Studies on the noncooperative binding of the Escherichia coli DNA unwinding protein to single-stranded nucleic acids.
The noncooperative binding of the Escherichia coli DNA unwinding protein to single-stranded DNA oligomers has been studied by means of equilibrium dialysis. Dialyses were performed under a number of solution and temperature conditions using oligomers of varying length and base compositions. The results of these studies, which include a Scatchard analysis of the binding, have allowed us to propose a model for the cooperative binding of the protein to single-stranded DNA. The results of experiments dealing with the interaction of the protein with single-stranded RNA are also presented.
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D002417:Cattle; D004247:DNA; D004277:DNA, Single-Stranded / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009838:Oligodeoxyribonucleotides; D009994:Osmolar Concentration; D011485:Protein Binding; D012313:RNA / Q000378:metabolism; D013095:Spermidine; D013816:Thermodynamics; D013950:Thymus Gland
D001426:Bacterial Proteins; D004277:DNA, Single-Stranded; D009838:Oligodeoxyribonucleotides; D012313:RNA; D004247:DNA; D013095:Spermidine