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The role of charge neutralization and cooperative binding of linker histone in. the higher‐order structure of chromatin
Author(s) -
Watanabe Fumiyuki
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80612-x
Subject(s) - chromatin , histone h1 , nucleosome , linker dna , chromatosome , chemistry , histone , solenoid , biophysics , linker , neutralization , histone code , molecule , microbiology and biotechnology , biochemistry , dna , biology , genetics , physics , quantum mechanics , computer science , antibody , operating system , organic chemistry
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.