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Related Concept Videos

Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

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Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

Screening assays for epigenetic targets using native histones as substrates.

Alexander-Thomas Hauser1, Elisabeth-Maria Bissinger, Eric Metzger

  • 1Institute of Pharmaceutical Sciences, University of Freiburg, Freiburg, Germany.

Journal of Biomolecular Screening
|October 4, 2011
PubMed
Summary

Researchers developed new in vitro assays using native core histones for studying chromatin-modifying enzymes. These assays provide a more accurate environment for identifying potential inhibitors of histone methyltransferases and demethylases.

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Area of Science:

  • Biochemistry
  • Epigenetics
  • Medicinal Chemistry

Background:

  • Aberrant histone methylation is implicated in various pathological processes.
  • Identifying selective inhibitors of chromatin-modifying enzymes is crucial for understanding transcriptional regulation.
  • Current high-throughput in vitro assays often use suboptimal oligopeptide substrates.

Purpose of the Study:

  • To establish in vitro assays utilizing native core histones as substrates.
  • To create an assay environment that more closely mimics native cellular conditions.
  • To enable more accurate identification and characterization of enzyme inhibitors.

Main Methods:

  • Setup and establishment of in vitro assays with native core histones.
  • Application of these substrates to a formaldehyde dehydrogenase assay for LSD1 (lysine-specific demethylase 1).
  • Development of two new antibody-based assays: a heterogeneous format for LSD1 and a homogeneous format for PRMT1 (protein arginine methyltransferase 1).

Main Results:

  • Demonstrated the utility of native core histones in in vitro assays for chromatin-modifying enzymes.
  • Successfully applied the new assay formats to characterize LSD1 and PRMT1.
  • Validated the assay system using known reference inhibitors for both enzymes.

Conclusions:

  • Native core histone substrates provide a more physiologically relevant environment for in vitro enzyme assays.
  • The developed antibody-based assays offer robust methods for inhibitor screening and characterization.
  • These improved assays facilitate the discovery of novel therapeutic agents targeting aberrant histone methylation.