Based upon the structure of S. cerevisiae arginyl-tRNA synthetase, the DALR domain forms a nucleic acid binding pocket that recognizes the minor groove side of arginine tRNA anticodon stems through van der Waals, hydrophobic and electrostatic interactions37. Thus, we investigated whether DALRD3 interacts with tRNAs and if so, whether there was a particular binding specificity for DALRD3. To elucidate the RNA interactions mediated by DALRD3, we transiently expressed and purified Strep-DALRD3 from 293T cells either alone or with FLAG-METTL2A/B (Fig. 2a). Following binding to streptactin resin, we confirmed the purification of Strep-DALRD3 along with the co-purification of METTL2A or 2B (Fig. 2a). These results further corroborate the interaction between DALRD3 and METTL2A/B as shown above.
