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• W2155805556 startingPage "1439" @default.
• W2155805556 abstract "This investigation demonstrates that the p53 and topoisomerase I (topo I) proteins which form a molecular complex in vivo are polyADP ribosylated following 1 Gy of gamma irradiation. Immunoprecipitations using a topo I monoclonal antibody were performed on protein extracts from gamma-irradiated TK6 human lymphoblastoid cells. Western blots on topo I immunoprecipitations probed with a polyADP-ribose polymer antibody demonstrated that several proteins, including p53, are co-immunoprecipitated with topo I. Furthermore, p53 and topo I are ADP ribosylated within 15 min following gamma irradiation. Unlike the other proteins within the complex, p53 is polyADP ribosylated at low levels in non-irradiated cells, and it is also the most heavily polyADP ribosylated following irradiation. Radiation induced polyADP ribosylation persists for at least 48 h following exposure. The DNA damage response does not involve the recruitment of free p53 to complex with topo I; the amount of p53 protein complexed with topo I was found to be independent of radiation exposure. It has recently been reported that p53 acts to catalytically stimulate the activity of topo I in the absence of DNA damage. We hypothesize that the rapid modification of the complex by polyADP ribosylation following radiation is a regulatory response to diminish topo I cleavage in the presence of DNA damage." @default.
• W2155805556 created "2016-06-24" @default.
• W2155805556 creator A5019402277 @default.
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• W2155805556 date "1999-08-01" @default.
• W2155805556 modified "2023-09-27" @default.
• W2155805556 title "PolyADP-ribose-mediated regulation of p53 complexed with topoisomerase I following ionizing radiation" @default.
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• W2155805556 doi "https://doi.org/10.1093/carcin/20.8.1439" @default.
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