J. Biol. Chem., Vol. 255, Issue 15, 7059-7062, Aug, 1980
Conformational changes in the H3 . H4 histone complex. Serological and circular dichroism studies
L Feldman, NV Beaudette, BD Stollar and GD Fasman
The H3.H4 complex has been extracted from calf thymus chromatin in either
0.05 M NaOAc, pH 5.0, or in 2.0 M KCl, 0.1 M KPO4, pH 6.7, and both forms
have been shown to consist solely of histones H3 and H4 when examined on
sodium dodecyl sulfate-polyacrylamide gels. Serological and circular
dichroism analyses indicate the existence of structural differences between
the two forms. Dilution of the high salt form of the complex into low salt
produces a time-dependent conformational change which is related to
reduction in the alpha helix content of the complex and which exposes
antigenic sites on the complex. The existence of multiple forms of the
H3.H4 complex may be related to the dynamic equilibrium of nucleosome
structure in vivo.