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PMID: 7439155 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Modulation of the nucleosome structure by histone acetylation.

European journal of biochemistry ·Vol. 110 ·No. 1 ·1980-09-00 ·Pages 143-52

Bode J, Henco K, Wingender E

Abstract

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 alpha-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.

MeSH Terms
Acetylation Animals Butyrates Cell Cycle Chickens Cricetinae Cricetulus Erythrocytes Female Histones Hot Temperature Macromolecular Substances Molecular Conformation Nucleosomes/drug effects Ovary/cytology Protamines/pharmacology
Chemicals
Butyrates Histones Macromolecular Substances Nucleosomes Protamines
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bode J
Henco K
Wingender E
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1980-09-00
Pages
143-52
Language
English
Region
England
NLM ID
0107600
Subset
IM
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