| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2051298 | FEBS Letters | 2007 | 6 Pages |
Abstract
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.
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Authors
Wei-Feng Liu, Ao Zhang, Yuan Cheng, Hai-Meng Zhou, Yong-Bin Yan,