Histone-like protein in the prokaryote Thermoplasma acidophilum.
The DNA of the prokaryote Thermoplasma acidophilum is associated with a histone-like protein that has the following properties: it has a high content (23%) of basic amino acids, is positively charged at neutral pH, is soluble in acid, and can stabilize DNA against thermal denaturation. In polyacrylamide gel electrophoresis, in the presence of either sodium dodecylsulfate or urea, it migrates at the same rate as histone IV (F2a1) of calf thymus. The amino acid composition, however, it unusually rich in the amides of acidic amino acids (16-20%), and it does not appear to be closely homologous to any of the classes of eukaryotic histones. Escherichia coli DNA, on the other hand, was associated with no detectable acid-soluble proteins, and the nucleoprotein thermally denatured at a lower temperature than pure DNA.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001426:Bacterial Proteins / Q000032:analysis; D002417:Cattle; D002850:Chromatography, Gel; D004247:DNA; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000032:analysis / Q000302:isolation & purification; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances; D009174:Mycoplasma / Q000032:analysis*; D009691:Nucleic Acid Denaturation; D011485:Protein Binding; D013045:Species Specificity; D013950:Thymus Gland
D000596:Amino Acids; D001426:Bacterial Proteins; D006657:Histones; D046911:Macromolecular Substances; D004247:DNA