First evidence of a functional interaction between DNA quadruplexes and poly(ADP-ribose) polymerase-1.
We discovered that the abundant human nuclear protein poly(ADP-ribose) polymerase-1 (hPARP-1) binds to intramolecular DNA quadruplexes in vitro with high affinity and with a stoichiometry of two proteins for one quadruplex. Using an enzymatic assay, we have shown that hPARP-1 gets catalytically activated upon binding to G-quadruplexes localized at the c-kit promoter and human telomere regions. This is the first example of a truly functional quadruplex-protein interaction, which has possible implications in understanding hPARP-1 mediated mechanisms of transcription regulation and telomere end protection.
Soldatenkov
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Vetcher
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Duka
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Ladame
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D054856:G-Quadruplexes; D006801:Humans; D018625:Microscopy, Atomic Force; D011065:Poly(ADP-ribose) Polymerases / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D019009:Proto-Oncogene Proteins c-kit / Q000235:genetics / Q000378:metabolism
D011065:Poly(ADP-ribose) Polymerases; D019009:Proto-Oncogene Proteins c-kit