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Biophys Chem. 1992 Jun;43(2):197-211.

Solution studies of the interactions between the histone core proteins and DNA using fluorescence spectroscopy.

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University of Wisconsin, School of Pharmacy, Madison 53706.

Erratum in

  • Biophys Chem 1993 May;46(3):295-6.


The equilibrium interactions between histone H2A-H2B and H3/H4 subunits with 200 base pair chicken erythrocyte DNA have been studied by monitoring the fluorescence polarization of a long-lived fluorescence probe covalently bound to the histone subunits. These studies have brought to light the formation of highly asymmetric complexes exhibiting very high histone/DNA stoichiometries as well as very high apparent affinities. The stoichiometries observed for these non-nucleosome complexes depended both upon the concentration of the histones and the concentration of the DNA 200mer. The observed stoichiometries varied approximately between 4 and 16 histone octamers/DNA 200mer and the affinities were in the nanomolar range. These results are discussed in terms of their in vitro as well as their possible in vivo significance.

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