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A miniaturized readout strategy for endogenous histone deacetylase activity
Jan Oliver Jost1, Alfred Hanswillemenke, Dirk Schwarzer
1Interfaculty Institute of Biochemistry, University of Tuebingen, Hoppe-Seyler-Str. 4, 72076 Tuebingen, Germany. dirk.schwarzer@uni-tuebingen.de.
Molecular Biosystems
|May 27, 2015
Summary
We developed a new assay to measure histone deacetylase (HDAC) activity. This tool helps profile the substrate selectivity of HDACs on histone H4 and p53.
Area of Science:
- Biochemistry
- Molecular Biology
- Drug Discovery
Background:
- Histone deacetylases (HDACs) are crucial drug targets.
- Characterizing HDACs is challenging due to poor accessibility.
Purpose of the Study:
- To develop a miniaturized assay for multi-site readout of deacetylase activity.
- To profile the substrate selectivity of HDACs.
Main Methods:
- Developed a miniaturized assay.
- Utilized the assay for multi-site readout of deacetylase activity.
- Profiled substrate selectivity on histone H4 and p53.
Main Results:
- Successfully developed and implemented a miniaturized assay.
- Enabled multi-site readout of deacetylase activity.
- Characterized substrate selectivity of HDACs for histone H4 and p53 acetylation sites.
Conclusions:
- The developed assay facilitates HDAC characterization.
- Provides insights into substrate selectivity for histone H4 and p53.
- A valuable tool for drug discovery targeting HDACs.
