Histone Hl-DNA interaction. Influence of phosphorylation on the interaction of histone Hl with linear fragmented DNA.
By measuring the fluorescence polarization of fluorescent histone H1 derivatives complexed with DNA, binding of the histone to DNA was studied as a function of ionic strength in the solution prior to and after the H1 phosphorylation on Ser-37 residue. Fluorescent labels were covalently linked either specifically to Tyr-72 residues or unspecifically to lysine residues in the H1 polypeptide chain. The values of the corresponding rotational relaxation times showed that at low ionic strength all the segments of the H1 molecule were immobilized on binding to DNA. The gradual increasing NaC1 concentration in the solution of H1-DNA complex was accompanied at first by additional retardation of the histone mobility in the complex, and then by progressive release of histone H1 from from the complex which was completed at 0.5-0.6 M NaC1 irrespective of phosphorylation. tat the same time the phosphorylation of histone H1 led to removal of the central and, presumably, N-terminal regions of H1 from DNA.
D004247:DNA / Q000378:metabolism*; D003619:Dansyl Compounds; D006657:Histones / Q000378:metabolism*; D009994:Osmolar Concentration; D010085:Oxidative Phosphorylation; D006656:Protamine Kinase / Q000378:metabolism; D011485:Protein Binding; D012965:Sodium Chloride; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D013950:Thymus Gland
D003619:Dansyl Compounds; D006657:Histones; D012965:Sodium Chloride; D004247:DNA; D006656:Protamine Kinase