Identification of a novel Xenopus laevis poly (A) binding protein |
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Authors: | Cosson Bertrand Braun Frederique Paillard Luc Blackshear Perry Beverley Osborne H |
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Institution: | UMR6061 CNRS--Génétique et Développement, Université de Rennes 1, Faculté de Médecine, 2 avenue Professeur Leon Bernard, CS 34317, 35043 Rennes cedex, France. bertrand.cosson@univ-rennes1.fr |
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Abstract: | Poly (A) binding proteins are intimately implicated in controlling a number of events in mRNA metabolism from nuclear polyadenylation to cytoplasmic translation and stability. The known poly(A) binding proteins can be divided into three distinct structural groups (prototypes PABP1, PABPN1/PABP2 and Nab2p) and two functional families, showing that similar functions can be accomplished by differing structural units. This has prompted us to perform a screen for novel poly(A) binding proteins using Xenopus laevis. A novel poly(A) binding protein of 32 kDa (p32) was identified. Sequence analysis showed that p32 has about 50% identity to the known nuclear poly(A) binding proteins (PABPN1) but is more closely related to a group of mammalian proteins of unknown function. The expression of Xenopus laevis ePABP2 is restricted to early embryos. Accordingly, we propose that p32 is the founder member of a novel class of poly(A) binding proteins named ePABP2. |
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Keywords: | ePABP2 Cytoplasmic protein Oocytes Embryos |
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