title: Effect of DNA length and H4 acetylation on the thermal stability of reconstituted nucleosome particles.
abstract: To examine the factors involved with nucleosome stability, we reconstituted nonacetylated particles containing various lengths (192, 162, and 152 base pairs) of DNA onto the Lytechinus variegatus nucleosome positioning sequence in the absence of linker histone. We characterized the particles and examined their thermal stability. DNA of less than chromatosome length (168 base pairs) produces particles with altered denaturation profiles, possibly caused by histone rearrangement in those core-like particles. We also examined the effects of tetra-acetylation of histone H4 on the thermal stability of reconstituted nucleosome particles. Tetra-acetylation of H4 reduces the nucleosome thermal stability by 0.8 degrees C as compared with nonacetylated particles. This difference is close to values published comparing bulk nonacetylated nucleosomes and core particles to ones enriched for core histone acetylation, suggesting that H4 acetylation has a dominant effect on nucleosome particle energetics.
authors.affiliation: Department of Microbiology, University of California, Davis, California 95616, USA. jssiino@ucdavis.edu
authors.forename: Joseph S
authors.initials: JS
authors.lastname: Siino
authors.forename: Peter M
authors.initials: PM
authors.lastname: Yau
authors.forename: Brian S
authors.initials: BS
authors.lastname: Imai
authors.forename: Joe M
authors.initials: JM
authors.lastname: Gatewood
authors.forename: E Morton
authors.initials: EM
authors.lastname: Bradbury
mesh_terms: D000107:Acetylation; D000818:Animals; D001483:Base Sequence; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D006367:HeLa Cells; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000378:metabolism*; D011489:Protein Denaturation; D013696:Temperature
chemical_list: D006657:Histones; D009707:Nucleosomes; D004247:DNA