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Nucleic Acids Research, 1983, Vol. 11, No. 2 461-472
© 1983

MOLECULAR BIOLOGY

Association of eukaryotic DNA topoisomerase I with nucleosomes and chromosomal proteins

Kashayar Javaherian and Leroy F. Liu

Department of Physiological Chemistry, Johns Hopkins Medical School Baltimore, MD 21205 USA

Received August 10, 1982. Revised December 8, 1982. Accepted December 8, 1982.

A DNA topoisomerase activity is found to be associated with the nucleosomes released by the Staphylococcal nuclease digestion of HeLa nuclei. Such an association is found to be salt dependent. A number of criteria have established that this DNA topoisomerase activity is due to HeLa topo I(Liu,L. F. and Miller, K. G.(1980) Proc. Natl. Acad. Sci. USA 78, 3489-3491). A similar association has been demonstrated from the in vitro studies using purified mononucleosomes and eukaryotic DNA topoisomerase 1. Nonhistone HMG proteins and histone H1 are found to stimulate topoisomerase activity in vitro and form tight complexes with eukaryotic DNA topoisomerase I. The intimate interactions of topoisomerase I with chromosomal proteins and nucleosomes may be an essential feature of the topoisomerase function in vivo.


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