Nucleoside-specific ribonuclease enzymes are useful for mapping chemical modifications in RNA. An uridine-specific ribonuclease from <i>Momordica charantia </i>can be one such molecular tool to sequence these modifications in RNA so that their structural and functional roles can be investigated. In this study, we determined the optimal conditions for heterologous expression of recombinant ribonuclease MC1, and successfully purified the active protein from a bacterial system. The purified protein was tested for its ribonuclease activity and nucleoside specificity against commercially available tRNA<sup>Tyr</sup> by ion-pairing reverse phase liquid-chromatography coupled with mass spectrometry (IP-RP-LC-MS). Ability of this purified protein to sequence nucleoside modifications through its nucleoside specificity will be discussed.

Optimal conditions for expression and purification of recombinant U-specific MC1 ribonuclease

249th National Meeting (2015)

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