Open AccessModulation of the Nucleosome Structure by Histone Acetylation
Author(s) -
BODE Jürgen,
HENCO Karsten,
WINGENDER Edgar
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04849.x
Subject(s) - histone octamer , histone , nucleosome , chinese hamster ovary cell , biophysics , acetylation , chemistry , interphase , histone h1 , microbiology and biotechnology , dna , biochemistry , biology , receptor , gene
A rapid procedure for the isolation of core particles from Chinese hamster ovary cells is described which permits measurements, usually at the day of their preparation. Particles of 145 ± 5 base pairs, derived from interphase cells, will be compared with the analogue specimens from butyrate‐treated cells, metaphase cells and a standard preparation from chicken erythrocytes. Butyrate cause an increase in the acetylation of histones H3 and H4, which induces alterations of the interhistone and histone‐DNA interactions. Changes in the interhistone contacts, correlated to an extension of a‐helical segments, lead to an altered accessibility of the H3 cysteine side‐chains and to a different histone displacement by protamines. On the other hand, histone‐DNA contacts are loosened in parts and this is particularly evident from the changes in the premelting region of a thermal‐denaturation profile.