Abstract
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. Copyright © 1983, Wiley Blackwell. All rights reserved
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CITATION STYLE
BODE, J., GÓMEZ‐LIRA, M. M., & SCHRÖTER, H. (1983). Nucleosomal Particles Open as the Histone Core Becomes Hyperacetylated. European Journal of Biochemistry, 130(3), 437–445. https://doi.org/10.1111/j.1432-1033.1983.tb07170.x
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