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

2.50
Hdl Handle:
http://hdl.handle.net/10541/104738
Title:
ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.
Authors:
Banerjee, S; Bennion, Gordon; Goldberg, Martin W; Allen, Terence D
Abstract:
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.
Affiliation:
Department of Pathology, Royal Veterinary College, University of London, UK.
Citation:
ATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract. 1991, 19 (21):5999-6006 Nucleic Acids Res.
Journal:
Nucleic Acids Research
Issue Date:
11-Nov-1991
URI:
http://hdl.handle.net/10541/104738
DOI:
10.1093/nar/19.21.5999
PubMed ID:
1945884
Type:
Article
Language:
en
ISSN:
0305-1048
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorBanerjee, Sen
dc.contributor.authorBennion, Gordonen
dc.contributor.authorGoldberg, Martin Wen
dc.contributor.authorAllen, Terence Den
dc.date.accessioned2010-06-11T15:05:09Z-
dc.date.available2010-06-11T15:05:09Z-
dc.date.issued1991-11-11-
dc.identifier.citationATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract. 1991, 19 (21):5999-6006 Nucleic Acids Res.en
dc.identifier.issn0305-1048-
dc.identifier.pmid1945884-
dc.identifier.doi10.1093/nar/19.21.5999-
dc.identifier.urihttp://hdl.handle.net/10541/104738-
dc.description.abstractPhysiologically 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.en
dc.language.isoenen
dc.subject.meshAdenosine Triphosphate-
dc.subject.meshCell Extracts-
dc.subject.meshCell-Free System-
dc.subject.meshCentrifugation, Density Gradient-
dc.subject.meshChromatin-
dc.subject.meshDNA-
dc.subject.meshElectrophoresis-
dc.subject.meshHela Cells-
dc.subject.meshHistones-
dc.subject.meshHumans-
dc.subject.meshMagnesium-
dc.subject.meshMicrococcal Nuclease-
dc.subject.meshMicroscopy, Electron-
dc.subject.meshNucleic Acid Conformation-
dc.subject.meshNucleosomes-
dc.subject.meshPhosphorylation-
dc.titleATP dependent histone phosphorylation and nucleosome assembly in a human cell free extract.en
dc.typeArticleen
dc.contributor.departmentDepartment of Pathology, Royal Veterinary College, University of London, UK.en
dc.identifier.journalNucleic Acids Researchen

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