The core histones from the slime mold Physarum polycephalum. Isolation and characterization

Abstract

The histones of Physarum polycephalum have been isolated and fractionated using a combination of gel exclusion and ion-exchange chromatography or differential precipitation. The four core histones were unambiguously identified by gel electrophoresis, amino acid composition and N-terminal analysis. The molecular weight of Physarum histones H3, H2B and H4 are very close or identical to the corresponding histones from chicken erythrocytes. Physarum H2A is significantly larger than chicken erythrocyte H2A and its N-terminal residue is alanine. From the differences in amino acid compositions and in the peptide maps between Physarum and calf H4, one can expected some changes in the amino acid sequence of Physarum H4.