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Related Concept Videos

Histone Modification02:32

Histone Modification

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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...
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Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
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Assay development for histone methyltransferases.

Kurumi Y Horiuchi1, Mia M Eason, Joseph J Ferry

  • 1Department of Biochemistry, Reaction Biology Corporation, One Great Valley Parkway, Suite 2, Malvern, PA 19355, USA. kurumi.horiuchi@reactionbiology.com

Assay and Drug Development Technologies
|April 6, 2013
PubMed
Summary
This summary is machine-generated.

A novel radioisotope assay, the HotSpot(SM) platform, enables high-throughput screening of histone methyltransferases (HMTs). This method identified suramin as an inhibitor for DOT1L, NSD2, and PRMT4, advancing epigenetic drug discovery.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Epigenetics and Cancer Research

Background:

  • Epigenetic modifications, distinct from genetic mutations, are critical in human diseases, particularly cancer.
  • Histone methyltransferases (HMTs) regulate gene expression by methylating histone proteins, but lack standardized high-throughput screening (HTS) assays and reference inhibitors.
  • Understanding HMTs is crucial for developing targeted cancer therapies.

Purpose of the Study:

  • To develop and validate a miniaturized, radioisotope-based HTS assay for HMTs.
  • To characterize enzyme kinetics, substrate specificities, and perform compound profiling for HMTs.
  • To identify novel inhibitors for HMTs involved in cancer progression.

Main Methods:

  • Application of the HotSpot(SM) platform, a miniaturized radioisotope assay using tritiated S-adenosyl-L-methionine (SAM).
  • Assay development allows for the use of various substrates (peptides, proteins, nucleosomes) without modification.
  • High-throughput screening of a small library against DOT1L, followed by hit confirmation and profiling.

Main Results:

  • The HotSpot(SM) platform successfully enabled HTS, kinetic characterization, and substrate specificity determination for HMTs.
  • Suramin was identified as a potent inhibitor of DOT1L, NSD2, and PRMT4, with IC50 values in the low micromolar range.
  • The assay's versatility allows for the study of diverse HMTs and substrates.

Conclusions:

  • The HotSpot(SM) platform provides a robust and versatile HTS solution for methyltransferases.
  • This assay facilitates the discovery of novel epigenetic drug candidates, such as suramin, for cancer treatment.
  • The findings pave the way for further investigation of HMT inhibitors in oncology.