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Journal Articles Molecular Cell Year : 2001

Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins

Abstract

Members of the heterochromatin protein 1 (HP1) family are silencing nonhistone proteins. Here, we show that in P19 embryonal carcinoma (EC) nuclei, HP1 alpha, beta, and gamma form homo- and heteromers associated with nucleosomal core histones. In vitro, all three HP1s bind to tailed and tailless nucleosomes and specifically interact with the histone-fold of histone H3. Furthermore, HP1alpha interacts with the linker histone H1. HP1alpha binds to H3 and H1 through its chromodomain (CD) and hinge region, respectively. Interestingly, the Polycomb (Pc1/M33) CD also interacts with H3, and HP1alpha and Pc1/M33 binding to H3 is severely impaired by CD mutations known to abrogate HP1 and Polycomb silencing in Drosophila. These results define a novel function for the conserved CD and suggest that HP1 self-association and histone binding may play a crucial role in HP1-mediated heterochromatin assembly.

Dates and versions

hal-04093240 , version 1 (09-05-2023)

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Anders Lade Nielsen, Mustapha Oulad-Abdelghani, José A Ortiz, Aumorphia Remboutsika, Pierre Chambon, et al.. Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. Molecular Cell, 2001, 7 (4), pp.729-739. ⟨10.1016/s1097-2765(01)00218-0⟩. ⟨hal-04093240⟩
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