Nucleosomal particles open as the histone core becomes hyperacetylated.
Lymphoblastoid cells grown in the presence of the deacetylase inhibitor butyrate were used to isolate nucleosomal particles in a hyperacetylated state. During a non-denaturing gel electrophoresis these particles revealed a heterogeneity which is only in part due to the presence of nonhistone proteins. Monomers that are free from histone H1 and high-mobility-group (HMG) proteins 14 and 17 yield a subfractionation according to the degree of core histone acetylation beyond a limiting value of 10 acetyl groups/particle. It is shown that hyperacetylation provides particles with low mobilities and a considerable conformational freedom in contrast to HMG protein 14 which locks them in a conformation that has a similar electrophoretic behaviour but is more defined.
D000107:Acetylation; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006609:High Mobility Group Proteins; D006657:Histones / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D009707:Nucleosomes / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D011487:Protein Conformation
D002868:Chromosomal Proteins, Non-Histone; D006609:High Mobility Group Proteins; D006657:Histones; D009707:Nucleosomes