Abstract
Human papillomavirus E2 protein is a transcription factor of viral gene expression and DNA replication. Here we show that PARP is a positive regulator of the E2 protein of human papillomavirus type 18 (HPV-18). PARP interacted with the COOH terminal region of HPV-18 E2 in vitro. The E2 interaction domain within PARP is located in the NH2-terminal zinc finger motif and the BRCT motif included in the automodification domain. Overexpression of either wild type or the NH2-terminal region of PARP containing zinc finger and BRCT stimulated E2-dependent transcription. Gel retardation assay indicates that PARP augments DNA binding activity of E2 in vitro. We also show that PARP-1 is recruited to E2-dependent promoter in vivo using ChIP assay. These results suggest that PARP serves a transcriptional co-activator in E2-dependent transcription by interacting directly with the HPV E2 protein.
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Acknowledgements
This work was supported in part by the National Research Laboratory Program of the Korea Institute of Science and Technology Evaluation and Planning (KISTEP), by the Molecular Medicine Research Group Program of KISTEP through the Biomedical Research Center at Korea Advanced Institute of Science and Technology, and by the BK21 Program of the Ministry of Education, Republic of Korea.
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Lee, D., Kim, J., Kim, K. et al. Functional interaction between human papillomavirus type 18 E2 and poly(ADP-ribose) polymerase 1. Oncogene 21, 5877–5885 (2002). https://doi.org/10.1038/sj.onc.1205723
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DOI: https://doi.org/10.1038/sj.onc.1205723
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