TRDMT1 (tRNA (cytosine(38)-C(5))-methyltransferase): TRDMT1 is an enzyme responsible for catalyzing the methylation of cytosine at position 38 in tRNA molecules. This post-transcriptional modification, known as 5-methylcytosine (m5C), is essential for the stability and proper function of tRNA. Methylation of cytosine at position 38 contributes to tRNA folding, stability, and accurate codon recognition during translation. TRDMT1-mediated tRNA methylation plays crucial roles in various cellular processes, including protein synthesis, regulation of gene expression, and cellular stress responses. Dysregulation of TRDMT1 activity or tRNA methylation has been implicated in several human diseases, including cancer, neurodegenerative disorders, and developmental abnormalities. Additionally, TRDMT1 has been shown to participate in the cellular response to environmental stressors, such as oxidative stress and viral infections. Understanding the molecular mechanisms underlying TRDMT1-mediated tRNA methylation and its functional significance in cellular physiology and disease pathogenesis is an area of active research. Further elucidation of TRDMT1's role in regulating tRNA function and its implications for human health may uncover novel therapeutic targets for diseases associated with aberrant tRNA modification or translation regulation. Additionally, targeting TRDMT1 activity could potentially offer new strategies for modulating cellular stress responses and improving disease outcomes.


Test(s) that measure/test for TRDMT1

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