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Modulation of the nucleosome structure by histone acetylation.

Authors :
Bode J
Henco K
Wingender E
Source :
European journal of biochemistry [Eur J Biochem] 1980 Sep; Vol. 110 (1), pp. 143-52.
Publication Year :
1980

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.

Details

Language :
English
ISSN :
0014-2956
Volume :
110
Issue :
1
Database :
MEDLINE
Journal :
European journal of biochemistry
Publication Type :
Academic Journal
Accession number :
7439155
Full Text :
https://doi.org/10.1111/j.1432-1033.1980.tb04849.x