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KMID : 0624620140470100558
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BMB Reports
2014 Volume.47 No. 10 p.558 ~ p.562
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Secondary structure of the Irf7 5’-UTR, analyzed using SHAPE (selective 2’-hydroxyl acylation analyzed by primer extension)
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Kim Yun-Mi
Choi Won-Young
Oh Chang-Mok
Han Gyoon-Hee
Kim Young-Joon
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Abstract
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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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KEYWORD
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Irf7, OASL1, SHAPE, Secondary structure, 1M7
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