IvanWoo22/RNase_R_structure_prediction

RNase R is a member of the RNA exonuclease family that digests RNA from 3′ to 5′. Previous studies have identified RNase R from Mycoplasma genitalium (MgR) as its only RNA exonuclease, which is sensitive to Nm modification. However, the mechanism of this characteristic is not well understood. In this study, we aimed to explore the molecular mechanism of RNase R Nm sensitivity with the help of a newly established quantitative assay, which excluded the effect of hydrolytic activity. By comparing five wild-type RNase R from Mycoplasma, we indicated the importance of loop 18 in Nm sensitivity. Furthermore, we demonstrated the critical roles of L283, T278, and T279. This study deepened the molecular mechanism of the Nm sensitivity of MgR and provided the potential direction of protein engineering for application.