title: 1H, 13C and 15N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin.
abstract: Human emerin is an inner nuclear membrane protein involved in the response of the nucleus to mechanical stress. It contributes to the physical connection between the cytoskeleton and the nucleoskeleton. It is also involved in chromatin organization. Its N-terminal region is nucleoplasmic and comprises a globular LEM domain from residue 1 to residue 43. The three-dimensional structure of this LEM domain in complex with the chromatin BAF protein was solved from NMR data. Apart from the LEM domain, the nucleoplasmic region of emerin, from residue 44 to residue 221, is predicted to be intrinsically disordered. Mutations in this region impair binding to several emerin partners as lamin A, actin or HDAC3. However the molecular details of these recognition defects are unknown. Here we report (1)H, (15)N, (13)CO, (13)Cα and (13)Cβ NMR chemical shift assignments of the emerin fragment from residue 67 to residue 170, which is sufficient for nuclear localization and involved in lamin A binding. Chemical shift analysis confirms that this fragment is intrinsically disordered in 0 and 8 M urea.
authors.affiliation: Laboratoire de Biologie Structurale et Radiobiologie, Institute for Integrative Biology of the Cell (I2BC), CNRS, Univ. Paris South and IBITECS CEA, CEA Saclay Bât. 144, 91191, Gif-sur-Yvette Cedex, France.
authors.forename: Camille
authors.initials: C
authors.lastname: Samson
authors.affiliation: Laboratoire de Biologie Structurale et Radiobiologie, Institute for Integrative Biology of the Cell (I2BC), CNRS, Univ. Paris South and IBITECS CEA, CEA Saclay Bât. 144, 91191, Gif-sur-Yvette Cedex, France.
authors.forename: Isaline
authors.initials: I
authors.lastname: Herrada
authors.affiliation: Laboratoire de Biologie Structurale et Radiobiologie, Institute for Integrative Biology of the Cell (I2BC), CNRS, Univ. Paris South and IBITECS CEA, CEA Saclay Bât. 144, 91191, Gif-sur-Yvette Cedex, France.
authors.forename: Florian
authors.initials: F
authors.lastname: Celli
authors.affiliation: Laboratoire de Biologie Structurale et Radiobiologie, Institute for Integrative Biology of the Cell (I2BC), CNRS, Univ. Paris South and IBITECS CEA, CEA Saclay Bât. 144, 91191, Gif-sur-Yvette Cedex, France.|Department of NMR-assisted Structural Biology, Leibniz-Institut für Molekular Pharmakologie (FMP), 13125, Berlin, Germany.
authors.forename: Francois-Xavier
authors.initials: FX
authors.lastname: Theillet
authors.affiliation: Laboratoire de Biologie Structurale et Radiobiologie, Institute for Integrative Biology of the Cell (I2BC), CNRS, Univ. Paris South and IBITECS CEA, CEA Saclay Bât. 144, 91191, Gif-sur-Yvette Cedex, France. sophie.zinn@cea.fr.
authors.forename: Sophie
authors.identifier: http://orcid.org/0000-0002-7680-1088
authors.initials: S
authors.lastname: Zinn-Justin
mesh_terms: D004305:Dose-Response Relationship, Drug; D006801:Humans; D034904:Lamin Type A / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D014508:Urea / Q000494:pharmacology
chemical_list: D034904:Lamin Type A; D008565:Membrane Proteins; D009687:Nuclear Proteins; C092710:emerin; D014508:Urea
keywords: Emerin; Intrinsically disordered protein; Muscular dystrophy; NMR spectroscopy; Nuclear envelope; Urea