The Binding Effect Of Ape1 And P53 Protein In A549 Cells And Hela Cells
Keywords
Ape Protein, P Protein, Interaction
Abstract
Objective To explore the endogenous and exogenous interaction between apurinic/apyrimidinicendonuclease (APE1) and p53 protein. Methods The recombinant plasmid pET42a-hAPE1 was transfected into E.coliBL21(DE3), and IPTG was used to induce the expression of GST-APE1 protein. After identification, it was purified by metal chelation chromatography, and the purified protein was identified by Westernblot to obtain the GST-APE1 fusion protein. Co-immunoprecipitation (Co-IP) and GST protein sedimentation experiments were performed to detect the binding of endogenous and exogenous APE1 and p53 proteins respectively. Immunofluorescence labeling was combined with laser confocal microscopy to determine the subcellular localization of APE1 and p53 proteins. . Results The expression of the transfected plasmid was induced by IPTG. Using SDS-PAGE, it was found that there was a positive band of GST-APE1 at the expected position 64¡Á103. After purification with “Ni” column, the GST-APE1 fusion protein was obtained and identified by Westernblot. Co-immunoprecipitation and GST protein sedimentation experiments confirmed the existence of endogenous and exogenous binding interactions between APE1 and p53. The immunofluorescence-labeled APE1 and p53 proteins observed under laser confocal microscopy are both nuclear-cytoplasmic co-expressed proteins. After oxidative stress treatment, the proteins gradually moved from the cytoplasm to the nucleus, and their co-localization was obvious at the nuclear membrane. Conclusion APE1 and p53 proteins have endogenous and exogenous binding effects in A549 and HeLa cells, which may be related to their transcriptional regulation and the efficacy of tumor radiotherapy and chemotherapy.
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Original research done by Zhang, Li Mengxia, Cheng, Li Zengpeng, Wang Ge, Wang Dong, Yang Zhenzhou
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