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- W2552910574 abstract "Ccr4-Not is a conserved protein complex that shortens the 3' poly(A) tails of eukaryotic mRNAs to regulate transcript stability and translation into proteins. RNA-binding proteins are thought to facilitate recruitment of Ccr4-Not to certain mRNAs, but lack of an in-vitro-reconstituted system has slowed progress in understanding the mechanistic details of this specificity. Here, we generate a fully recombinant Ccr4-Not complex that removes poly(A) tails from RNA substrates. The intact complex is more active than the exonucleases alone and has an intrinsic preference for certain RNAs. The RNA-binding protein Mmi1 is highly abundant in preparations of native Ccr4-Not. We demonstrate a high-affinity interaction between recombinant Ccr4-Not and Mmi1. Using in vitro assays, we show that Mmi1 accelerates deadenylation of target RNAs. Together, our results support a model whereby both RNA-binding proteins and the sequence context of mRNAs influence deadenylation rate to regulate gene expression." @default.
- W2552910574 created "2016-11-30" @default.
- W2552910574 creator A5011931952 @default.
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- W2552910574 creator A5049606398 @default.
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- W2552910574 date "2016-11-01" @default.
- W2552910574 modified "2023-10-13" @default.
- W2552910574 title "Reconstitution of Targeted Deadenylation by the Ccr4-Not Complex and the YTH Domain Protein Mmi1" @default.
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- W2552910574 doi "https://doi.org/10.1016/j.celrep.2016.10.066" @default.
- W2552910574 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5120349" @default.
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