Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek
| Autor: | Gerard Grosveld, Edwin J. Mientjes, Rekha Iyengar, Craig J. McPherson, Andrew D. Hollenbach |
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| Rok vydání: | 2002 |
| Předmět: |
Transcription
Genetic Chromosomal Proteins Non-Histone Recombinant Fusion Proteins Histone Deacetylase 2 Histone Deacetylases Cell Line Histones Mice chemistry.chemical_compound Death-associated protein 6 Transcription (biology) Animals Humans Protein Isoforms Poly-ADP-Ribose Binding Proteins Adaptor Proteins Signal Transducing Oncogene Proteins Models Genetic biology Protein DEK Intracellular Signaling Peptides and Proteins Nuclear Proteins Cell Biology Molecular biology Chromatin Protein Structure Tertiary Cell biology DNA-Binding Proteins Repressor Proteins Nucleoproteins Histone Gene Expression Regulation chemistry biology.protein Nucleic Acid Conformation Phosphorylation Histone deacetylase Carrier Proteins Co-Repressor Proteins DNA Molecular Chaperones Protein Binding |
| Zdroj: | Journal of Cell Science. 115:3319-3330 |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | Human Daxx is a protein that functions, in part, as a transcriptional co-repressor through its interaction with a growing number of nuclear,DNA-associated proteins. To determine the mechanism by which hDaxx represses transcription, we used conventional chromatography to isolate endogenous hDaxx. We determined that hDaxx has an apparent molecular weight of 360 kDa,which is consistent with the fact that multiple domains of hDaxx are required for transcriptional repression and suggests that hDaxx associates with multiple proteins. Using co-fractionation and co-immunoprecipitation we demonstrate that hDaxx associates with proteins that are critical for transcriptional repression, such as histone deacetylase II, constituents of chromatin such as core histones H2A, H2B, H3 and H4, and Dek, a chromatin-associated protein reported to change the topology of DNA in chromatin in vitro. We also demonstrate a requirement for the SPT domain and the first paired amphipathic helix of hDaxx for its association with histone deacetylase II and acetylated histone H4, respectively. Finally, we provide evidence suggesting that the association of hDaxx with chromatin-related proteins is dependent on the post-translational phosphorylation status of hDaxx. A working model for the repressive action of hDaxx through its association with chromatin related proteins is presented. |
| Databáze: | OpenAIRE |
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