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Nucleic Acids Research, 1977, Vol. 4, No. 4 1065-1082
© 1977

Articles

Histone HI - DNA interaction.Influence of phosphorylation on the interaction of histone HI with linear fragmented DNA

B.O. Glotov, L.G. Nikolaev, S.N. Kurochkin and E.S. Severin

Institute of Molecular Biology, Academy of Sciences of the USSR Moscow, 117312, USSR

Received March 4, 1977. By measuring the fluorescence polarization of fluorescent histone H1 derivatives complexed with DBA, 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 the complex which was completed at 0.5-0.6 M HaCl irrespective of phosphorylation. At the same time the phoephorylation of histone H1 led to removal of the central and, presumably, N-terminal regions of H1 from DNA.


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