Effect of magnesium ions on the thermal stability of human poly(A)-specific ribonuclease

被引:28
|
作者
Liu, Wei-Feng
Zhang, Ao
Cheng, Yuan
Zhou, Hai-Meng [1 ]
Yan, Yong-Bin
机构
[1] Tsinghua Univ, Dept Biol Sci & Biotechnol, Prot Sci Lab, Minist Educ, Beijing 100084, Peoples R China
[2] Tsinghua Univ, Dept Biol Sci & Biotechnol, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
基金
中国国家自然科学基金;
关键词
poly(A) specific ribonuclease; thermal stability; divalent metal cation; thermal aggregation; mRNA turnover;
D O I
10.1016/j.febslet.2007.02.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Poly(A)-specific ribonuclease (PARN), a member of the DEDD family, is a key enzyme involved in the deadenylation of mRNA in higher eukaryotic cells. In this research, it was found that Mg2+ could protect PARN against thermal inactivation by increasing the midpoint of inactivation and decreasing the inactivation rate. This protective effect was unique to Mg2+ in a concentration-dependent manner. However, the thermal unfolding and aggregation was promoted by the addition of Mg2+ at high temperatures. These results revealed that Mg2+ might have dual effects on PARN stability: protecting the active site but endangering the overall structural stability. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:1047 / 1052
页数:6
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