Histone acetylation reduces nucleosome core particle linking number change

Vicki G. Norton; Brian S. Imai; Peter Yau; E. Morton Bradbury

doi:10.1016/0092-8674(89)90920-3

Histone acetylation reduces nucleosome core particle linking number change

Vicki G. Norton, Brian S. Imai, Peter Yau, E. Morton Bradbury

Research output: Contribution to journal › Article › peer-review

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.

Original language	English (US)
Pages (from-to)	449-457
Number of pages	9
Journal	Cell
Volume	57
Issue number	3
DOIs	https://doi.org/10.1016/0092-8674(89)90920-3
State	Published - May 5 1989
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/0092-8674(89)90920-3

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@article{3807527a86344b74863f1b53464809cb,

title = "Histone acetylation reduces nucleosome core particle linking number change",

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.",

author = "Norton, {Vicki G.} and Imai, {Brian S.} and Peter Yau and Bradbury, {E. Morton}",

note = "Funding Information: We would lrke to thank Dr. R. T. Simpson for his ktnd gift of the plasmid p5S207-18, Mrchael Dunlap and Bo Addison of the Facility of Advanced Instrumentation at the Unrversity of California, Davis; Bob Munn and Paul Lee of the Electron Microscopy Facility at the Untversity of Califor-ma. Davis for their krnd assrstance wtth the electron microscopy; Mrchel Roberge and Tim O{\textquoteright}Neill for helpful discussions. Kathleen Mar-trnerfor her assistance rn the preparation of this manuscript. This work was supported by National Institutes of Health grant GM 26901.",

year = "1989",

month = may,

day = "5",

doi = "10.1016/0092-8674(89)90920-3",

language = "English (US)",

volume = "57",

pages = "449--457",

journal = "Cell",

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TY - JOUR

T1 - Histone acetylation reduces nucleosome core particle linking number change

AU - Norton, Vicki G.

AU - Imai, Brian S.

AU - Yau, Peter

AU - Bradbury, E. Morton

N1 - Funding Information: We would lrke to thank Dr. R. T. Simpson for his ktnd gift of the plasmid p5S207-18, Mrchael Dunlap and Bo Addison of the Facility of Advanced Instrumentation at the Unrversity of California, Davis; Bob Munn and Paul Lee of the Electron Microscopy Facility at the Untversity of Califor-ma. Davis for their krnd assrstance wtth the electron microscopy; Mrchel Roberge and Tim O’Neill for helpful discussions. Kathleen Mar-trnerfor her assistance rn the preparation of this manuscript. This work was supported by National Institutes of Health grant GM 26901.

PY - 1989/5/5

Y1 - 1989/5/5

N2 - 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.

AB - 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.

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JO - Cell

JF - Cell

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ER -

Histone acetylation reduces nucleosome core particle linking number change

Abstract

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