Primary Structure of Histone H2A from Gonad of the Sea Urchin Psammechinus miliaris

Abstract

The complete amino acid sequence (125 residues) of sea urchin [P. miliaris] histone H2A was established by structural studies of peptides derived from tryptic and chymotryptic cleavage of the maleylated protein and from thermolysin cleavage of the intact protein. By comparison with calf homologous histone, the basic amino-terminal and carboxy-terminal parts of the protein show 11 substitutions and 4 deletions. The remainder of the sequence, mostly hydrophobic, is almost completely unchanged.