Biochimica et biophysica actaMay 23, 2006

Casein mRNA stability is maintained by interactions between its tail regions through HuR and poly(A)-binding proteins

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Updated Mar 20, 2026

Abstract

Beta-casein mRNA with a long poly(A) tail exhibited higher stability compared to that with a short poly(A) tail.

The poly(A) tail and specific sequences in the 3'-UTR regulate beta-casein mRNA stability.
Rapid degradation of beta-casein mRNA occurs when poly(A) homopolymer and 3'-UTR cRNA are added as competitors.
A region within the 3'-UTR interacts with the poly(A) tail, suggesting a role in mRNA stability.
An AU-rich element (ARE) found at nucleotides 897-905 is necessary for the stability of the beta-casein mRNA.
Binding of the poly(A)-binding protein (PABP) and the RNA-binding protein HuR to the 3'-UTR is diminished in the absence of the ARE site.
Degradation of beta-casein mRNA can be accelerated in conditions where HuR and PABP are depleted.

Simplified

The maintenance of mRNA stability has emerged as a mechanism of post-transcriptional control. We demonstrate that beta-casein mRNA stability is dictated by the poly(A) tail and sequences in the 3'-UTR. An in vitro mRNA decay assay revealed that beta-casein mRNA with a long poly(A) tail had higher stability than that with a short poly(A) tail. The addition of poly(A) homopolymer and 3'-UTR cRNA as competitor induced rapid degradation of beta-casein mRNA. The interaction between full-length beta-casein mRNA and poly(A) homopolymer was inhibited by the addition of the 3'-UTR cRNA in the lysates, which indicates that one region of the 3'-UTR associates with the poly(A) tail through an RNA-protein interaction. The putative AU-rich element (ARE) is present at nt 897-905; deletion and mutation analysis showed that the ARE site was required for maintaining the stability of the beta-casein 3'-UTR. In the immunoprecipitation analysis, the poly(A)-binding protein (PABP) and the RNA-binding protein HuR were pulled down by 3'-UTR cRNA, and the absence of the ARE site reduced the binding of these proteins. These experiments further revealed that the rapid degradation of beta-casein mRNA was induced by incubation with HuR- and PABP-depleted RRLs. Collectively, our results suggest that beta-casein mRNA is protected from degradation by virtue of the structural interaction between the 3'-UTR and poly(A) tail via a protein complex of HuR and PABP.

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Casein mRNA stability is maintained by interactions between its tail regions through HuR and poly(A)-binding proteins

Abstract

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