title: Identification of a nuclear domain with deacetylase activity.
abstract: Here, we describe the identification and characterization of a nuclear body (matrix-associated deacetylase body) whose formation and integrity depend on deacetylase activity. Typically, there are 20-40 0.5-microM bodies per nucleus, although the size and number can vary substantially. The structure appears to contain both class I and the recently described class II histone deacetylases (HDAC)5 and 7 along with the nuclear receptor corepressors SMRT (silencing mediator for retinoid and thyroid receptor) and N-CoR (nuclear receptor corepressor). Addition of the deacetylase inhibitors trichostatin A and sodium butyrate completely disrupt these nuclear bodies, providing a demonstration that the integrity of a nuclear body is enzyme dependent. We demonstrate that HDAC5 and 7 can associate with at least 12 distinct proteins, including several members of the NuRD and Sin3A repression complexes, and appear to define a new but related complex.
authors.affiliation: Howard Hughes Medical Institute, Gene Expression Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
authors.forename: M
authors.initials: M
authors.lastname: Downes
authors.forename: P
authors.initials: P
authors.lastname: Ordentlich
authors.forename: H Y
authors.initials: HY
authors.lastname: Kao
authors.forename: J G
authors.initials: JG
authors.lastname: Alvarez
authors.forename: R M
authors.initials: RM
authors.lastname: Evans
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000201:enzymology*; D000882:Haplorhini; D006655:Histone Deacetylases / Q000737:chemistry / Q000378:metabolism*; D008856:Microscopy, Fluorescence / Q000379:methods; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
chemical_list: D006655:Histone Deacetylases