H2a.z Stabilizes Chromatin in a Way That is Dependent on Core Histone Acetylation.
From: Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada.
The Journal of biological chemistry
- Publish Date: Jul 2006
- ISSN: 0021-9258
- Volume: 281
- Issue: 29
- Pages: 20036-44
- Medium: Print
- Language: English
- Citation (JAMA): Thambirajah Anita A, Dryhurst Deanna, Ishibashi Toyotaka, et al. H2a.z Stabilizes Chromatin in a Way That is Dependent on Core Histone Acetylation.. J. Biol. Chem. Jul 2006;281:20036-44
Abstract
The functional and structural chromatin roles of H2A.Z are still controversial. This work represents a further attempt to resolve the current functional and structural dichotomy by characterizing chromatin structures containing native H2A.Z. We have analyzed the role of this variant in mediating the stability of the histone octamer in solution using gel-filtration chromatography at different pH. It was found that decreasing the pH from neutral to acidic conditions destabilized the histone complex. Furthermore, it was shown that the H2A.Z-H2B dimer had a reduced stability. Sedimentation velocity analysis of nucleosome core particles (NCPs) reconstituted from native H2A.Z-containing octamers indicated that these particles exhibit a very similar behavior to that of native NCPs consisting of canonical H2A. Sucrose gradient fractionation of native NCPs under different ionic strengths indicated that H2A.Z had a subtle tendency to fractionate with more stabilized populations. An extensive analysis of the salt-dependent dissociation of histones from hydroxyapatite-adsorbed chromatin revealed that, whereas H2A.Z co-elutes with H3-H4, hyperacetylation of histones (by treatment of chicken MSB cells with sodium butyrate) resulted in a significant fraction of this variant eluting with the canonical H2A. These studies also showed that the late elution of this variant (correlated to enhanced binding stability) was independent of the chromatin size and of the presence or absence of linker histones.
Mesh Headings (Keywords): Acetylation, Animals, Chickens, Chromatin, Circular Dichroism, Dimerization, Erythrocytes, Histones, Hydrogen-Ion Concentration, Mardivirus, Nucleosomes
Check for Full Text / PubMed Unique Identifier (PMID): 16707487
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.