Histone-like protein in the Archaebacterium Sulfolobus acidocaldarius.
The Archaebacterium Thermoplasma acidophilum contains a basic chromosomal protein remarkably similar to the histones of eukaryotes. Therefore, it was of interest to examine a different Archaebacterium for similar proteins. We chose to examine Sulfolobus acidocaldarius because it is thermophilic, like T. acidophilum, but nevertheless the two organisms are not particularly closely related. Two major chromosomal proteins were found in S. acidocaldarius. The smaller of these was soluble in 0.2 M H2SO4 and had a molecular weight of 14500. The larger was acid-insoluble and had a molecular weight of about 36000. Together, the proteins protected about 5% of the DNA against nuclease digestion and stabilized about 50% against thermal denaturation. Overall, the properties of these proteins were intermediate between those of the Escherichia coli protein HU and T. acidophilum protein HTa.
D000596:Amino Acids / Q000032:analysis; D001105:Archaea / Q000032:analysis*; D001419:Bacteria / Q000032:analysis*; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002499:Centrifugation, Density Gradient; D004268:DNA-Binding Proteins / Q000302:isolation & purification*; D003852:Deoxyribonucleoproteins / Q000302:isolation & purification; D006657:Histones / Q000302:isolation & purification*; D008836:Micrococcal Nuclease; D008970:Molecular Weight; D009691:Nucleic Acid Denaturation
D000596:Amino Acids; D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D003852:Deoxyribonucleoproteins; D006657:Histones; D008836:Micrococcal Nuclease