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A functional deadenylation assay identifies human CUG‐BP as a deadenylation factor
Author(s) -
Paillard Luc,
Legagneux Vincent,
Osborne H. Beverley
Publication year - 2003
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1016/s0248-4900(03)00010-8
Subject(s) - xenopus , biology , rna binding protein , microbiology and biotechnology , rna , cytoplasm , rna splicing , myotonic dystrophy , genetics , gene
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.