Abstract

Table of contents
Plenary Lectures
Award Lecture
Oral Sessions Day1, Day2, Day3
Poster Presentations Day1, Day2, Day3
Workshops
Panel Discussion
Luncheon Seminar Day1, Day2, Day3
Timetable

Oral Sessions

Day 3: Friday, May 20　10:45-11:00　Room C (Seiun 2)

3C-O1-1045（3P-40）　　PDF

Analysis of a Metalloprotein, Ribonuclease H1 from Escherichia coli by ESI-MS

(1Osaka Univ., 2Osaka Univ., 3CIGB, 4JEOL)
oTomoshige Ando1, Elias Tannous2, Jorge Fernandez-de-Cossio3, Jun Tamura4, Shigenori Kanaya2, Toshifumi Takao1

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.