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

作者：Kim Yun Mi; Choi Won Young; Oh Chang Mok; Han Gyoon Hee; Kim Young Joon^*

来源：BMB Reports, 2014, 47(10): 558-562.

DOI：10.5483/BMBRep.2014.47.10.281

• Irf7
• OASL1
• SHAPE
• Secondary structure
• 1M7

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.

• 出版日期2014-10-31