Epigenetic regulation of the binding activity of translation inhibitory proteins that bind the 3′ untranslated region of β-F1-ATPase mRNA by adenine nucleotides and the redox state

Here, we describe the binding affinities and the regulation of the binding activities of the fetal liver proteins that interact with the 3′ untranslated region of β-F1-ATPase mRNA (β-mRNA). These proteins (3′β 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 3′β FBPs. In contrast, oxidizing and alkylating reagents abolished the binding activity of 3′β 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 3′β 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 3′β FBPs and therefore in the translation of β-mRNA.