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

Cited 18 time in webofscience Cited 0 time in scopus
  • Hit : 371
  • Download : 0
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.
Publisher
NATURE PUBLISHING GROUP
Issue Date
2002-08
Language
English
Article Type
Article
Keywords

CALCIUM-INDUCED DIFFERENTIATION; HUMAN KERATINOCYTES; ADP-RIBOSYLATION; TRANSCRIPTIONAL REPRESSOR; CELL-DIFFERENTIATION; MAMMALIAN-CELLS; E7 ONCOPROTEIN; E6 ONCOPROTEIN; EARLY PROMOTER; HELA-CELLS

Citation

ONCOGENE, v.21, no.38, pp.5877 - 5885

ISSN
0950-9232
URI
http://hdl.handle.net/10203/80536
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 18 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0