title: Part of Xenopus translin is localized in the centrosomes during mitosis.
abstract: During oogenesis, maternal mRNAs are synthesised and stored in a translationally dormant form due to the presence of regulatory elements at the 3' untranslated regions (3'UTR). In Xenopus oocytes, several studies have described the presence of RNA-binding proteins capable to repress maternal-mRNA translation. The testis-brain RNA-binding protein (TB-RBP/Translin) is a single-stranded DNA- and RNA-binding protein which can bind the 3' UTR regions (Y and H elements) of stored mRNAs and can suppress in vitro translation of the mRNAs that contain these sequences. Here we report the cloning of the Xenopus homologue of the TB-RBP/Translin protein (X-translin) as well as its expression, its localisation, and its biochemical association with the protein named Translin associated factor X (Trax) in Xenopus oocytes. The fact that this protein is highly present in the cytoplasm from stage VI oocytes until 48 h embryos and that it has been described as capable to inhibit paternal mRNA translation, indicates that it could play an important role in maternal mRNA translation control during Xenopus oogenesis and embryogenesis. Moreover, we investigated X-translin localisation during cell cycle in XTC cells. In interphase, although a weak and diffuse nuclear staining was observed, X-translin was mostly present in the cytoplasm where it exhibited a prominent granular staining. Interestingly, part of X-translin underwent a remarkable redistribution throughout mitosis and associated with centrosomes, which may suggest a new unknown role for this protein in cell cycle.
authors.affiliation: Centre de Recherches de Biochimie Macromoléculaire, CNRS UPR 1086, 1919 Route de Mende, Montpellier cedex 5, 34293, France.
authors.forename: A
authors.initials: A
authors.lastname: Castro
authors.forename: M
authors.initials: M
authors.lastname: Peter
authors.forename: L
authors.initials: L
authors.lastname: Magnaghi-Jaulin
authors.forename: S
authors.initials: S
authors.lastname: Vigneron
authors.forename: D
authors.initials: D
authors.lastname: Loyaux
authors.forename: T
authors.initials: T
authors.lastname: Lorca
authors.forename: J C
authors.initials: JC
authors.lastname: Labbé
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D018385:Centrosome / Q000378:metabolism*; D016384:Consensus Sequence; D018076:DNA, Complementary / Q000032:analysis; D004277:DNA, Single-Stranded / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D008938:Mitosis / Q000235:genetics*; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000378:metabolism; D009865:Oocytes / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014982:Xenopus laevis / Q000196:embryology
chemical_list: D002352:Carrier Proteins; D018076:DNA, Complementary; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; C095563:TSN protein, human; C498305:TSNAX protein, human