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

被引：323

作者：

Nielsen, AL

Oulad-Abdelghani, M

Ortiz, JA

Remboutsika, E

Chambon, P

Losson, R

机构：

[1] Coll France, ULP, CNRS,INSERM, Inst Genet & Biol Mol & Cellulaire, F-67404 Illkirch, France

[2] Aarhus Univ, Inst Human Genet, DK-8000 Aarhus C, Denmark

[3] Aarhus Univ, Dept Biol Mol & Struct, DK-8000 Aarhus C, Denmark

[4] Natl Inst Med Res, London NW7 1AA, England

来源：

MOLECULAR CELL | 2001年 / 7卷 / 04期

关键词：

D O I：

10.1016/S1097-2765(01)00218-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Members of the heterochromatin protein 1 (HP1) family are silencing nonhistone proteins. Here, we show that in P-19 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, HP1 alpha interacts with the linker histone H1. HP1 alpha binds to H3 and H1 through its chromodomain (CD) and hinge region, respectively. Interestingly, the Polycomb (Pc1/M33) CD also interacts with H3, and HP1 alpha 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.

引用

页码：729 / 739

页数：11

共 45 条

[1] Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31 [J].