ArticleJournal of virology1998
The carboxyl-terminal region of the human papillomavirus type 16 E1 protein determines E2 protein specificity during DNA replication.
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 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- The E1 proteins.Virology · 2013Review
- Gene- and protein-delivered zinc finger-staphylococcal nuclease hybrid for inhibition of DNA replication of human papillomavirus.PloS one · 2013Article
- Casein kinase II motif-dependent phosphorylation of human papillomavirus E7 protein promotes p130 degradation and S-phase induction in differentiated human keratinocytes.Journal of virology · 2008Article
- Inhibition of DNA replication of human papillomavirus by artificial zinc finger proteins.Journal of virology · 2006Article
- Molecular basis for advances in cervical screening.Molecular diagnosis : a journal devoted to the understanding of human disease through the clinical application of molecular biology · 2005Review
- Human papillomavirus (HPV) origin-binding protein associates with mitotic spindles to enable viral DNA partitioning.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Characterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein.Journal of virology · 2003Article
- Papillomavirus E1 proteins: form, function, and features.Virus genes · 2002Review
- HPV-16 E2 gene disruption and sequence variation in CIN 3 lesions and invasive squamous cell carcinomas of the cervix: relation to numerical chromosome abnormalities.Molecular pathology : MP · 2000Article
- Identification of domains of the human papillomavirus type 11 E1 helicase involved in oligomerization and binding to the viral origin.Journal of virology · 2000Article
- The hinge of the human papillomavirus type 11 E2 protein contains major determinants for nuclear localization and nuclear matrix association.Journal of virology · 2000Article
- Role of the ATP-binding domain of the human papillomavirus type 11 E1 helicase in E2-dependent binding to the origin.Journal of virology · 1999Article
- Human papillomavirus DNA replication compartments in a transient DNA replication system.Journal of virology · 1999Article
- Interaction between cyclin-dependent kinases and human papillomavirus replication-initiation protein E1 is required for efficient viral replication.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- A fifteen-amino-acid peptide inhibits human papillomavirus E1-E2 interaction and human papillomavirus DNA replication in vitro.Journal of virology · 1998Article
- Transcription factor YY1 represses cell-free replication from human papillomavirus origins.Journal of virology · 1998Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The mechanism of DNA replication is conserved among papillomaviruses. The virus-encoded E1 and E2 proteins collaborate to target the origin and recruit host DNA replication proteins. Expression vectors of E1 and E2 proteins support homologous and heterologous papillomaviral origin replication in transiently transfected cells. Viral proteins from different genotypes can also collaborate, albeit with different efficiencies, indicating a certain degree of specificity in E1-E2 interactions. We report that, in the assays of our study, the human papillomavirus type 11 (HPV-11) E1 protein functioned with the HPV-16 E2 protein, whereas the HPV-16 E1 protein exhibited no detectable activity with the HPV-11 E2 protein. Taking advantage of this distinction, we used chimeric E1 proteins to delineate the E1 protein domains responsible for this specificity. Hybrids containing HPV-16 E1 amino-terminal residues up to residue 365 efficiently replicated either viral origin in the presence of either E2 protein. The reciprocal hybrids containing amino-terminal HPV-11 sequences exhibited a high activity with HPV-16 E2 but no activity with HPV-11 E2. Reciprocal hybrid proteins with the carboxyl-terminal 44 residues from either E1 had an intermediate property, but both collaborated more efficiently with HPV-16 E2 than with HPV-11 E2. In contrast, chimeras with a junction in the putative ATPase domain showed little or no activity with either E2 protein. We conclude that the E1 protein consists of distinct structural and functional domains, with the carboxyl-terminal 284 residues of the HPV-16 E1 protein being the primary determinant for E2 specificity during replication, and that chimeric exchanges in or bordering the ATPase domain inactivate the protein.
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