Yeast tRNA (m(7)G46) methyltransferase contains two protein subunits (Trm8 and Trm82). To address the RNA recognition mechanism of the Trm8-Trm82 complex, we investigated methyl acceptance activities of eight truncated yeast tRNA(Phe) transcripts. Both the D-stem and T-stem structures were required for efficient methyl-transfer. To clarify the role of the D-stem structure, we tested four mutant transcripts, in which tertiary base pairs were disrupted. The tertiary base pairs were important but not essential for the methyl-transfer to yeast tRNA(Phe) transcript, suggesting that these base pairs support the induced fit of the G46 base into the catalytic pocket.
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| Gene/Complex | Qualifier | Gene Ontology Term | Annotation Extension | Evidence | Source | Assigned On |
|---|---|---|---|---|---|---|
| TRM8 | part of | tRNA (m7G46) methyltransferase complex | IDA | SGD | 2018-09-14 | |
| TRM8 | enables | tRNA (guanine(46)-N7)-methyltransferase activity | IDA | SGD | 2022-06-24 | |
| TRM8 | involved in | tRNA (guanine-N7)-methylation | IDA | SGD | 2018-09-14 | |
| TRM82 | involved in | tRNA (guanine-N7)-methylation | IDA | SGD | 2018-09-14 | |
| TRM82 | part of | tRNA (m7G46) methyltransferase complex | IDA | SGD | 2018-09-14 | |
| TRM82 | enables | enzyme activator activity | IDA | SGD | 2022-06-24 |