Functional interaction between human papillomavirus type 18 E2 and poly(ADP-ribose) polymerase 1.
Oncogene
; 21(38): 5877-85, 2002 Aug 29.
Article
en En
| MEDLINE
| ID: mdl-12185587
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 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.
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Bases de datos:
MEDLINE
Asunto principal:
Proteínas Oncogénicas Virales
/
Poli(ADP-Ribosa) Polimerasas
Límite:
Humans
Idioma:
En
Revista:
Oncogene
Asunto de la revista:
BIOLOGIA MOLECULAR
/
NEOPLASIAS
Año:
2002
Tipo del documento:
Article