Distinct roles of the R3H and RRM domains in poly(A)-specific ribonuclease structural integrity and catalysis

Article ID	Journal	Published Year	Pages	File Type
10537011	Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics	2013	10 Pages	PDF

Abstract

âº We investigate the roles of three RNA-binding domains in PARN structure/function. âº The R3H domain can bind with various oligonucleotides with no preference. âº Removal of the R3H domain dissociates PARN into active monomers. âº Three RNA-binding sites act cooperatively in binding with long poly(A) substrates.

Keywords

P46 PARN P54 1-anilinonaphtalene-8-sulfonate Poly(A)-specific ribonuclease P60 p74 RRM SEC p62 CTD DTT IPTG isopropyl-1-thio-β-d-galactopyranoside RNA-recognition motif Size-exclusion chromatography Enzymatic property C-terminal domain dithiothreitol circular dichroism ANS Structural feature RNA binding