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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Acknowledgment
The research was supported by grants from the National Institutes of Health (R01 GM077452) to Alexei V. Tulin.
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Ji, Y. (2011). Noncovalent pADPr Interaction with Proteins and Competition with RNA for Binding to Proteins. In: Tulin, A. (eds) Poly(ADP-ribose) Polymerase. Methods in Molecular Biology, vol 780. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-270-0_6
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DOI: https://doi.org/10.1007/978-1-61779-270-0_6
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Publisher Name: Humana Press, Totowa, NJ
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Online ISBN: 978-1-61779-270-0
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