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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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초록

OASL1 is a member of the 2’-5’-oligoadenylate synthetase(OAS) family and promotes viral clearance by activating RNaseL. OASL1 interacts with the 5’-untranslated region (UTR) ofinterferon regulatory factor 7 (Irf7) and inhibits its translation. To identify the secondary structure required for OASL1binding, 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 ofresidues in single-stranded regions by 1-methyl-7-nitroisatoicanhydride (1M7). We found five major acylation sites locatedin, or next to, predicted single-stranded regions of the Irf75’-UTR. These results demonstrate the involvement of the stemstructure of the Irf7 5’-UTR in the regulation of Irf7 translation,mediated by OASL1.

Abstract

OASL1 is a member of the 2’-5’-oligoadenylate synthetase(OAS) family and promotes viral clearance by activating RNaseL. OASL1 interacts with the 5’-untranslated region (UTR) ofinterferon regulatory factor 7 (Irf7) and inhibits its translation. To identify the secondary structure required for OASL1binding, 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 ofresidues in single-stranded regions by 1-methyl-7-nitroisatoicanhydride (1M7). We found five major acylation sites locatedin, or next to, predicted single-stranded regions of the Irf75’-UTR. These results demonstrate the involvement of the stemstructure of the Irf7 5’-UTR in the regulation of Irf7 translation,mediated by OASL1.

참고문헌 (21)

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