Analysis of the human HP1 interactome reveals novel binding partners

Claire Rosnoblet, Julien Vandamme, Pamela Voelkel, Pierre-Olivier Angrand

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

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. (C) 2011 Elsevier Inc. All rights reserved.
Original languageEnglish
JournalJournal of Hazardous Materials
Volume413
Issue number2
Pages (from-to)206-211
Number of pages6
ISSN0304-3894
DOIs
Publication statusPublished - 2011
Externally publishedYes

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