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http://dx.doi.org/10.5483/BMBRep.2014.47.10.281

Secondary structure of the Irf7 5'-UTR, analyzed using SHAPE (selective 2'-hydroxyl acylation analyzed by primer extension)  

Kim, Yun-Mi (Department of Integrated OMICs for Biomedical Science, Yonsei University)
Choi, Won-Young (Department of Biochemistry, Yonsei University)
Oh, Chang-Mok (Department of Biotechnology, Yonsei University)
Han, Gyoon-Hee (Department of Integrated OMICs for Biomedical Science, Yonsei University)
Kim, Young-Joon (Department of Integrated OMICs for Biomedical Science, Yonsei University)
Publication Information
BMB Reports / v.47, no.10, 2014 , pp. 558-562 More about this Journal
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.
Keywords
Irf7; OASL1; SHAPE; Secondary structure; 1M7;
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