ArticleJournal of virology1998
Functional interaction of the bovine papillomavirus E2 transactivation domain with TFIIB.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- E2 Tyrosine 102 Regulates MmuPV1 Pathogenesis In Vivo.Pathogens (Basel, Switzerland) · 2025Article
- A conserved cysteine in the DNA-binding domain of MmuPV1 E2 is required for replicationJournal of virology · 2025Article
- Phosphorylation of the Bovine Papillomavirus E2 Protein on Tyrosine Regulates Its Transcription and Replication Functions.Journal of virology · 2017Article
- Phosphorylation of HPV-16 E2 at serine 243 enables binding to Brd4 and mitotic chromosomes.PloS one · 2014Article
- The papillomavirus E2 proteins.Virology · 2013Review
- Acetylation of conserved lysines in bovine papillomavirus E2 by p300.Journal of virology · 2013Article
- NRIP, a novel calmodulin binding protein, activates calcineurin to dephosphorylate human papillomavirus E2 protein.Journal of virology · 2011Article
- Small molecule inhibitors of human papillomavirus protein - protein interactions.The open virology journal · 2011Article
- Tax1BP1 interacts with papillomavirus E2 and regulates E2-dependent transcription and stability.Journal of virology · 2009Article
- Modification of papillomavirus E2 proteins by the small ubiquitin-like modifier family members (SUMOs).Virology · 2008Article
- Brd4-independent transcriptional repression function of the papillomavirus e2 proteins.Journal of virology · 2007Article
- Interaction of papillomavirus E2 protein with the Brm chromatin remodeling complex leads to enhanced transcriptional activation.Journal of virology · 2007Article
- Bromodomain protein 4 mediates the papillomavirus E2 transcriptional activation function.Journal of virology · 2006Article
- Interaction of bovine papillomavirus E2 protein with Brd4 stabilizes its association with chromatin.Journal of virology · 2005Article
- Direct interaction between nucleosome assembly protein 1 and the papillomavirus E2 proteins involved in activation of transcription.Molecular and cellular biology · 2004Article
- Analysis of chromatin attachment and partitioning functions of bovine papillomavirus type 1 E2 protein.Journal of virology · 2004Article
- The Papillomavirus E2 protein binds to and synergizes with C/EBP factors involved in keratinocyte differentiation.Journal of virology · 2003Article
- Cooperative activation of human papillomavirus type 8 gene expression by the E2 protein and the cellular coactivator p300.Journal of virology · 2002Article
- Induction of the bovine papillomavirus origin "onion skin"-type DNA replication at high E1 protein concentrations in vivo.Journal of virology · 2002Article
- Mapping the sequences that mediate interaction of the equine herpesvirus 1 immediate-early protein and human TFIIB.Journal of virology · 2001Article
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Authors and funding
3 authors.
Funding
Abstract
Induction of gene expression by the papillomavirus E2 protein requires its approximately 220-amino-acid amino-terminal transactivation domain (TAD) to interact with cellular factors that lead to formation of an activated RNA polymerase complex. These interaction partners have yet to be identified and characterized. The E2 protein localizes the transcription complex to the target promoter through its carboxy-terminal sequence-specific DNA binding domain. This domain has been reported to bind the basal transcription factors TATA-binding protein and TFIIB. We present evidence establishing a direct interaction between amino acids 74 to 134 of the E2 TAD and TFIIB. Within this region, the E2 point mutant N127Y was partially defective and W99C was completely defective for TFIIB binding in vitro, and these mutants displayed reduced or no transcriptional activity, respectively, upon transfection into C33A cells. Overexpression of TFIIB specifically restored transactivation by N127Y to close to wild-type levels, while W99C remained inactive. To further demonstrate the functional interaction of TFIIB with the wild-type E2 TAD, this region was fused to a bacterial DNA binding domain (LexA:E2:1-216). Upon transfection with increasing amounts of LexA:E2:1-216, there was reduction of its transcriptional activity, a phenomenon thought to result from titration of limiting factors, or squelching. Squelching of LexA:E2:1-216, or the wild-type E2 activator, was partially relieved by overexpression of TFIIB. We conclude that a specific region of the E2 TAD functionally interacts with TFIIB.
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