Energy-dependent chromatin accessibility and nucleosome mobility in a cell-free system.
Chromatin structure must be flexible to allow the binding of regulatory proteins and to accommodate different levels of gene activity. Chromatin assembled in a cell-free system derived from Drosophila embryos contains an activity that hydrolyses ATP to render entire nucleosome arrays mobile. Nucleosome movements, most likely their sliding, occurred even in the presence of the linker histone H1. The dynamic state of chromatin in the presence of the activity and ATP globally increased the accessibility of nucleosomal DNA to incoming proteins. This unprecedented demonstration of energy-dependent nucleosome mobility identifies a new principle which is likely to be fundamental to the mechanism of chromatin remodelling and the binding of regulatory proteins.
Varga-Weisz
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European Molecular Biology Laboratory, Heidelberg, Germany.
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Becker
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D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002474:Cell-Free System; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D015252:Deoxyribonucleases, Type II Site-Specific / Q000378:metabolism; D004330:Drosophila / Q000196:embryology / Q000235:genetics*; D029721:Drosophila Proteins; D004734:Energy Metabolism; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics; D006657:Histones / Q000378:metabolism; D018398:Homeodomain Proteins; D008957:Models, Genetic; D009068:Movement / Q000502:physiology*; D009707:Nucleosomes / Q000502:physiology*; D011401:Promoter Regions, Genetic / Q000235:genetics; D014157:Transcription Factors / Q000378:metabolism
D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D018840:HSP70 Heat-Shock Proteins; D006657:Histones; D018398:Homeodomain Proteins; D009707:Nucleosomes; D014157:Transcription Factors; C063460:Trl protein, Drosophila; D000255:Adenosine Triphosphate; D004247:DNA; D015252:Deoxyribonucleases, Type II Site-Specific