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Biol Cell. 2003 Mar-Apr;95(2):107-13.

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

Author information

1
CNRS UMR 6061, Faculté de Médecine, Université Rennes 1, 2, avenue Léon-Bernard, CS 34317, 35043 cedex, Rennes, France. Luc.Paillard@univ-rennes1.fr

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.

PMID:
12799066
DOI:
10.1016/s0248-4900(03)00010-8
[Indexed for MEDLINE]

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