3C-O1-1045(3P-40) PDF
ESI-MSによる大腸菌由来Ribonuclease H1の分析
We analyzed the metalloenzyme, Ribonuclease H1 form Escherichia coli (RNase H1) and the complex with its substrate, RNA/DNA hybrid. RNase H1 is an endoribonuclease that hydrolyzes the RNA strand of RNA/DNA hybrid. RNase H1 activity requires divalent metal ions (Mn2+, Mg2+) for the hydrolysis of phosphodiester bond, producing 5’-phosphate and 3’-hydroxyl termini. In this study, we aim to detect the complex of RNase H1: divalent metal ions: RNA/DNA hybrid using ESI-MS, and to reveal stoichiometry of these molecules.