Effect of magnesium ions on the thermal stability of human poly(A)‐specific ribonuclease
- 14 February 2007
- journal article
- Published by Wiley in FEBS Letters
- Vol. 581 (5) , 1047-1052
- https://doi.org/10.1016/j.febslet.2007.02.008
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.Keywords
This publication has 39 references indexed in Scilit:
- mRNA deadenylation by PARN is essential for embryogenesis in higher plantsRNA, 2004
- Messenger RNA Turnover in Eukaryotes: Pathways and EnzymesCritical Reviews in Biochemistry and Molecular Biology, 2004
- The mechanism and regulation of deadenylation: Identification and characterization of Xenopus PARNRNA, 2001
- The cap-to-tail guide to mRNA turnoverNature Reviews Molecular Cell Biology, 2001
- A 54-kDa Fragment of the Poly(A)-specific Ribonuclease Is an Oligomeric, Processive, and Cap-interacting Poly(A)-specific 3′ ExonucleaseJournal of Biological Chemistry, 2000
- mRNA stability in eukaryotesCurrent Opinion in Genetics & Development, 2000
- Circularization of mRNA by Eukaryotic Translation Initiation FactorsMolecular Cell, 1998
- Poly(A) Tail Shortening by a Mammalian Poly(A)-specific 3′-ExoribonucleaseJournal of Biological Chemistry, 1997
- Function and Characterization of Poly(A)-Specific 3´ ExoribonucleasesPublished by Springer Nature ,1997
- Mechanisms and control of mRNA turnover in Saccharomyces cerevisiaeMicrobiological Reviews, 1996