The kinetics of the interaction of a helix-destabilizing protein from roe-deer liver with DNA and the influence of phosphorylation.
The kinetics of the interaction of the DNA double-helix-destabilizing protein from roe-deer liver with different DNAs revealed a fast phase which is observed both by the increase in A260 of the DNA and the quenching of the protein intrinsic fluorescence. A slow phase with a smaller amplitude is only recorded by the increase of A260.--The protein contains slightly less than two phosphate groups per molecule, removal of one of which by alkaline phosphatase does not affect its activity; however, removal of both phosphates decreases the DNA-unwinding property significantly. A similar decrease in activity is also revealed upon incorporation of an additional phosphate by cAMP-dependent protein kinase I.--Results of the protection of poly[d(A--T)] from DNase I digestion by the protein are in favor of a migration of the protein along the DNA.
D000818:Animals; D002846:Chromatography, Affinity; D004247:DNA / Q000378:metabolism*; D004265:DNA Helicases / Q000302:isolation & purification / Q000378:metabolism*; D003670:Deer; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D010766:Phosphorylation; D011067:Poly dA-dT
D011067:Poly dA-dT; D004247:DNA; D004265:DNA Helicases