title: Noncovalent pADPr interaction with proteins and competition with RNA for binding to proteins.
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.
authors.affiliation: Epigenetics and Progenitor Cell Program, Fox Chase Cancer Center, Philadelphia, PA, USA.
authors.forename: Yingbiao
authors.initials: Y
authors.lastname: Ji
mesh_terms: D024202:Electrophoretic Mobility Shift Assay; D006801:Humans; D015151:Immunoblotting; D047468:Immunoprecipitation; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D011064:Poly Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases