title: Uridylation and PABP Cooperate to Repair mRNA Deadenylated Ends in Arabidopsis.
abstract: Uridylation emerges as a key modification promoting mRNA degradation in eukaryotes. In addition, uridylation by URT1 prevents the accumulation of excessively deadenylated mRNAs in Arabidopsis. Here, we show that the extent of mRNA deadenylation is controlled by URT1. By using TAIL-seq analysis, we demonstrate the prevalence of mRNA uridylation and the existence, at lower frequencies, of mRNA cytidylation and guanylation in Arabidopsis. Both URT1-dependent and URT1-independent types of uridylation co-exist but only URT1-mediated uridylation prevents the accumulation of excessively deadenylated mRNAs. Importantly, uridylation repairs deadenylated extremities to restore the size distribution observed for non-uridylated oligo(A) tails. In vivo and in vitro data indicate that Poly(A) Binding Protein (PABP) binds to uridylated oligo(A) tails and determines the length of U-extensions added by URT1. Taken together, our results uncover a role for uridylation and PABP in repairing mRNA deadenylated ends and reveal that uridylation plays diverse roles in eukaryotic mRNA metabolism.
authors.affiliation: Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 67000 Strasbourg, France.
authors.forename: Hélène
authors.initials: H
authors.lastname: Zuber
authors.affiliation: Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 67000 Strasbourg, France.
authors.forename: Hélène
authors.initials: H
authors.lastname: Scheer
authors.affiliation: Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 67000 Strasbourg, France.
authors.forename: Emilie
authors.initials: E
authors.lastname: Ferrier
authors.affiliation: Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 67000 Strasbourg, France.
authors.forename: François Michaël
authors.initials: FM
authors.lastname: Sement
authors.affiliation: Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 67000 Strasbourg, France.
authors.forename: Pierre
authors.initials: P
authors.lastname: Mercier
authors.affiliation: Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 67000 Strasbourg, France.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Stupfler
authors.affiliation: Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 67000 Strasbourg, France. Electronic address: dominique.gagliardi@ibmp-cnrs.unistra.fr.
authors.forename: Dominique
authors.initials: D
authors.lastname: Gagliardi
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D015153:Blotting, Western; D047468:Immunoprecipitation; D035683:MicroRNAs / Q000378:metabolism; D011061:Poly A / Q000378:metabolism; D011072:Poly U / Q000378:metabolism; D039102:Poly(A)-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D034622:RNA Interference; D012316:RNA Nucleotidyltransferases / Q000235:genetics / Q000378:metabolism*; D020871:RNA Stability; D012333:RNA, Messenger / Q000378:metabolism*; D034741:RNA, Small Interfering / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification
chemical_list: D029681:Arabidopsis Proteins; D035683:MicroRNAs; D039102:Poly(A)-Binding Proteins; D012333:RNA, Messenger; D034741:RNA, Small Interfering; D011994:Recombinant Proteins; D011061:Poly A; D011072:Poly U; D012316:RNA Nucleotidyltransferases; C584074:URT1 protein, Arabidopsis