ArticleBMB reports2014
Secondary structure of the Irf7 5'-UTR, analyzed using SHAPE (selective 2'-hydroxyl acylation analyzed by primer extension).
Article in BMB reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 3 citations in OpenAlex.
- Expression dynamics and antiviral role of chicken OASL during infectious bronchitis virus infection.Poultry science · 2026Article
- Ribosome profiling reveals a functional role for autophagy in mRNA translational control.Communications biology · 2020Article
- OASL1 Traps Viral RNAs in Stress Granules to Promote Antiviral Responses.Molecules and cells · 2018Article
- Oligoadenylate synthase-like (OASL) proteins: dual functions and associations with diseases.Experimental & molecular medicine · 2015Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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Abstract
OASL1 is a member of the 2'-5'-oligoadenylate synthetase (OAS) family and promotes viral clearance by activating RNase L. OASL1 interacts with the 5'-untranslated region (UTR) of interferon regulatory factor 7 (Irf7) and inhibits its translation. To identify the secondary structure required for OASL1 binding, we examined the 5'-UTR of the Irf7 transcript using "selective 2'-hydroxyl acylation analyzed by primer extension" (SHAPE). SHAPE takes advantage of the selective acylation of residues in single-stranded regions by 1-methyl-7-nitroisatoic anhydride (1M7). We found five major acylation sites located in, or next to, predicted single-stranded regions of the Irf7 5'-UTR. These results demonstrate the involvement of the stem structure of the Irf7 5'-UTR in the regulation of Irf7 translation, mediated by OASL1.
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