Four highly stable eukaryotic mRNAs assemble 3' untranslated region RNA-protein complexes sharing cis and trans components.

Assembly of a sequence-specific RNA-protein complex on the 3' untranslated region (3'UTR) of human alpha-globin mRNA (alpha-complex) correlates with mRNA stabilization. Here we map a limited segment of the alpha-globin 3'UTR that is both necessary and sufficient for alpha-complex formation. The sequence of this binding region identifies three additional, highly stable mRNAs that share closely related, pyrimidine-rich cis-motifs in their respective 3'UTRs. Each mRNA assembles a sequence-specific ribonucleoprotein complex at this conserved region. These complexes are structurally related, and each contains a 39-kDa cytoplasmic poly(C) binding protein previously demonstrated to be essential to formation of the alpha-complex. These observations indicate the existence of a general determinant for stabilization of eukaryotic mRNAs.