The histone chaperone SET/TAF-Ibeta interacts functionally with the CREB-binding protein
Autor: | Thomais Papamarcaki, George Sflomos, Zoe Karetsou, Goran Martic |
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Rok vydání: | 2005 |
Předmět: |
Transcriptional Activation
Transcription Genetic Chromosomal Proteins Non-Histone Biophysics Biochemistry Chromatin remodeling Histones Histone H1 Histone H2A Histone code Humans Immunoprecipitation Biotinylation Histone Chaperones CREB-binding protein Fluorescent Antibody Technique Indirect Molecular Biology Glutathione Transferase Microscopy Confocal biology Cell Cycle Nuclear Proteins Cell Biology Molecular biology CREB-Binding Protein Recombinant Proteins Cell biology DNA-Binding Proteins Histone Histone methyltransferase Transcription Coactivator Mutation biology.protein Trans-Activators HeLa Cells Molecular Chaperones Plasmids Protein Binding Transcription Factors |
Zdroj: | Biochemical and biophysical research communications. 335(2) |
ISSN: | 0006-291X |
Popis: | The oncoprotein SET/TAF-Ibeta is a histone chaperone which is involved in cell-cycle control and chromatin remodeling. Confocal laser scanning microscopy reveals that SET is localized in distinct foci of variable size throughout the nucleoplasm of interphase cells. We report here that SET interacts directly with the acetyltransferase CREB-binding protein (CBP) and enhances the transactivation potential of the transcription coactivator. Our data suggest that the histone chaperone SET regulates the CBP-mediated transcription and may indicate a general principle by which transcriptional regulators cooperate with histone chaperones for gene activation. |
Databáze: | OpenAIRE |
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