H5 Histone and DNA-relaxing enzyme of chicken erythrocytes. Interaction with superhelical DNA.
The interaction of closed circular duplex DNA with the lysine-rich H5 histone fraction of avian erythrocytes has been studied. H5, like H1 histone, interacts preferentially with superhelical DNA. The extent of interaction increases with increasing negative or positive superhelicity. Salt-extracted lysine-rich histones show the same specificity for interaction with superhelices as do acid-extracted preparations. Chicken erythrocyte nuclei contain DNA-relaxing enzyme. This enzyme is extracted from the nuclei at lower salt concentrations than those required to extract H1 and H5 histones and is, therefore, probably a function of a protein distinct from H1 and H5 histones.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D002645:Chickens; D004270:DNA, Circular / Q000378:metabolism; D004912:Erythrocytes / Q000201:enzymology*; D004996:Ethidium; D006657:Histones / Q000378:metabolism; D007700:Kinetics; D009690:Nucleic Acid Conformation; D009994:Osmolar Concentration; D011485:Protein Binding; D012965:Sodium Chloride / Q000494:pharmacology
D004270:DNA, Circular; D006657:Histones; D012965:Sodium Chloride; D004996:Ethidium