Histones bind more tightly to bromodeoxyuridine-substituted DNA than to normal DNA.
Using a membrane filter assay, we have obtained results from both kinetic and competition experiments indicating that histones bind more strongly to bromodeoxyuridine-substituted DNA than to normal DNA. At 37 degrees C in our standard buffer of 0.2 M ionic strength, the rate of dissociation of histones H1, H2, and h4 from BrdU-substituted DNA is respectively 7, 4, and 2 times slower than it is from normal DNA. Competition experiments show an even greater difference between BrdU-substituted and normal DNA with respect to histone binding. The tighter binding of histones to BrdU-substituted DNA is of interest because of the known effects of BrdU on eukaryotic chromosome condensation and staining, virus induction, and the inhibition of differentiation.
D001665:Binding Sites; D001973:Bromodeoxyuridine; D004247:DNA; D004279:DNA, Viral; D005374:Filtration; D006657:Histones; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D010944:Plants; D011485:Protein Binding
D004279:DNA, Viral; D006657:Histones; D004247:DNA; D001973:Bromodeoxyuridine