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

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 OA...

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Published in:BMB reports 2014, 47(10), , pp.558-562
Main Authors: Kim, Yun-Mi, Choi, Won-Young, Oh, Chang-Mok, Han, Gyoon-Hee, Kim, Young-Joon
Format: Article
Language:English
Subjects:
화학
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Summary: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. [BMB Reports 2014; 47(10): 558-562]
ISSN:1976-6696
1976-670X
DOI:10.5483/BMBRep.2014.47.10.281