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.