Abstract
Jun dimerization protein-2 (JDP2) is a component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Here, we examine the functional mechanisms of JDP2 and show that it can inhibit p300-mediated acetylation of core histones in vitro and in vivo. Inhibition of histone acetylation requires the N-terminal 35 residues and the DNA-binding region of JDP2. In addition, we demonstrate that JDP2 has histone-chaperone activity in vitro. These results suggest that the sequence-specific DNA-binding protein JDP2 may control transcription via direct regulation of the modification of histones and the assembly of chromatin.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation
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Animals
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Base Sequence
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Cell Cycle Proteins / antagonists & inhibitors
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Cell Cycle Proteins / metabolism
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DNA / genetics
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DNA / metabolism
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HeLa Cells
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Histone Acetyltransferases / antagonists & inhibitors
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Histone Acetyltransferases / metabolism
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Histones / metabolism*
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Humans
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In Vitro Techniques
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Mice
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Molecular Chaperones / chemistry
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism
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Nucleosomes / metabolism
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Protein Binding
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Repressor Proteins / chemistry
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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Sequence Deletion
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Transcription Factors / antagonists & inhibitors
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Transcription Factors / metabolism
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p300-CBP Transcription Factors
Substances
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Cell Cycle Proteins
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Histones
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Jundp2 protein, mouse
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Molecular Chaperones
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Nucleosomes
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Recombinant Proteins
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Repressor Proteins
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Transcription Factors
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DNA
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Histone Acetyltransferases
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p300-CBP Transcription Factors
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p300-CBP-associated factor