Journal
MOLECULAR CELL
Volume 64, Issue 4, Pages 734-745Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2016.09.038
Keywords
-
Categories
Funding
- NIH/ORIP HEI [S10 RR029205]
- DOE Office of Science [DE-AC02-06CH11357]
- NIH/NIGMS [R01GM079196, R35GM118080, F31GM097910, P30 CA008748]
Ask authors/readers for more resources
The eukaryotic RNA exosome is an essential and conserved 3'-to-5' exoribonuclease complex that degrades or processes nearly every class of cellular RNA. The nuclear RNA exosome includes a 9-subunit non-catalytic core that binds Rrp44 (Dis3) and Rrp6 subunits to modulate their processive and distributive 3'-to-5' exoribonuclease activities, respectively. Here we utilize an engineered RNA with two 30 ends to obtain a crystal structure of an 11-subunit nuclear exosome bound to RNA at 3.1 angstrom. The structure reveals an extended RNA path to Rrp6 that penetrates into the non-catalytic core; contacts between the non-catalytic core and Rrp44, which inhibit exoribonuclease activity; and features of the Rrp44 exoribonuclease site that support its ability to degrade 3' phosphate RNA substrates. Using reconstituted exosome complexes, we show that 3' phosphate RNA is not a substrate for Rrp6 but is readily degraded by Rrp44 in the nuclear exosome.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available