Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9882386 | Archives of Biochemistry and Biophysics | 2005 | 6 Pages |
Abstract
Here, we describe the binding affinities and the regulation of the binding activities of the fetal liver proteins that interact with the 3â² untranslated region of β-F1-ATPase mRNA (β-mRNA). These proteins (3â²Î² FBPs), which are involved in the repression of β-mRNA translation during fetal development, have poly(A)-binding activity. Reducing agents do not affect the RNA-binding activity of 3â²Î² FBPs. In contrast, oxidizing and alkylating reagents abolished the binding activity of 3â²Î² FBPs to its target RNA element, an effect that is partially prevented by the presence of reducing agents. Interestingly, the availability of adenine nucleotides regulates in a concentration-dependent manner the binding activities of 3â²Î² FBPs. The results suggest that epigenetic changes that occur at the time of birth affecting both the redox and energy state of the liver play a relevant role in the regulation of the binding activities of 3â²Î² FBPs and therefore in the translation of β-mRNA.
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Authors
José M. Izquierdo, José M. Cuezva,