Small-Molecule Screening Assay for Mono-ADP-Ribosyltransferases

Methods Mol Biol. 2018:1813:237-244. doi: 10.1007/978-1-4939-8588-3_16.

Abstract

Mono-ADP-ribosyltransferases of the PARP/ARTD enzyme family are enzymes catalyzing the transfer of a single ADP-ribose unit to target proteins. The enzymes have various roles in vital cellular processes such as DNA repair and transcription, and many of the enzymes are linked to cancer-relevant functions. Thus inhibition of the enzymes is a potential way to discover and develop new drugs against cancer. Here we describe an activity-based screening assay for mono-ADP-ribosyltransferases. The assay utilizes the natural substrate of the enzymes, NAD+, and it is based on chemically converting the leftover substrate to a fluorophore and measuring its relative concentration after the enzymatic reaction. The assay is homogenous, robust, and cost-effective and, most importantly, applicable to mono-ADP-ribosyltransferases as well as poly-ADP-ribosyltransferases for screening of small-molecule inhibitors against the enzymes.

Keywords: ARTD; Inhibitor; Mono-ADP-ribosyltransferase; PARP; Screening assay.

MeSH terms

  • ADP Ribose Transferases / antagonists & inhibitors*
  • ADP Ribose Transferases / chemistry
  • DNA Repair / drug effects
  • High-Throughput Screening Assays / methods*
  • Humans
  • NAD / chemistry
  • Neoplasms / drug therapy*
  • Small Molecule Libraries / chemistry
  • Small Molecule Libraries / pharmacology*
  • Substrate Specificity

Substances

  • Small Molecule Libraries
  • NAD
  • ADP Ribose Transferases