Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion
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Sandra Krull [2] ; Julia Dörries [1] ; Björn Boysen [3] ; Sonja Reidenbach [3] ; Lars Magnius [4] ; Helene Norder [4] ; Johan Thyberg [5] ; Volker C Cordes [2]
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[1] Max Planck Institute for Biophysical Chemistry
Max Planck Institute for Biophysical Chemistry
Landkreis Göttingen, Alemania
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[2] Max-Planck-Institut für Biophysikalische Chemie, Göttingen, Germany; Zentrum für Molekulare Biologie der Universität Heidelberg, Heidelberg, Germany
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[3] Zentrum für Molekulare Biologie der Universität Heidelberg, Heidelberg, Germany
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[4] Department of Virology, Swedish Institute for Infectious Disease Control, Solna, Sweden
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[5] Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden
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- Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 29, Nº. 10, 2010, págs. 1659-1673
- Idioma: inglés
- Enlaces
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Resumen
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.
