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PMID: 2541913 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Histone acetylation reduces nucleosome core particle linking number change.

Cell ·Vol. 57 ·No. 3 ·1989-05-05 ·Pages 449-57

Norton VG, Imai BS, Yau P, Bradbury EM

Abstract

Nucleosome core particles differing in their levels of histone acetylation have been formed on a closed circular DNA that contains a tandemly repeated 207 bp nucleosome positioning sequence. The effect of acetylation on the linking number per nucleosome particle has been determined. With increasing levels of acetylation, the negative linking number change per nucleosome decreases from -1.04 +/- 0.08 for control to -0.82 +/- 0.05 for highly acetylated nucleosomes. These results indicate that histone acetylation has the ability to release negative supercoils previously constrained by nucleosomes into a closed chromatin loop and in effect function as a eukaryotic gyrase.

MeSH Terms
Acetylation Base Composition Chromosomes/analysis DNA Topoisomerases, Type II/physiology DNA, Circular/metabolism,ultrastructure DNA, Superhelical/analysis Genetic Linkage HeLa Cells Histones/metabolism Humans Nucleosomes/metabolism,ultrastructure Plasmids RNA, Ribosomal, 5S/genetics
Chemicals
DNA, Circular DNA, Superhelical Histones Nucleosomes RNA, Ribosomal, 5S DNA Topoisomerases, Type II
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Norton V G
Department of Biological Chemistry, School of Medicine, University of California, Davis 95616.
Imai B S
Yau P
Bradbury E M
Article Info
Journal
Cell
Abbr.
Cell
ISSN
0092-8674
Published
1989-05-05
Pages
449-57
Language
English
Region
United States
NLM ID
0413066
Subset
IM
Grants
NIGMS NIH HHS · GM 26901 · United States
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