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.
机构:
Tsinghua Univ, Sch Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R ChinaTsinghua Univ, Sch Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
He, Guang-Jun
Liu, Wei-Feng
论文数: 0引用数: 0
h-index: 0
机构:
Tsinghua Univ, Sch Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R ChinaTsinghua Univ, Sch Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
Liu, Wei-Feng
Yan, Yong-Bin
论文数: 0引用数: 0
h-index: 0
机构:
Tsinghua Univ, Sch Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R ChinaTsinghua Univ, Sch Life Sci, State Key Lab Biomembrane & Membrane Biotechnol, Beijing 100084, Peoples R China
Yan, Yong-Bin
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES,
2011,
12
(05):
: 2901
-
2916