Acta Phys. -Chim. Sin. ›› 2001, Vol. 17 ›› Issue (10): 865-867.doi: 10.3866/PKU.WHXB20011001

• Communication •     Next Articles

Thermodynamic Study on Binding of Archaebacterial RNase HII and Metal Ions

Lai Bing;Li Ying;Cao Ao-Neng;Lai Lu-Hua   

  1. State Key Laboratory for Structural Studies of Stable and Unstable Species,Institute of Physical Chemistry,College of Chemistry,Peking University,Beijing 100871
  • Received:2001-06-11 Revised:2001-07-05 Published:2001-10-15
  • Contact: Lai Lu-Hua E-mail:lai@mdl.ipc.pku.edu.cn

Abstract: RNase H,a ribonuclease specifically degrades the RNA chain in RNA:DNA hybrid,exists vastly in organisms from procaryotic to humanic.We use isothermal titration calorimetry to study the binding thermodynamics of Mg2+,Mn2+,Ca2+ to a type II RNase H from an archaeon:Methanococcus jannaschii.For the first time we obtain the thermodynamic parameters of this binding reaction and verify that these metal ions bind with RNase HII with a ratio of 1:1.This will give an important information for studying RNase HII reaction mechanism and folding properties.

Key words: RNase HII, Isothermal titration calorimetry, Divalent metal ion