Literature DB >> 6259161

The effect of histone hyperacetylation on the nuclease sensitivity and the solubility of chromatin.

M Perry, R Chalkley.   

Abstract

We have examined the effects of histone hyperacetylation upon nuclease digestion of nuclei and subsequent fractionation of chromosomal material in the presence of MgCl2. DNase I shows a maximum sensitivity towards hyperacetylated nuclei at somewhat elevated ionic strengths (150-200 mM NaCl), whereas micrococcal nuclease exhibits no specificity for acetylated nuclei over a broad range of ionic strengths. Fractionation in the presence of MgCl2 of hyperacetylated nuclei digested with micrococcal nuclease results in a substantial increase in the amount of soluble chromatin relative to that obtained with control nuclei. This increased yield of Mg2+-soluble chromatin results from the recruitment into this fraction of oligonucleosomes containing extremely hyperacetylated histones. These results suggest that contiguous nucleosomes containing highly acetylated histones may be altered in their ability to interact with themselves and with other nucleosomes.

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Year:  1981        PMID: 6259161

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  26 in total

1.  Evidence for torsional stress in transcriptionally activated chromatin.

Authors:  M W Leonard; R K Patient
Journal:  Mol Cell Biol       Date:  1991-12       Impact factor: 4.272

Review 2.  On the biological role of histone acetylation.

Authors:  A Csordas
Journal:  Biochem J       Date:  1990-01-01       Impact factor: 3.857

Review 3.  Milestones in transcription and chromatin published in the Journal of Biological Chemistry.

Authors:  Joel M Gottesfeld
Journal:  J Biol Chem       Date:  2019-02-01       Impact factor: 5.157

4.  Treatment with sodium butyrate inhibits the complete condensation of interphase chromatin.

Authors:  A T Annunziato; L L Frado; R L Seale; C L Woodcock
Journal:  Chromosoma       Date:  1988       Impact factor: 4.316

5.  Histone acetylation in chicken erythrocytes. Rates of acetylation and evidence that histones in both active and potentially active chromatin are rapidly modified.

Authors:  D E Zhang; D A Nelson
Journal:  Biochem J       Date:  1988-02-15       Impact factor: 3.857

6.  The Influence of Ionic Environment and Histone Tails on Columnar Order of Nucleosome Core Particles.

Authors:  Nikolay V Berezhnoy; Ying Liu; Abdollah Allahverdi; Renliang Yang; Chun-Jen Su; Chuan-Fa Liu; Nikolay Korolev; Lars Nordenskiöld
Journal:  Biophys J       Date:  2016-04-26       Impact factor: 4.033

7.  Influence of histone acetylation on the solubility, H1 content and DNase I sensitivity of newly assembled chromatin.

Authors:  C A Perry; A T Annunziato
Journal:  Nucleic Acids Res       Date:  1989-06-12       Impact factor: 16.971

8.  The beta-globin domain in immature chicken erythrocytes: enhanced solubility is coincident with histone hyperacetylation.

Authors:  D A Nelson; R C Ferris; D E Zhang; C R Ferenz
Journal:  Nucleic Acids Res       Date:  1986-02-25       Impact factor: 16.971

9.  Computer modeling reveals that modifications of the histone tail charges define salt-dependent interaction of the nucleosome core particles.

Authors:  Ye Yang; Alexander P Lyubartsev; Nikolay Korolev; Lars Nordenskiöld
Journal:  Biophys J       Date:  2009-03-18       Impact factor: 4.033

10.  Chicken erythrocyte beta-globin chromatin: enhanced solubility is a direct consequence of induced histone hyperacetylation.

Authors:  W R Alonso; R C Ferris; D E Zhang; D A Nelson
Journal:  Nucleic Acids Res       Date:  1987-11-25       Impact factor: 16.971

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