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

FEBS Lett. 2007 Mar 6;581(5):1047-52. doi: 10.1016/j.febslet.2007.02.008. Epub 2007 Feb 14.

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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Cations, Divalent / pharmacology
  • Enzyme Stability / drug effects
  • Exoribonucleases / antagonists & inhibitors
  • Exoribonucleases / metabolism*
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Magnesium / pharmacology*
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / metabolism
  • Thermodynamics

Substances

  • Cations, Divalent
  • Recombinant Proteins
  • Exoribonucleases
  • poly(A)-specific ribonuclease
  • Magnesium