Journal
NUCLEIC ACIDS RESEARCH
Volume 43, Issue 1, Pages 544-552Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku1289
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Funding
- National Institutes of Health-National Institute of Allergy and Infectious Diseases [R21-AI097803]
- National Institutes of Health-National Institute of General Medical Science [T32-GM008367]
- Emory University Research Council [URC 2010050]
- Department of Biochemistry, Emory University
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Human 2 '-5 ' oligoadenylate synthetase-1 (OAS1) is central in innate immune system detection of cytoplasmic double-stranded RNA (dsRNA) and promotion of host antiviral responses. However, the molecular signatures that promote OAS1 activation are currently poorly defined. We show that the 3 '-end polyuridine sequence of viral and cellular RNA polymerase III non-coding transcripts is critical for their optimal activation of OAS1. Potentiation of OAS1 activity was also observed with a model dsRNA duplex containing an OAS1 activation consensus sequence. We determined that the effect is attributable to a single appended 3 '-end residue, is dependent upon its single-stranded nature with strong preference for pyrimidine residues and is mediated by a highly conserved OAS1 residue adjacent to the dsRNA binding surface. These findings represent discovery of a novel signature for OAS1 activation, the 3 '-single-stranded pyrimidine (3 '-ssPy) motif, with potential functional implications for OAS1 activity in its antiviral and other anti-proliferative roles.
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