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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Functional interaction between human papillomavirus type 18 E2 and poly(ADP-ribose) polymerase 1.

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 NH(2)-terminal zinc finger motif and the BRCT motif included in the automodification domain. Overexpression of either wild type or the NH(2)-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.[1]

References

  1. Functional interaction between human papillomavirus type 18 E2 and poly(ADP-ribose) polymerase 1. Lee, D., Kim, J.W., Kim, K., Joe, C.O., Schreiber, V., Ménissier-De Murcia, J., Choe, J. Oncogene (2002) [Pubmed]
 
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