title: The nuclear matrix and the regulation of chromatin organization and function.
abstract: Nuclear DNA is organized into loop domains, with the base of the loop being bound to the nuclear matrix. Loops with transcriptionally active and/or potentially active genes have a DNase I-sensitive chromatin structure, while repressed chromatin loops have a condensed configuration that is essentially invisible to the transcription machinery. Core histone acetylation and torsional stress appear to be responsible for the generation and/or maintenance of the open potentially active chromatin loops. The transcriptionally active region of the loop makes several dynamic attachments with the nuclear matrix and is associated with core histones that are dynamically acetylated. Histone acetyltransferase and deacetylase, which catalyze this rapid acetylation and deacetylation, are bound to the nuclear matrix. Several transcription factors are components of the nuclear matrix. Histone acetyltransferase, deacetylase, and transcription factors may contribute to the dynamic attachment of the active chromatin domains with the nuclear matrix at sites of ongoing transcription.
authors.affiliation: Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of Manitoba, Winnipeg, Canada.
authors.forename: J R
authors.initials: JR
authors.lastname: Davie
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000502:physiology* / Q000648:ultrastructure*; D006609:High Mobility Group Proteins / Q000502:physiology; D006657:Histones / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D015530:Nuclear Matrix / Q000502:physiology* / Q000648:ultrastructure*; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship
chemical_list: D002843:Chromatin; D006609:High Mobility Group Proteins; D006657:Histones