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In Vitro Activity Assays for MYST Histone Acetyltransferases and Adaptation for High-Throughput Inhibitor Screening.

C E McCullough1, R Marmorstein2

  • 1University of Pennsylvania, Philadelphia, PA, United States.

Methods in Enzymology
|July 4, 2016
PubMed
Summary

This chapter details methods for studying MYST proteins, a key family of acetyltransferases involved in gene regulation and DNA repair. It provides protocols for protein preparation, biochemical assays, and high-throughput screening for MYST inhibitors.

Keywords:
Bisubstrate kineticsEnzyme assaysHigh-throughput screeningHistone acetyltransferasesMYST proteinsPing-pong mechanism

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Lysine acetylation is a crucial posttranslational modification regulating diverse cellular processes.
  • MYST proteins are the largest family of acetyltransferases, impacting gene expression, DNA repair, and cell cycle.
  • Understanding MYST protein function requires robust biochemical characterization methods.

Purpose of the Study:

  • To describe methods for preparing and biochemically characterizing MYST family acetyltransferases.
  • To provide protocols for enzyme and binding assays, including cofactor and inhibitor interactions.
  • To guide researchers in adapting assays for high-throughput screening of small molecule MYST inhibitors.

Main Methods:

  • Recombinant protein expression and purification of MYST acetyltransferases.
  • Enzyme assays to determine steady-state kinetic parameters.
  • Binding assays to quantify cofactor and inhibitor interactions.

Main Results:

  • Established protocols for preparing functional recombinant MYST proteins.
  • Validated enzyme and binding assays for MYST acetyltransferase activity.
  • Demonstrated adaptability of assays for high-throughput screening (HTS) of inhibitors.

Conclusions:

  • Provides essential methodologies for the biochemical study of MYST proteins.
  • Facilitates the discovery of small molecule inhibitors targeting MYST enzymes.
  • Aims to improve data quality and experimental design in MYST protein research.