Skip to Main content Skip to Navigation
Journal articles

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.
Document type :
Journal articles
Complete list of metadata

https://hal.archives-ouvertes.fr/hal-01461939
Contributor : Catherine Drouet <>
Submitted on : Wednesday, February 8, 2017 - 2:54:53 PM
Last modification on : Thursday, July 8, 2021 - 3:51:07 AM

Identifiers

Citation

Camille Samson, Isaline Herrada, Florian Celli, François-Xavier Theillet, Sophie Zinn-Justin. 1H, 13C and 15N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin.. Biomolecular NMR Assignments, Springer, 2016, pp.179-82. ⟨10.1007/s12104-015-9662-7⟩. ⟨hal-01461939⟩

Share

Metrics

Record views

293