| Autor: |
A. Soldatenkov, V., Duka, T., A. Soldatenkov, V., Ladame, S., A. Vetcher, A. |
| Zdroj: |
ACS Chemical Biology; April 2008, Vol. 3 Issue: 4 p214-219, 6p |
| Abstrakt: |
We discovered that the abundant human nuclear protein poly(ADP-ribose) polymerase-1 (hPARP-1) binds to intramolecular DNA quadruplexes in vitrowith 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. |
| Databáze: |
Supplemental Index |
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