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Nucleic Acids Research, 1991, Vol. 19, No. 21 5999-6006
© 1991

MOLECULAR BIOLOGY

ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract

Subhasis Banerjee, Gordon R. Benninon1, Martin W. Goldberg1 and Terry D. Allen1

Department of Pathology, The Royal Veterinary Colege Royal College Street, University of London, London NW1 0TU 1CRC Paterson Institute for Cancer Research Manchester M20 9BX, UK

Received June 19, 1991. Accepted September 25, 1991.

Physiologically spaced nucleosome formation in HeLa cell extracts is ATP dependent. ATP hydrolysis is required for chromatin assembly on both linear and covalently closed circular DNA. The link between the phosphorylation state of histones and nucleosome formation has been examined and we demonstrate that in the absence of histone phosphorylation no stable and regularly spaced nucleosomes are formed. Phosphorylated H3 stabilizes the nucleosome core; while phosphorylation of histone H2a is necessary to increase the linker length between nucleosomes from 0 to - 4 5 bp. Histone H1 alone, whether phosphorylated or unphosphorylated, does not increase the nucleosome repeat length in the absence of core histone phosphorylation. Phosphorylations of H1 and H3 correlate with condensation of chromatin. Maximum ATP hydrolysis which is necessary to increase the periodicity of nucleosomes from ~ 150 to ~ 185 bp, not only inhibits H1 and H3 phosphorylation but facilitates their dephosphorylation.


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