title: New Insights into Structural Disorder in Human Respiratory Syncytial Virus Phosphoprotein and Implications for Binding of Protein Partners.
abstract: Phosphoprotein is the main cofactor of the viral RNA polymerase ofMononegaviralesIt is involved in multiple interactions that are essential for the polymerase function. Most prominently it positions the polymerase complex onto the nucleocapsid, but also acts as a chaperone for the nucleoprotein.Mononegaviralesphosphoproteins lack sequence conservation, but contain all large disordered regions. We show here that N- and C-terminal intrinsically disordered regions account for 80% of the phosphoprotein of the respiratory syncytial virus. But these regions display marked dynamic heterogeneity. Whereas almost stable helices are formed C terminally to the oligomerization domain, extremely transient helices are present in the N-terminal region. They all mediate internal long-range contacts in this non-globular protein. Transient secondary elements together with fully disordered regions also provide protein binding sites recognized by the respiratory syncytial virus nucleoprotein and compatible with weak interactions required for the processivity of the polymerase.
authors.affiliation: From the Institut de Chimie des Substances Naturelles, UPR2301, Centre National de la Recherche Scientifique, Université Paris Saclay, 91190 Gif-sur-Yvette and.
authors.forename: Nelson
authors.initials: N
authors.lastname: Pereira
authors.affiliation: From the Institut de Chimie des Substances Naturelles, UPR2301, Centre National de la Recherche Scientifique, Université Paris Saclay, 91190 Gif-sur-Yvette and.
authors.forename: Christophe
authors.initials: C
authors.lastname: Cardone
authors.affiliation: From the Institut de Chimie des Substances Naturelles, UPR2301, Centre National de la Recherche Scientifique, Université Paris Saclay, 91190 Gif-sur-Yvette and.
authors.forename: Safa
authors.initials: S
authors.lastname: Lassoued
authors.affiliation: the Unité de Virologie et Immunologie Moléculaires, UR892, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France.
authors.forename: Marie
authors.initials: M
authors.lastname: Galloux
authors.affiliation: the Unité de Virologie et Immunologie Moléculaires, UR892, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France.
authors.forename: Jenna
authors.initials: J
authors.lastname: Fix
authors.affiliation: From the Institut de Chimie des Substances Naturelles, UPR2301, Centre National de la Recherche Scientifique, Université Paris Saclay, 91190 Gif-sur-Yvette and.
authors.forename: Nadine
authors.initials: N
authors.lastname: Assrir
authors.affiliation: From the Institut de Chimie des Substances Naturelles, UPR2301, Centre National de la Recherche Scientifique, Université Paris Saclay, 91190 Gif-sur-Yvette and.
authors.forename: Ewen
authors.initials: E
authors.lastname: Lescop
authors.affiliation: From the Institut de Chimie des Substances Naturelles, UPR2301, Centre National de la Recherche Scientifique, Université Paris Saclay, 91190 Gif-sur-Yvette and.
authors.forename: François
authors.initials: F
authors.lastname: Bontems
authors.affiliation: the Unité de Virologie et Immunologie Moléculaires, UR892, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France.
authors.forename: Jean-François
authors.initials: JF
authors.lastname: Eléouët
authors.affiliation: From the Institut de Chimie des Substances Naturelles, UPR2301, Centre National de la Recherche Scientifique, Université Paris Saclay, 91190 Gif-sur-Yvette and christina.sizun@cnrs.fr.
authors.forename: Christina
authors.identifier: 0000-0002-5760-2614
authors.initials: C
authors.lastname: Sizun
mesh_terms: D000595:Amino Acid Sequence; D004578:Electron Spin Resonance Spectroscopy; D064267:Intrinsically Disordered Proteins / Q000737:chemistry / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D018113:Respiratory Syncytial Virus, Human / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid
chemical_list: D064267:Intrinsically Disordered Proteins; D010750:Phosphoproteins
keywords: RNA dependent RNA polymerase; intrinsically disordered protein; molecular recognition element; nuclear magnetic resonance (NMR); nucleoprotein; phosphoprotein; protein dynamic; respiratory syncytial virus; viral replication; viral transcription