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- W1566578128 abstract "The soluble guanylyl cyclases (sGC), the receptor for nitric oxide, are heterodimers consisting of an alpha- and beta-subunit. This study aimed to investigate the translational mechanism of the sGC beta2-subunit. Two mRNA species for sGC beta2 were isolated from human kidney. These transcripts had dissimilar 5'-untranslated regions (5'-UTRs). The most abundant sGC beta2 mRNA showed numerous upstream open reading frames (ORFs) and stable secondary structures that inhibited in vivo and in vitro translation. To evaluate whether these 5'-UTRs harbored an internal ribosome entry site (IRES) that allows translation by an alternative mechanism, we inserted these regions between the two luciferase genes of a bicistronic vector. Transfection of those genetic constructs into HeLa cells demonstrated that both sGC beta2 leaders had IRES activity in a cell-type dependent manner. Finally, the secondary structural model of the sGC beta2 5'-UTR predicts a Y-type pseudoknot that characterizes the IRES of cellular mRNAs. In conclusion, our findings suggest that sGC beta2 5'-UTRs have IRES activity that may permit sGC beta2 expression under conditions that are not optimal for scanning-dependent translation." @default.
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- W1566578128 date "2008-06-28" @default.
- W1566578128 modified "2023-10-17" @default.
- W1566578128 title "An internal ribosome entry site mediates the initiation of soluble guanylyl cyclase β2 mRNA translation" @default.
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- W1566578128 doi "https://doi.org/10.1111/j.1742-4658.2008.06505.x" @default.
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