Nucleosome-Interacting Proteins Regulated by DNA and Histone Methylation

被引：515

作者：

Bartke, Till ^{[1
,2
]}

Vermeulen, Michiel ^{[3
]}

Xhemalce, Blerta ^{[1
,2
]}

Robson, Samuel C. ^{[1
,2
]}

Mann, Matthias ^{[3
]}

Kouzarides, Tony ^{[1
,2
]}

机构：

[1] Gurdon Inst, Cambridge CB2 1QN, England

[2] Dept Pathol, Cambridge CB2 1QN, England

[3] Max Planck Inst Biochem, Dept Prote & Signal Transduct, D-82152 Martinsried, Germany

来源：

CELL | 2010年 / 143卷 / 03期

关键词：

CHROMATIN MODIFICATIONS; HETEROCHROMATIN; TRANSCRIPTION; BINDING; H3; ACETYLATION; RECOGNITION; COMPLEX; KDM2A; HP1;

D O I：

10.1016/j.cell.2010.10.012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Modifications on histones or on DNA recruit proteins that regulate chromatin function. Here, we use nucleosomes methylated on DNA and on histone H3 in an affinity assay, in conjunction with a SILAC-based proteomic analysis, to identify "crosstalk'' between these two distinct classes of modification. Our analysis reveals proteins whose binding to nucleosomes is regulated by methylation of CpGs, H3K4, H3K9, and H3K27 or a combination thereof. We identify the origin recognition complex (ORC), including LRWD1 as a subunit, to be a methylation-sensitive nucleosome interactor that is recruited cooperatively by DNA and histone methylation. Other interactors, such as the lysine demethylase Fbxl11/KDM2A, recognize nucleosomes methylated on histones, but their recruitment is disrupted by DNA methylation. These data establish SILAC nucleosome affinity purifications (SNAP) as a tool for studying the dynamics between different chromatin modifications and provide a modification binding "profile'' for proteins regulated by DNA and histone methylation.

引用

页码：470 / 484

页数：15

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