物理化学学报 >> 2001, Vol. 17 >> Issue (10): 865-867.doi: 10.3866/PKU.WHXB20011001

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古细菌RNase HII与金属离子结合的热力学研究

赖兵;李颖;曹傲能;来鲁华   

  1. 分子动态与稳态结构国家重点实验室,北京大学物理化学研究所,北京大学化学学院,北京　100871
  • 收稿日期:2001-06-11 修回日期:2001-07-05 发布日期:2001-10-15
  • 通讯作者: 来鲁华 E-mail:lai@mdl.ipc.pku.edu.cn

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

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摘要： RNase H是一种专一性水解RNA:DNA杂合链中RNA链的核糖核酸酶,它广泛存在于从原核生物到人的生物体中.本文通过等温滴定量热技术研究了Mg2＋,Mn2＋和Ca2＋与一种古细菌Methanococcus jannaschii中的II型RNase H结合的热力学.首次用这种方法获得了这一结合过程的热力学参数.并证实了这些金属离子与RNase HII按1∶1结合.为RNase HII酶反应机理和折叠研究提供了重要信息.

关键词: RNase HII, 等温滴定量热, 二价金属离子

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