%0 Journal Article %T Identification of a novel Xenopus laevis poly (A) binding protein. %+ Mer et santé (MS) %+ Recherches en cancérologie %+ Université européenne de Bretagne - European University of Brittany (UEB) %+ Institut de Génétique et Développement de Rennes (IGDR) %+ Duke University [Durham] %A Cosson, Bertrand %A Braun, Frederique %A Paillard, Luc %A Blackshear, Perry %A Beverley Osborne, H. %< avec comité de lecture %@ 0248-4900 %J Biology of the Cell %I Wiley %V 96 %N 7 %P 519-27 %8 2004-09 %D 2004 %R 10.1016/j.biolcel.2004.04.006 %M 15380618 %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biologyJournal articles %X 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. %G English %L hal-00982685 %U https://univ-rennes.hal.science/hal-00982685 %~ UNIV-NANTES %~ UPMC %~ UNIV-RENNES1 %~ CNRS %~ IFR140 %~ IGDR %~ IGDR-EGD %~ UR1-UFR-SVE %~ UR1-HAL %~ UR1-SDV %~ TEST-UNIV-RENNES %~ TEST-UR-CSS %~ UNIV-RENNES %~ SORBONNE-UNIVERSITE %~ SU-SCIENCES %~ SU-SCI %~ SU-TI %~ UR1-BIO-SA %~ ALLIANCE-SU %~ NANTES-UNIVERSITE %~ UNIV-NANTES-AV2022 %~ TEST3-HALCNRS %~ SBR