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Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
Published on: September 21, 2011
Steroid receptor coactivator-1 is a histone acetyltransferase
T E Spencer1, G Jenster, M M Burcin
1Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
Nature
|September 20, 1997
Summary
Steroid receptor coactivator SRC-1 has histone acetyltransferase activity, aiding gene transcription. This activity, along with PCAF, helps overcome chromatin repression, enabling gene activation.
Area of Science:
- Molecular Biology
- Epigenetics
- Gene Regulation
Background:
- Steroid receptors and coactivators typically enhance gene expression by forming transcription complexes.
- Accessing repressed chromatin remains a key question in understanding gene activation in vivo.
- Histone acetyltransferases (HATs) are known to counteract chromatin's inhibitory effects on transcription.
Purpose of the Study:
- To investigate the role of steroid receptor coactivator SRC-1 in chromatin modulation.
- To determine if SRC-1 possesses intrinsic histone acetyltransferase (HAT) activity.
- To explore the interaction between SRC-1, PCAF, and histone acetylation in gene transcription.
Main Methods:
- Biochemical assays to assess HAT activity of SRC-1.
- Protein interaction studies to examine SRC-1 and PCAF binding.
- Analysis of histone acetylation patterns on specific gene promoters.
Main Results:
- SRC-1 exhibits intrinsic HAT activity, primarily targeting histones H3 and H4.
- SRC-1 interacts with another HAT, p300/CBP-associated factor (PCAF).
- Ligand binding to steroid receptors may trigger SRC-1 and PCAF-mediated histone acetylation.
Conclusions:
- SRC-1's HAT activity is crucial for overcoming chromatin repression.
- Coordinated action of SRC-1 and PCAF facilitates transcription factor access to repressed chromatin.
- This mechanism enhances steroid receptor-mediated gene activation and increases specific gene transcription.
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