TY - JOUR
T1 - Structural analysis of the yeast exosome Rrp6p-Rrp47p complex by small-angle x-ray scattering
AU - Dedic, Emil
AU - Seweryn, Paulina
AU - Jonstrup, Anette Thyssen
AU - Flygaard, Rasmus Koch
AU - Fedosova, Natalya U
AU - Hoffmann, Søren Vrønning
AU - Boesen, Thomas
AU - Brodersen, Ditlev E.
N1 - Copyright © 2014. Published by Elsevier Inc.
PY - 2014/7/18
Y1 - 2014/7/18
N2 - The RNase D-type 3'-5' exonuclease Rrp6p from Saccharomyces cerevisiae is a nuclear-specific cofactor of the RNA exosome and associates in vivo with Rrp47p (Lrp1p). Here, we show using biochemistry and small-angle x-ray scattering (SAXS) that Rrp6p and Rrp47p associate into a stable, heterodimeric complex with an elongated shape consistent with binding of Rrp47p to the nuclease domain and opposite of the HRDC domain of Rrp6p. Rrp47p reduces the exonucleolytic activity of Rrp6p on both single-stranded and structured RNA substrates without significantly altering the affinity towards RNA or the ability of Rrp6p to degrade RNA secondary structure.
AB - The RNase D-type 3'-5' exonuclease Rrp6p from Saccharomyces cerevisiae is a nuclear-specific cofactor of the RNA exosome and associates in vivo with Rrp47p (Lrp1p). Here, we show using biochemistry and small-angle x-ray scattering (SAXS) that Rrp6p and Rrp47p associate into a stable, heterodimeric complex with an elongated shape consistent with binding of Rrp47p to the nuclease domain and opposite of the HRDC domain of Rrp6p. Rrp47p reduces the exonucleolytic activity of Rrp6p on both single-stranded and structured RNA substrates without significantly altering the affinity towards RNA or the ability of Rrp6p to degrade RNA secondary structure.
U2 - 10.1016/j.bbrc.2014.06.032
DO - 10.1016/j.bbrc.2014.06.032
M3 - Journal article
C2 - 24937447
SN - 0006-291X
VL - 450
SP - 634
EP - 640
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -