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Updated: May 29, 2026

An Optimized Quantitative Pull-Down Analysis of RNA-Binding Proteins Using Short Biotinylated RNA
Published on: February 17, 2023
Noncovalent pADPr interaction with proteins and competition with RNA for binding to proteins
1Epigenetics and Progenitor Cell Program, Fox Chase Cancer Center, Philadelphia, PA, USA.
Abstract:
PARP1 can modify a variety of proteins through conserved domains in noncovalent manner. Since poly(ADP-ribose) is highly negatively charged and has a strong binding affinity for its target proteins, noncovalent binding by poly(ADP-ribose) modulates the protein activity during developmental processes. In this section, the methods including co-immunoprecipitation and dot-blot assay were illustrated for determining the specific interaction between poly(ADP-ribose) and proteins. Furthermore, the protocol for RNA EMSA was described to determine whether pADPr binding to hnRNPs can inhibit RNA-binding ability of human hnRNP A1.
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