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Assays for Validating Histone Acetyltransferase Inhibitors
Published on: August 6, 2020
Probing p300/CBP associated factor (PCAF)-dependent pathways with a small molecule inhibitor.
Rahul Modak1, Jeelan Basha, Narendra Bharathy
1Transcription and Disease Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research , Bangalore, India 560064.
ACS Chemical Biology
|April 11, 2013
Summary
Embelin, a natural compound, specifically inhibits PCAF (KAT2B) activity, revealing its crucial role in muscle differentiation and gene regulation. This discovery offers new insights into PCAF
Area of Science:
- Biochemistry
- Molecular Biology
- Epigenetics
Background:
- PCAF (KAT2B) is a lysine acetyltransferase (KAT) involved in gene transcription.
- Its specific role is poorly understood due to the absence of selective inhibitors.
- PCAF acetylates histone H3K9 and other proteins, acting as a transcriptional coactivator.
Purpose of the Study:
- To identify a specific inhibitor for PCAF's acetyltransferase activity.
- To elucidate the exclusive role of PCAF's acetyltransferase function.
- To identify PCAF-regulated gene networks during muscle differentiation.
Main Methods:
- Screening for natural compounds with PCAF inhibitory activity.
- In vitro acetylation assays using recombinant PCAF.
- In vivo studies in mice to assess embelin's specificity.
- Analysis of gene networks regulated by PCAF during muscle differentiation.
Main Results:
- Embelin, a hydroxybenzoquinone, was identified as a specific inhibitor of PCAF.
- Embelin selectively inhibits H3Lys9 acetylation in vitro and in vivo.
- PCAF-regulated gene networks during muscle differentiation were identified using embelin.
Conclusions:
- Embelin is a specific inhibitor of PCAF acetyltransferase activity.
- PCAF plays a broader regulatory role in muscle differentiation beyond MyoD acetylation.
- This study provides a tool to investigate PCAF functions and its targets.
