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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. Nielsen, A.L., Oulad-Abdelghani, M., Ortiz, J.A., Remboutsika, E., Chambon, P., Losson, R. Mol. Cell (2001) [Pubmed]
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