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• W2066337857 abstract "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." @default.
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• W2066337857 date "2006-03-01" @default.
• W2066337857 modified "2023-10-14" @default.
• W2066337857 title "Stability of casein mRNA is ensured by structural interactions between the 3′-untranslated region and poly(A) tail via the HuR and poly(A)-binding protein complex" @default.
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• W2066337857 doi "https://doi.org/10.1016/j.bbaexp.2006.04.004" @default.
• W2066337857 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16714065" @default.
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