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

Yun Mi Kim, Won Young Choi, Chang Mok Oh, Gyoon Hee Han, Young Joon Kim

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)558-562
Number of pages5
JournalBMB reports
Volume47
Issue number10
DOIs
Publication statusPublished - 2014

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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