| Abstract: | The nucleotide sequence selectivity of histone binding has been measured by thermal denaturation of reconstituted nucleoproteins. When DNAs of different average base compositions competed for the binding of purified histone fractions during in vitro reconstitutions in the presence of salt and urea, a decreasing (A + T)-binding preference was observed following the order H1 greater than H2B greater than H5 greater than H2A greater than H2A + H2B] greater than H2A + H2B + H3 + H4], H1 + (H2A + H2B + H3 + H4)2]. Nucleoprotein complexes formed under conditions shown to yield more physiologically comparable nucleosome structures revealed a minimal (A + T)-binding preference. These results suggest that homotypic and heterotypic histone interactions decreased the nucleotide sequence selectivity of nucleosome binding. |
