ArticleJournal of virology2008
Dimerization of the papillomavirus E2 protein is required for efficient mitotic chromosome association and Brd4 binding.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Like Brothers in Arms: How Hormonal Stimuli and Changes in the Metabolism Signaling Cooperate, Leading HPV Infection to Drive the Onset of Cervical Cancer.International journal of molecular sciences · 2022Review
- Article
- The Relationship between Estrogen-Related Signaling and Human Papillomavirus Positive Cancers.Pathogens (Basel, Switzerland) · 2020Review
- Hitchhiking of Viral Genomes on Cellular Chromosomes.Annual review of virology · 2019Review
- The SMC5/6 Complex Interacts with the Papillomavirus E2 Protein and Influences Maintenance of Viral Episomal DNA.Journal of virology · 2018Article
- DNA Damage Reduces the Quality, but Not the Quantity of Human Papillomavirus 16 E1 and E2 DNA Replication.Viruses · 2016Article
- Failure to interact with Brd4 alters the ability of HPV16 E2 to regulate host genome expression and cellular movement.Virus research · 2016Article
- Evidence supporting a role for TopBP1 and Brd4 in the initiation but not continuation of human papillomavirus 16 E1/E2-mediated DNA replication.Journal of virology · 2015Article
- Papillomavirus genomes associate with BRD4 to replicate at fragile sites in the host genome.PLoS pathogens · 2014Article
- Current understanding of the role of the Brd4 protein in the papillomavirus lifecycle.Viruses · 2013Review
- Recruitment of Brd4 to the human papillomavirus type 16 DNA replication complex is essential for replication of viral DNA.Journal of virology · 2013Article
- Analysis of the papillomavirus E2 and bromodomain protein Brd4 interaction using bimolecular fluorescence complementation.PloS one · 2013Article
- Hitchhiking on host chromatin: how papillomaviruses persist.Biochimica et biophysica acta · 2012Review
- A point mutation in the DNA-binding domain of HPV-2 E2 protein increases its DNA-binding capacity and reverses its transcriptional regulatory activity on the viral early promoter.BMC molecular biology · 2012Article
- Interaction of the betapapillomavirus E2 tethering protein with mitotic chromosomes.Journal of virology · 2010Article
- The human papillomavirus type 8 E2 tethering protein targets the ribosomal DNA loci of host mitotic chromosomes.Journal of virology · 2009Article
- Replication and partitioning of papillomavirus genomes.Advances in virus research · 2008Review
- Tumor suppressor or oncogene? A critical role of the human papillomavirus (HPV) E2 protein in cervical cancer progression.American journal of cancer researchArticle
- Papillomavirus interaction with cellular chromatin.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The E2 proteins of several papillomaviruses link the viral genome to mitotic chromosomes to ensure retention and the efficient partitioning of genomes into daughter cells following cell division. Bovine papillomavirus type 1 E2 binds to chromosomes in a complex with Brd4, a cellular bromodomain protein. Interaction with Brd4 is also important for E2-mediated transcriptional regulation. The transactivation domain of E2 is crucial for interaction with the Brd4 protein; proteins lacking or mutated in this domain do not interact with Brd4. However, we found that the C-terminal DNA binding/dimerization domain of E2 is also required for efficient binding to Brd4. Mutations that eliminated the DNA binding function of E2 had no effect on the ability of E2 to interact with Brd4, but an E2 protein with a mutation that disrupted C-terminal dimerization bound Brd4 with greatly reduced efficiency. Furthermore, E2 proteins in which the C-terminal domains were replaced with the dimeric DNA binding domain of EBNA-1 or Gal4 bound efficiently to the Brd4 protein, but the replacement of the E2 C-terminal domain with a monomeric red fluorescent protein did not rescue efficient Brd4 binding. Thus, E2 bound to Brd4 most efficiently as a dimer. To prove this finding further, the E2 DNA binding domain was replaced with an FKBP12-derived domain in which dimerization was regulated by a bivalent ligand. This fusion protein bound Brd4 efficiently only in the presence of the ligand, confirming that a dimer of E2 was required. Correspondingly, E2 proteins that could dimerize were able to bind to mitotic chromosomes much more efficiently than monomeric E2 polypeptides.
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