Abstract
The chromatin is comprised of repeating subunits that make up the nucleosome which is composed of an octamer of histones: H3, H4, H2A, and H2B. The replication-dependent and -independent nucleosome assembly occurs in an ordered fashion and is aided by cellular proteins such as histone chaperones and chromatin remodelers. Previously, we found that the histone chaperone NPM1 activates transcription from the chromatin template. Here we report that NPM3, a member of the nucleophosmin/nucleoplasmin family, lacks intrinsic histone chaperone activity, inhibits histone assembly activity of NPM1 in vitro, and dramatically enhances transcription in a cellular system.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Line
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HeLa Cells
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Histones / antagonists & inhibitors
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Histones / metabolism
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Humans
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Multigene Family / physiology*
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Nuclear Proteins / antagonists & inhibitors
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism
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Nuclear Proteins / physiology
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Nucleophosmin
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Nucleoplasmins / chemistry
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Nucleoplasmins / genetics
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Nucleoplasmins / physiology*
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Nucleosomes / chemistry
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Nucleosomes / genetics
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Nucleosomes / physiology
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Trans-Activators / chemistry
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Trans-Activators / genetics
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Trans-Activators / physiology*
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Transcription, Genetic*
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Up-Regulation / genetics
Substances
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Histones
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NPM1 protein, human
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NPM3 protein, human
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Nuclear Proteins
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Nucleoplasmins
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Nucleosomes
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Trans-Activators
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Nucleophosmin