The transactivation and DNA binding domains of the BPV-1 E2 protein have different roles in cooperative origin binding with the E1 protein.
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Summary
The studies indicate that the E2 transactivation domain is sufficient for interaction with the E1 protein and that theE2 DNA binding domain is required for interactionWith origin DNA sequences.
- Type
- article
- Published
- 1996-07-01
- Cited by
- 37
- References
- 1
- Access
- Open access
- OpenAlex
- https://openalex.org/W2072456482
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:40357189
Keywords
Transactivation, Biology, SeqA protein domain, Binding domain, HMG-box
References
Cited by
- Replication and partitioning of papillomavirus genomes.
- Functional interactions between papillomavirus E1 and E2 proteins
- Amino acids critical for the functions of the bovine papillomavirus type 1 E2 transactivator
- Functional interaction of a novel cellular protein with the papillomavirus E2 transactivation domain
- The determinants for the native activities of the bovine papillomavirus type 1 E2 protein are separable
- Mechanism and Requirements for Bovine Papillomavirus, Type 1, E1 Initiator Complex Assembly Promoted by the E2 Transcription Factor Bound to Distal Sites*
- Hydrophobic residue contributions to sequence-specific DNA binding by the bovine papillomavirus helicase E1.
- Identification of single amino acids in the human papillomavirus 11 E2 protein critical for the transactivation or replication functions.
- Regulation of human papillomavirus type 1 replication by the viral E2 protein.
- The bovine papillomavirus E2 transactivator is stimulated by the E1 initiator through the E2 activation domain.
- Reconstitution of papillomavirus E2-mediated plasmid maintenance in Saccharomyces cerevisiae by the Brd4 bromodomain protein.
- Common determinants in DNA melting and helicase-catalysed DNA unwinding by papillomavirus replication protein E1
- The Papillomavirus E2 Proteins
- Replication of a chimeric origin containing elements from Epstein-Barr virus ori P and bovine papillomavirus minimal origin.
- Two distinct regions of the BPV1 E1 replication protein interact with the activation domain of E2.
- An acidic amphipathic helix in the Bovine Papillomavirus E2 protein is critical for DNA replication and interaction with the E1 protein.
- Interaction of the papillomavirus E2 protein with mitotic chromosomes.
- The Mitotic Chromosome Binding Activity of the Papillomavirus E2 Protein Correlates with Interaction with the Cellular Chromosomal Protein, Brd4
- Two Patches of Amino Acids on the E2 DNA Binding Domain Define the Surface for Interaction with E1
- Purification and biochemical characterization of the E1 replication initiation protein of the cutaneous human papillomavirus type 1.
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