Effect of magnesium ions on the thermal stability of human poly(A)‐specific ribonuclease | Zendy

Liu Wei-Feng | Zendy; Zhang Ao | Zendy; Cheng Yuan | Zendy; Zhou Hai-Meng | Zendy; Yan Yong-Bin | Zendy

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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.

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