The Rrp6 C-terminal domain binds RNA and activates the nuclear RNA exosome Journal Article

Authors: Wasmuth, E. V.; Lima, C. D.
Article Title: The Rrp6 C-terminal domain binds RNA and activates the nuclear RNA exosome
Abstract: The eukaryotic RNA exosome is an essential, multi-subunit complex that catalyzes RNA turnover, maturation, and quality control processes. Its non-catalytic donut-shaped core includes 9 subunits that associate with the 3′ to 5′ exoribonucleases Rrp6, and Rrp44/Dis3, a subunit that also catalyzes endoribonuclease activity. Although recent structures and biochemical studies of RNA bound exosomes from S. cerevisiae revealed that the Exo9 central channel guides RNA to either Rrp6 or Rrp44 using partially overlapping and mutually exclusive paths, several issues related to RNA recruitment remain. Here, we identify activities for the highly basic Rrp6 C-terminal tail that we term the 'lasso' because it binds RNA and stimulates ribonuclease activities associated with Rrp44 and Rrp6 within the 11-subunit nuclear exosome. Stimulation is dependent on the Exo9 central channel, and the lasso contributes to degradation and processing activities of exosome substrates in vitro and in vivo. Finally, we present evidence that the Rrp6 lasso may be a conserved feature of the eukaryotic RNA exosome. © The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.
Journal Title: Nucleic Acids Research
Volume: 45
Issue: 2
ISSN: 0305-1048
Publisher: Oxford University Press  
Date Published: 2017-01-01
Start Page: 846
End Page: 860
Language: English
DOI: 10.1093/nar/gkw1152
PROVIDER: scopus
PMCID: PMC5314766
PUBMED: 27899565
Notes: Article -- Export Date: 3 April 2017 -- Source: Scopus
Citation Impact
MSK Authors
  1. Christopher D Lima
    95 Lima
  2. Elizabeth Wasmuth
    10 Wasmuth