title: Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex.
abstract: mRNA localization is an essential mechanism of gene regulation and is required for processes such as stem-cell division, embryogenesis and neuronal plasticity. It is not known which features in the cis-acting mRNA localization elements (LEs) are specifically recognized by motor-containing transport complexes. To the best of our knowledge, no high-resolution structure is available for any LE in complex with its cognate protein complex. Using X-ray crystallography and complementary techniques, we carried out a detailed assessment of an LE of the ASH1 mRNA from yeast, its complex with its shuttling RNA-binding protein She2p, and its highly specific, cytoplasmic complex with She3p. Although the RNA alone formed a flexible stem loop, She2p binding induced marked conformational changes. However, only joining by the unstructured She3p resulted in specific RNA recognition. The notable RNA rearrangements and joint action of a globular and an unfolded RNA-binding protein offer unprecedented insights into the step-wise maturation of an mRNA-transport complex.
authors.affiliation: Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.
authors.forename: Franziska Theresia
authors.initials: FT
authors.lastname: Edelmann
authors.affiliation: Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Department Chemie, Technische Universität München, Garching, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Schlundt
authors.affiliation: Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.
authors.forename: Roland Gerhard
authors.initials: RG
authors.lastname: Heym
authors.affiliation: Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
authors.forename: Andreas
authors.initials: A
authors.lastname: Jenner
authors.affiliation: Biomedical Center of the Ludwig-Maximilians-Universität München, Department of Cell Biology, Planegg-Martinsried, Germany.
authors.forename: Annika
authors.initials: A
authors.lastname: Niedner-Boblenz
authors.affiliation: Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
authors.forename: Muhammad Ibrahim
authors.initials: MI
authors.lastname: Syed
authors.affiliation: Architecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France.
authors.forename: Jean-Christophe
authors.identifier: 0000-0003-1647-8917
authors.initials: JC
authors.lastname: Paillart
authors.affiliation: Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Department Chemie, Technische Universität München, Garching, Germany.
authors.forename: Ralf
authors.initials: R
authors.lastname: Stehle
authors.affiliation: Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.
authors.forename: Robert
authors.initials: R
authors.lastname: Janowski
authors.affiliation: Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.|Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Department Chemie, Technische Universität München, Garching, Germany.
authors.forename: Michael
authors.initials: M
authors.lastname: Sattler
authors.affiliation: Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.
authors.forename: Ralf-Peter
authors.initials: RP
authors.lastname: Jansen
authors.affiliation: Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany.|Biomedical Center of the Ludwig-Maximilians-Universität München, Department of Cell Biology, Planegg-Martinsried, Germany.
authors.forename: Dierk
authors.identifier: 0000-0002-5589-369X
authors.initials: D
authors.lastname: Niessing
mesh_terms: D001483:Base Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D055029:Inverted Repeat Sequences; D008958:Models, Molecular; D011485:Protein Binding; D034443:RNA Transport; D012333:RNA, Messenger / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
chemical_list: C098733:ASH1 protein, S cerevisiae; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D012097:Repressor Proteins; C471175:SHE2 protein, S cerevisiae; C471176:SHE3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins