ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.

Physiologically spaced nucleosome formation in HeLa cell extracts is ATP dependent. ATP hydrolysis is required for chromatin assembly on both linear and covalently closed circular DNA. The link between the phosphorylation state of histones and nucleosome formation has been examined and we demonstrat...

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Main Authors: Banerjee, S, Bennion, G R, Goldberg, M W, Allen, T D
Formato: Artigo
Idioma:en
Publicado em: 1991
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC329058/
https://ncbi.nlm.nih.gov/pubmed/1945884
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spelling pubmed-3290582004-02-10 ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract. Banerjee, S Bennion, G R Goldberg, M W Allen, T D Nucleic Acids Res Physiologically spaced nucleosome formation in HeLa cell extracts is ATP dependent. ATP hydrolysis is required for chromatin assembly on both linear and covalently closed circular DNA. The link between the phosphorylation state of histones and nucleosome formation has been examined and we demonstrate that in the absence of histone phosphorylation no stable and regularly spaced nucleosomes are formed. Phosphorylated H3 stabilizes the nucleosome core; while phosphorylation of histone H2a is necessary to increase the linker length between nucleosomes from 0 to approximately 45 bp. Histone H1 alone, whether phosphorylated or unphosphorylated, does not increase the nucleosome repeat length in the absence of core histone phosphorylation. Phosphorylations of H1 and H3 correlate with condensation of chromatin. Maximum ATP hydrolysis which is necessary to increase the periodicity of nucleosomes from approximately 150 to approximately 185 bp, not only inhibits H1 and H3 phosphorylation but facilitates their dephosphorylation. 1991-11-11 /pmc/articles/PMC329058/ /pubmed/1945884 Text en
institution US National Library of Medicine
collection PubMed Central
language en
format Article
description Physiologically spaced nucleosome formation in HeLa cell extracts is ATP dependent. ATP hydrolysis is required for chromatin assembly on both linear and covalently closed circular DNA. The link between the phosphorylation state of histones and nucleosome formation has been examined and we demonstrate that in the absence of histone phosphorylation no stable and regularly spaced nucleosomes are formed. Phosphorylated H3 stabilizes the nucleosome core; while phosphorylation of histone H2a is necessary to increase the linker length between nucleosomes from 0 to approximately 45 bp. Histone H1 alone, whether phosphorylated or unphosphorylated, does not increase the nucleosome repeat length in the absence of core histone phosphorylation. Phosphorylations of H1 and H3 correlate with condensation of chromatin. Maximum ATP hydrolysis which is necessary to increase the periodicity of nucleosomes from approximately 150 to approximately 185 bp, not only inhibits H1 and H3 phosphorylation but facilitates their dephosphorylation.
author Banerjee, S
Bennion, G R
Goldberg, M W
Allen, T D
spellingShingle Banerjee, S
Bennion, G R
Goldberg, M W
Allen, T D
ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.
author_facet Banerjee, S
Bennion, G R
Goldberg, M W
Allen, T D
author_sort Banerjee, S
title ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.
title_short ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.
title_full ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.
title_fullStr ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.
title_full_unstemmed ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.
title_sort atp dependent histone phosphorylation and nucleosome assembly in a human cell free extract.
publishDate 1991
url https://ncbi.nlm.nih.gov/pmc/articles/PMC329058/
https://ncbi.nlm.nih.gov/pubmed/1945884
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