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High-Throughput Arginylation Assay in Microplate Format.

Sougata Saha1, Junling Wang2, Anna S Kashina3

  • 1Tezpur University, Napaam, Assam, India.

Methods in Molecular Biology (Clifton, N.J.)
|April 3, 2023
PubMed
Summary
This summary is machine-generated.

We developed a new biochemical assay for arginylation by Arginyltransferase 1 (ATE1). This high-throughput screening method identified two compounds affecting ATE1 activity in vitro and in vivo.

Keywords:
ATE1 inhibitorsAngiogenesisArginylationCell motilityTannic acid

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Arginyltransferase 1 (ATE1) plays a crucial role in protein degradation pathways.
  • Understanding ATE1-mediated arginylation is vital for various biological processes.
  • Existing methods for studying ATE1 activity are limited in throughput and scope.

Purpose of the Study:

  • To develop a novel, high-throughput biochemical assay for ATE1-mediated arginylation.
  • To identify small molecules that modulate ATE1 activity.
  • To enable high-volume analysis of ATE1 substrates.

Main Methods:

  • Developed a microplate-based biochemical assay for in vitro arginylation.
  • The assay utilizes the N-terminal peptide of beta-actin as a model substrate for ATE1.
  • Screened a library of 3280 diverse chemical compounds.

Main Results:

  • Successfully established a robust and scalable assay for ATE1 activity.
  • Identified two distinct compounds that specifically inhibit or activate ATE1-regulated processes.
  • Demonstrated the assay's applicability for both in vitro and in vivo studies.

Conclusions:

  • The developed microplate assay is suitable for high-throughput screening of ATE1 modulators.
  • This assay facilitates the discovery of novel small molecules impacting ATE1 function.
  • The assay can be adapted for different ATE1 substrates, broadening its utility.