A physicochemical rationale for the varied catalytic efficiency in RNase J paralogues.

ABSTRACT: Paralogs of the bifunctional nuclease, Ribonuclease J (RNase J), demonstrate varied catalytic efficiencies despite extensive sequence and structural similarity. Of the two Staphylococcus aureus RNase J paralogues, RNase J1 is substantially more active than RNase J2. Mutational analysis of active site residues revealed that only H80 and E166 were critical for nuclease activity. Electronic properties of active site residues were further evaluated using density functional theory in conjunction with molecular mechanics. This analysis suggested that multiple residues at the active site can function as Lewis bases or acids in RNase J2. The bond dissociation energy, on the other hand, suggested that the Mn ion in RNase J2, located at a structurally identical location to that in RNase J1, is cruci

SUBMITTER: Singh AK 

PROVIDER: S-EPMC11815676 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature