Presence of histones in Aspergillus nidulans.
Five major histone proteins have been extracted from chromatin isolated from purified nuclei of the fungus, Aspergillus nidulans. These proteins had chromatographic properties which were similar to reference calf thymus histones and were purified to electrophoretic homegeneity by gel chromatography of Bio-Gel P10, Bio-Gel P60, and Sephadex G-100. Electrophoresis of these proteins in three different systems (urea-starch, urea-acetic acid polyacrylamide, and discontinuous SDS polyacrylamide) showed that the A. nidulans histones H3 and H4 were nearly identical to calf thymus H3 and H4 with respect to net charge and molecular weight criteria, whereas the fungal histones H1, H2a and H2b were similar but not identical to the corresponding calf thymus histones. Amino acid analysis of A. nidulans histones H2a, H2b, and H4 showed them to be closely related to the homologous calf thymus histones. The mobility patterns of A. nidulans ribosomal basic proteins in three different electrophoretic systems were distinctly different from those of the fungal histones.
D000596:Amino Acids / Q000032:analysis; D001233:Aspergillus nidulans / Q000032:analysis*; D002843:Chromatin / Q000032:analysis; D002850:Chromatography, Gel; D004586:Electrophoresis; D005656:Fungal Proteins / Q000032:analysis / Q000302:isolation & purification*; D006657:Histones / Q000032:analysis / Q000302:isolation & purification*; D008970:Molecular Weight; D012269:Ribosomal Proteins / Q000032:analysis
D000596:Amino Acids; D002843:Chromatin; D005656:Fungal Proteins; D006657:Histones; D012269:Ribosomal Proteins