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Vol. 13, No. 15, pp. 1924-1935, August 1, 1999
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; 2 Institute of Cell and
Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, UK;
3 Molecular Biology Program, Memorial Sloan Kettering Cancer
Center, New York, New York 10021 USA
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.
[Key Words: DNA methylation; histone deacetylase complex; nucleosome remodeling; gene silencing]
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