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Identification of a novel Xenopus laevis poly (A) binding protein
Author(s) -
Cosson Bertrand,
Braun Frederique,
Paillard Luc,
Blackshear Perry,
Beverley H. Osborne
Publication year - 2004
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/j.biolcel.2004.04.006
Subject(s) - xenopus , biology , poly(a) binding protein , polyadenylation , dna binding protein , cytoplasm , translation (biology) , microbiology and biotechnology , rna binding protein , messenger rna , nuclear protein , function (biology) , biochemistry , transcription factor , gene
Summry— 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.