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Effect of magnesium ions on the thermal stability of human poly(A)‐specific ribonuclease
Author(s) -
Liu Wei-Feng,
Zhang Ao,
Cheng Yuan,
Zhou Hai-Meng,
Yan Yong-Bin
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.02.008
Subject(s) - ribonuclease , chemistry , thermal stability , magnesium , enzyme , biochemistry , gene , rna , organic chemistry
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 Mg 2+ could protect PARN against thermal inactivation by increasing the midpoint of inactivation and decreasing the inactivation rate. This protective effect was unique to Mg 2+ in a concentration‐dependent manner. However, the thermal unfolding and aggregation was promoted by the addition of Mg 2+ at high temperatures. These results revealed that Mg 2+ might have dual effects on PARN stability: protecting the active site but endangering the overall structural stability.