Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion

Amassments of heterochromatin in somatic cells occur in close contact with the nuclear envelope (NE) but are gapped by channel- and cone-like zones that appear largely free of heterochromatin and associated with the nuclear pore complexes (NPCs). To identify proteins involved in forming such heteroc...

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Hauptverfasser: Krull, Sandra (VerfasserIn) , Dörries, Julia (VerfasserIn) , Boysen, Björn (VerfasserIn) , Reidenbach, Sonja (VerfasserIn) , Magnius, Lars (VerfasserIn) , Norder, Helene (VerfasserIn) , Thyberg, Johan (VerfasserIn) , Cordes, Volker (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 20 April 2010
In: The EMBO journal
Year: 2010, Jahrgang: 29, Heft: 10, Pages: 1659-1673
ISSN:1460-2075
DOI:10.1038/emboj.2010.54
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/emboj.2010.54
Verlag, lizenzpflichtig, Volltext: https://www.embopress.org/doi/full/10.1038/emboj.2010.54
Volltext
Verfasserangaben:Sandra Krull, Julia Dörries, Björn Boysen, Sonja Reidenbach, Lars Magnius, Helene Norder, Johan Thyberg and Volker C Cordes

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520 |a Amassments of heterochromatin in somatic cells occur in close contact with the nuclear envelope (NE) but are gapped by channel- and cone-like zones that appear largely free of heterochromatin and associated with the nuclear pore complexes (NPCs). To identify proteins involved in forming such heterochromatin exclusion zones (HEZs), we used a cell culture model in which chromatin condensation induced by poliovirus (PV) infection revealed HEZs resembling those in normal tissue cells. HEZ occurrence depended on the NPC-associated protein Tpr and its large coiled coil-forming domain. RNAi-mediated loss of Tpr allowed condensing chromatin to occur all along the NE's nuclear surface, resulting in HEZs no longer being established and NPCs covered by heterochromatin. These results assign a central function to Tpr as a determinant of perinuclear organization, with a direct role in forming a morphologically distinct nuclear sub-compartment and delimiting heterochromatin distribution. 
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