Abstract:
:Retinoic acid-inducible gene I (RIG-I) is a pattern recognition receptor expressed in metazoan cells that is responsible for eliciting the production of type I interferons and pro-inflammatory cytokines upon detection of intracellular, non-self RNA. Structural studies of RIG-I have identified a novel Pincer domain composed of two alpha helices that physically tethers the C-terminal domain to the SF2 helicase core. We find that the Pincer plays an important role in mediating the enzymatic and signaling activities of RIG-I. We identify a series of mutations that additively decouple the Pincer motif from the ATPase core and show that this decoupling results in impaired signaling. Through enzymological and biophysical analysis, we further show that the Pincer domain controls coupled enzymatic activity of the protein through allosteric control of the ATPase core. Further, we show that select regions of the HEL1 domain have evolved to potentiate interactions with the Pincer domain, resulting in an adapted ATPase cleft that is now responsive to adjacent domains that selectively bind viral RNA.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Rawling DC,Kohlway AS,Luo D,Ding SC,Pyle AMdoi
10.1093/nar/gku817subject
Has Abstractpub_date
2014-10-01 00:00:00pages
11601-11issue
18eissn
0305-1048issn
1362-4962pii
gku817journal_volume
42pub_type
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