Ma Y","Chen Y","Zhu D","Dai H"],"additional_accession":[]},"is_claimable":false,"name":"New substrates and determinants for tRNA recognition of RNA methyltransferase DNMT2/TRDMT1.","description":"Methylation is a common post-transcriptional modification of tRNAs, particularly in the anticodon loop region. The cytosine 38 (C38) in tRNAs, such as tRNA<sup>Asp-GUC</sup>, tRNA<sup>Gly-GCC</sup>, tRNA<sup>Val-AAC</sup>, and tRNA<sup>Glu-CUC</sup>, can be methylated by human DNMT2/TRDMT1 and some homologs found in bacteria, plants, and animals. However, the substrate properties and recognition mechanism of DNMT2/TRDMT1 remain to be explored. Here, taking into consideration common features of the four known substrate tRNAs, we investigated methylation activities of DNMT2/TRDMT1 on the tRNA<sup>Gly-GCC</sup> truncation and point mutants, and conformational changes of mutants. The results demonstrated that human DNMT2/TRDMT1 preferred substrate tRNA<sup>Gly-GCC</sup> in vitro. L-shaped conf","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Dec","modification":"2026-05-06T03:13:39.34Z","creation":"2025-02-19T00:56:14.191Z"},"accession":"S-EPMC8632113","cross_references":{"pubmed":["34110975"],"doi":["10.1080/15476286.2021.1930756"]}}