The role of charge neutralization and cooperative binding of linker histone in the higher-order structure of chromatin.
The binding mode and stoichiometry of interaction between soluble rat liver chromatin and histone H1 (H1) were studied. H1 binding to chromatin is cooperative. Chromatin accepts 3.6 molecules of H1/nucleosome at 0 M salt, close to the required ratio for neutralization of 90% of the charges on the phosphate groups of chromatin (4.0 H1 molecules/nucleosome). The proposal is put forward that critical charge neutralization (90%) has a significant influence on the irregular appearance of chromatin.
Watanabe
F
F
Institut für Zellbiologie, ETH Hönggerberg, Zürich, Switzerland.
D000818:Animals; D001665:Binding Sites; D002843:Chromatin / Q000378:metabolism*; D004563:Electrochemistry; D005453:Fluorescence; D006657:Histones / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism; D051381:Rats
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes