Optimal conditions and specificity of interaction of a distinct class of nonhistone chromosomal proteins with DNA.
A subclass of nonhistone chromatin proteins with high DNA affinity has been isolated from rat liver. The interaction of the isolated proteins with DNA in vitro was characterized utilizing a nitrocellulose filter binding technique. The temperature, time, concentration, ionic strength, and pH dependence were characterized. Optimal interaction was observed at 0.19 M naCl, pH 7.5 with a protein to DNA ratio of 13 (w/w). Equilibrium and kinetic competition experiments indicated that these proteins interact optimally with A-T rich and single-stranded DNA. The data also suggest that these proteins might affect the helixcoil transiton of DNA.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002414:Cations, Monovalent; D002875:Chromosomes / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D003852:Deoxyribonucleoproteins; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000378:metabolism; D046911:Macromolecular Substances; D009698:Nucleoproteins / Q000378:metabolism; D009994:Osmolar Concentration; D011485:Protein Binding; D051381:Rats; D013696:Temperature
D002414:Cations, Monovalent; D003852:Deoxyribonucleoproteins; D046911:Macromolecular Substances; D009698:Nucleoproteins; D004247:DNA