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Nucleic Acids Research, 1983, Vol. 11, No. 12 4065-4075
© 1983

MOLECULAR BIOLOGY

Histone hyperacetylation has little effect on the higher order folding of chromatin

James D. McGhee1,+, Joanne M. Nickol1, Gary Felsenfeld1 and Donald C. Rau2

1Laboratory of Molecular Biology National Institute of Arthritis, Diabetes and Digestive and Kidney Diseases, National Institutes of Health , Bethesda, MD 20205, USA 2laboratory of Chemical Physics, National Institute of Arthritis, Diabetes and Digestive and Kidney Diseases, National Institutes of Health Bethesda, MD 20205, USA

Received March 17, 1983. Revised May 25, 1983. Accepted May 25, 1983.

HeLa cells were grown in the presence of 10 mM sodium butyrate and soluble chromatin containing hyperacetylated histones was prepared by mild micrococcal nuclease digestion and sucrose gradient fractionation. Sedimentation and electric dichroism were used to study the cation-induced folding of this acetylated chromatin from the 10 nm filament to the 30 nm solenoid conformation. Although under some conditions acetylated chromatin appears slightly less condensed than control chromatin, the major conclusion is that hyperacetylation of histones does not in itself prevent the formation of the higher order chromatin solenoid.

+Present address: Department of Medical Biochemistry, Faculty of Medicine, University of Calgary, Calgary, Alberta, Canada T2N 1N4.


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