title: NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities.
abstract: ATP-dependent chromatin-remodeling complexes are known to facilitate transcriptional activation by opening chromatin structures. We report a novel human complex, named NURD, which contains not only ATP-dependent nucleosome disruption activity, but also histone deacetylase activity, which usually associates with transcriptional repression. The deacetylation is stimulated by ATP on nucleosomal templates, suggesting that nucleosome disruption aids the deacetylase to access its substrates. One subunit of NURD was identified as MTA1, a metastasis-associated protein with a region similar to the nuclear receptor core-pressor, N-CoR; and antibodies against NURD partially relieve transcriptional repression by thyroid hormone receptor. These results suggest that ATP-dependent chromatin remodeling can participate in transcriptional repression by assisting repressors in gaining access to chromatin.
authors.affiliation: Laboratory of Genetics, National Institute on Aging, National Institute of Health, Gerontology Research Center, Baltimore, Maryland 21224, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Xue
authors.forename: J
authors.initials: J
authors.lastname: Wong
authors.forename: G T
authors.initials: GT
authors.lastname: Moreno
authors.forename: M K
authors.initials: MK
authors.lastname: Young
authors.forename: J
authors.initials: J
authors.lastname: Côté
authors.forename: W
authors.initials: W
authors.lastname: Wang
mesh_terms: D000251:Adenosine Triphosphatases / Q000276:immunology / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000502:physiology*; D000595:Amino Acid Sequence; D000906:Antibodies / Q000276:immunology / Q000494:pharmacology; D001324:Autoantigens; D002843:Chromatin / Q000235:genetics / Q000378:metabolism*; D004265:DNA Helicases / Q000276:immunology / Q000378:metabolism; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006655:Histone Deacetylases / Q000276:immunology / Q000378:metabolism*; D006657:Histones / Q000378:metabolism; D006801:Humans; D019169:Jurkat Cells; D046911:Macromolecular Substances; D056245:Mi-2 Nucleosome Remodeling and Deacetylase Complex; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000235:genetics / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D011988:Receptors, Thyroid Hormone / Q000235:genetics / Q000502:physiology; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D015534:Trans-Activators; D014157:Transcription Factors / Q000378:metabolism; D014158:Transcription, Genetic / Q000187:drug effects / Q000235:genetics; D014407:Tumor Cells, Cultured
chemical_list: D000906:Antibodies; D001324:Autoantigens; C115323:CHD4 protein, human; D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; C089320:MTA1 protein, human; D009707:Nucleosomes; D011506:Proteins; D011988:Receptors, Thyroid Hormone; D012097:Repressor Proteins; C071731:SIN3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D015534:Trans-Activators; D014157:Transcription Factors; D000255:Adenosine Triphosphate; D006655:Histone Deacetylases; D056245:Mi-2 Nucleosome Remodeling and Deacetylase Complex; D000251:Adenosine Triphosphatases; D004265:DNA Helicases