Program

Oral Sessions

Day 2, May 16（Wed.）　17:05-17:20　Room B (Seiun 1)

2B-O3-M-1705　　PDF

Analysis of the Complex of Metallo-protein RNase HI and Substrate RNA/DNA Hybrid by Native Mass Spectrometry

(¹Osaka Univ., ²CIGB, ³Osaka Univ.)
^oTomoshige Ando¹, Jorge Fernandez-de-cossio², Shigenori Kanaya³, Toshifumi Takao¹

Ribonuclease HI (RNase HI) is an endoribonuclease which hydrolyzes the RNA strand of RNA/DNA hybrids, and generates 5’-phosphate and 3’-hydroxy termini. The enzymatic activity of RNase HI requires the divalent metal ions (Mg²⁺ or Mn²⁺). The enzyme-substrate complex is usually difficult to detect because it is subjected to rapid reaction, resulting in dissociation. In this study, we tried to measure the ternary complex of RNase HI, RNA/DNA hybrid, and Mn²⁺ ion, which has the enzymatic activity, by native mass spectrometry for its detection.