Analysis of the human HP1 interactome reveals novel binding partners

Claire Rosnoblet; Julien Vandamme; Pamela Völkel; Pierre-Olivier Angrand

doi:10.1016/j.bbrc.2011.08.059

Analysis of the human HP1 interactome reveals novel binding partners

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

25 Citations (Scopus)

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.

Original language	English
Journal	Biochemical and Biophysical Research Communications
Volume	413
Issue number	2
Pages (from-to)	206-11
Number of pages	6
ISSN	0006-291X
DOIs	https://doi.org/10.1016/j.bbrc.2011.08.059
Publication status	Published - 23 Sept 2011

Keywords

Amino Acid Sequence
Chromosomal Proteins, Non-Histone
HeLa Cells
Humans
Molecular Sequence Data
Protein Binding

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10.1016/j.bbrc.2011.08.059

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title = "Analysis of the human HP1 interactome reveals novel binding partners",

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.",

keywords = "Amino Acid Sequence, Chromosomal Proteins, Non-Histone, HeLa Cells, Humans, Molecular Sequence Data, Protein Binding",

author = "Claire Rosnoblet and Julien Vandamme and Pamela V{\"o}lkel and Pierre-Olivier Angrand",

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TY - JOUR

T1 - Analysis of the human HP1 interactome reveals novel binding partners

AU - Rosnoblet, Claire

AU - Vandamme, Julien

AU - Völkel, Pamela

AU - Angrand, Pierre-Olivier

PY - 2011/9/23

Y1 - 2011/9/23

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Chromosomal Proteins, Non-Histone

KW - HeLa Cells

KW - Humans

KW - Molecular Sequence Data

KW - Protein Binding

U2 - 10.1016/j.bbrc.2011.08.059

DO - 10.1016/j.bbrc.2011.08.059

M3 - Journal article

C2 - 21888893

SN - 0006-291X

VL - 413

SP - 206

EP - 211

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Analysis of the human HP1 interactome reveals novel binding partners

Abstract

Keywords

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