Interaction of Histone Acetylases and Deacetylases In Vivo
| Autor: | Yonghong Wang, Keiko Ozato, Richard M. Siegel, Shigakazu Sasaki, Tomohiko Kanno, Satoshi Yamagoe, Bruce H. Howard, Yoshihiro Nakatani, Yuka Kanno, Glen Humphrey, Michael J. Lenardo |
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| Rok vydání: | 2003 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Macromolecular Substances Cellular differentiation Gene Expression Cell Cycle Proteins Histone Deacetylase 1 P300-CBP Transcription Factors In Vitro Techniques Histone Deacetylases Acetyltransferases Fluorescence Resonance Energy Transfer Humans p300-CBP Transcription Factors Molecular Biology Transcription factor Histone Acetyltransferases biology Cell Differentiation U937 Cells Cell Biology Recombinant Proteins HDAC1 Chromatin Cell biology Histone Biochemistry PCAF Multiprotein Complexes Trans-Activators biology.protein HeLa Cells Transcription Factors |
| Zdroj: | Molecular and Cellular Biology. 23:1025-1033 |
| ISSN: | 1098-5549 |
| DOI: | 10.1128/mcb.23.3.1025-1033.2003 |
| Popis: | Having opposing enzymatic activities, histone acetylases (HATs) and deacetylases affect chromatin and regulate transcription. The activities of the two enzymes are thought to be balanced in the cell by an unknown mechanism that may involve their direct interaction. Using fluorescence resonance energy transfer analysis, we demonstrated that the acetylase PCAF and histone deacetylase 1 (HDAC1) are in close spatial proximity in living cells, compatible with their physical interaction. In agreement, coimmunoprecipitation assays demonstrated that endogenous HDACs are associated with PCAF and another acetylase, GCN5, in HeLa cells. We found by glycerol gradient sedimentation analysis that HATs are integrated into a large multiprotein HDAC complex that is distinct from the previously described HDAC complexes containing mSin3A, Mi-2/NRD, or CoREST. This HDAC-HAT association is partly accounted for by a direct protein-protein interaction observed in vitro. The HDAC-HAT complex may play a role in establishing a dynamic equilibrium of the two enzymes in vivo. |
| Databáze: | OpenAIRE |
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