Analysis of the human HP1 interactome reveals novel binding partners.

Chromatinomics, Interdisciplinary Research Institute, Universite de Lille Nord de France, Universite de Lille 1 Sciences et Technologies/CNRS USR 3078, 50 Avenue Halley, Parc Scientifique de Haute Borne, F-59658 Villeneuve d'Ascq Cedex, France.
Heterochromatin protein 1 (HP1) has first been described in Drosophila as an essential component of constitutive heterochromatin required for stable epigenetic gene silencing. Less is known about the three mammalian HP1 isotypes CBX1, CBX3 and CBX5. Here, we applied a tandem affinity purification approach coupled with tandem mass spectrometry methodologies in order to identify interacting partners of the mammalian HP1 isotypes. Our analysis identified with high confidence about 30-40 proteins co-eluted with CBX1 and CBX3, and around 10 with CBX5 including a number of novel HP1-binding partners. Our data also suggest that HP1 family members are mainly associated with a single partner or within small protein complexes composed of limited numbers of components. Finally, we showed that slight binding preferences might exist between HP1 family members.
Mesh Terms:
Amino Acid Sequence, Chromosomal Proteins, Non-Histone, HeLa Cells, Humans, Molecular Sequence Data, Protein Binding
Biochem. Biophys. Res. Commun. Sep. 23, 2011; 413(2);206-11 [PUBMED:21888893]
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