1H, 13C and 15N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin

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• 作者：Camille Samson ; Isaline Herrada ; Florian Celli…
• 关键词：Nuclear envelope ; Emerin ; Intrinsically disordered protein ; Urea ; NMR spectroscopy ; Muscular dystrophy
• 刊名：Biomolecular NMR Assignments
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：10
• 期：1
• 页码：179-182
• 全文大小：780 KB
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• 作者单位：Camille Samson (1)
  Isaline Herrada (1)
  Florian Celli (1)
  Francois-Xavier Theillet (1) (2)
  Sophie Zinn-Justin (1)
  
  1. 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
  2. Department of NMR-assisted Structural Biology, Leibniz-Institut für Molekular Pharmakologie (FMP), 13125, Berlin, Germany
  
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

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 1H, 15N, 13CO, 13Cα and 13Cβ 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.