Separate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding.

@article{Gillitzer2000SeparateDI,
  title={Separate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding.},
  author={Eric Gillitzer and G. T. Chen and Arne Stenlund},
  journal={The EMBO journal},
  year={2000},
  volume={19 12},
  pages={3069-79}
}
The E1 and E2 proteins from bovine papillomavirus bind cooperatively to binding sites in the viral origin of DNA replication. The DNA-binding domains (DBDs) of the two proteins interact with each other, and the E2 transactivation domain interacts with the helicase domain of E1. Mutations that disrupt the interaction between the two DBDs also disrupt the interaction between the E2 activation domain and the E1 helicase domain, demonstrating interdependence of the two interactions. Cooperative… CONTINUE READING

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