Pea Histones H2A and H2B: Variable and Conserved Regions in the Sequences

Abstract

Pea histone II group, a mixture of H2A and H2B obtained by chromatography on an ion-exchange resin, was further fractionated by carboxymethylcellulose chromatography and purified by Bio-Gel P-60 chromatography. Their chromatographic behaviors and gel electro phoretic mobilities of single bands differed significantly from those of calf H2A and H2B. Their amino acid compositions were similar to those of the calf histones as a whole, but differed in detail in certain respects. The partial sequence of pea H2B was deduced from the amino acid compositions of BrCN cleavage fragments and tryptic peptides in comparison with the known sequence of calf H2B. It is different in the amino-terminal basic region from the calf H2B, with a blocked amino terminaland a larger number of residues. In contrast, the middle and carboxy-terminal hydrophobic regions are relatively similar, with at least 19-21 different residues and microhrterogeneity at two positions of the pea sequence. The sequence of H2A may vary in much the same way as that of H2B, as suggested by the similar extent of differences in their amino acid compositions. It is thus assumed that the amino-terminal regions, at least, of H2A and H2B histones are variable in evolution provided that they remain basic enough to bind DNA, whereas the middle and carboxy-terminal hydrophobic regions of H2A, H2B, H3, and H4 should be conserved to ensure precise histone core formation inside the repeated units of chromatin.