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A functional deadenylation assay identifies human CUG-BP as a deadenylation factor.

Abstract : CUG-BP is a human nuclear and cytoplasmic RNA-binding protein. A role in the control of alternative splicing has been reported, but to date no cytoplasmic function for this protein has been demonstrated. A close sequence homolog of CUG-BP is EDEN-BP that is required for the specific cytoplasmic poly(A) tail shortening of certain mRNAs after fertilization of Xenopus eggs. Here, we show that human CUG-BP and Xenopus EDEN-BP have very similar RNA-binding specificities. In addition, we use a deadenylation assay to show that CUG-BP is able to act as a deadenylation factor. In contrast, a mutant form of CUG-BP, though still able to bind to RNA with a specificity similar to that of wild-type CUG-BP, does not act as a deadenylation factor. It is suggested that the CUG expansion associated with Type 1 myotonic dystrophy can affect the function or the activity of CUG-BP, leading to a trans-dominant effect on normal RNA processing. The results presented here identify CUG-BP-dependent deadenylation as a potential cytoplasmic target for this trans-dominant effect.
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Contributor : Vincent Legagneux Connect in order to contact the contributor
Submitted on : Thursday, March 25, 2010 - 3:16:26 PM
Last modification on : Wednesday, March 30, 2022 - 2:35:44 PM

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Luc Paillard, Vincent Legagneux, Howard Beverley Osborne. A functional deadenylation assay identifies human CUG-BP as a deadenylation factor.. Biology of the Cell, Wiley, 2003, 95 (2), pp.107-13. ⟨10.1016/S0248-4900(03)00010-8⟩. ⟨inserm-00467001⟩



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