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PMID: 10444591 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation.

Genes & development ·Vol. 13 ·No. 15 ·1999-08-01 ·Pages 1924-35

Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D

Abstract

ATP-dependent nucleosome remodeling and core histone acetylation and deacetylation represent mechanisms to alter nucleosome structure. NuRD is a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. The histone deacetylases HDAC1 and HDAC2 and the histone binding proteins RbAp48 and RbAp46 form a core complex shared between NuRD and Sin3-histone deacetylase complexes. The histone deacetylase activity of the core complex is severely compromised. A novel polypeptide highly related to the metastasis-associated protein 1, MTA2, and the methyl-CpG-binding domain-containing protein, MBD3, were found to be subunits of the NuRD complex. MTA2 modulates the enzymatic activity of the histone deacetylase core complex. MBD3 mediates the association of MTA2 with the core histone deacetylase complex. MBD3 does not directly bind methylated DNA but is highly related to MBD2, a polypeptide that binds to methylated DNA and has been reported to possess demethylase activity. MBD2 interacts with the NuRD complex and directs the complex to methylated DNA. NuRD may provide a means of gene silencing by DNA methylation.

MeSH Terms
Adenosine Triphosphatases Amino Acid Sequence Autoantigens/isolation & purification,metabolism Base Sequence Carrier Proteins/chemistry,genetics,isolation & purification,metabolism Cloning, Molecular DNA/chemistry,genetics,metabolism DNA Helicases DNA Methylation DNA-Binding Proteins/chemistry,genetics,isolation & purification,metabolism HeLa Cells Histone Deacetylase 1 Histone Deacetylase 2 Histone Deacetylases/chemistry,genetics,isolation & purification,metabolism Humans Mi-2 Nucleosome Remodeling and Deacetylase Complex Molecular Sequence Data Multienzyme Complexes/chemistry,genetics,isolation & purification,metabolism Nuclear Proteins/isolation & purification,metabolism Nucleosomes/chemistry,genetics,metabolism Protein Binding Recombinant Fusion Proteins/isolation & purification,metabolism Repressor Proteins Retinoblastoma-Binding Protein 4 Retinoblastoma-Binding Protein 7 Sequence Homology, Amino Acid Transcription Factors
Chemicals
Autoantigens CHD4 protein, human Carrier Proteins DNA-Binding Proteins MBD2 protein MBD3 protein, human Mbd3 protein, mouse Multienzyme Complexes Nuclear Proteins Nucleosomes RBBP4 protein, human RBBP7 protein, human Rbbp4 protein, mouse Recombinant Fusion Proteins Repressor Proteins Retinoblastoma-Binding Protein 4 Retinoblastoma-Binding Protein 7 Transcription Factors DNA MTA2 protein, human HDAC1 protein, human Hdac2 protein, mouse Histone Deacetylase 1 Histone Deacetylase 2 Histone Deacetylases Mi-2 Nucleosome Remodeling and Deacetylase Complex Adenosine Triphosphatases DNA Helicases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Zhang Y
Howard Hughes Medical Institute (HHMI), Division of Nucleic Acids Enzymology, Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
Ng H H
Erdjument-Bromage H
Tempst P
Bird A
Reinberg D
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Article Info
Journal
Genes & development
Abbr.
Genes Dev
ISSN
0890-9369
DOI
10.1101/gad.13.15.1924
Published
1999-08-01
Pages
1924-35
Language
English
Region
United States
NLM ID
8711660
PMCID
PMC316920
Subset
IM
Grants
Wellcome Trust · United Kingdom
NIGMS NIH HHS · F32 GM019515 · United States
NIGMS NIH HHS · GM-48518 · United States
NIGMS NIH HHS · 1F32GM19515-01 · United States
Databases
GENBANK
AF159259
External Links
PubMed source DOI: 10.1101/gad.13.15.1924 PMC Full Text View journal details
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