Journal
EMBO JOURNAL
Volume 19, Issue 12, Pages 3069-3079Publisher
OXFORD UNIV PRESS
DOI: 10.1093/emboj/19.12.3069
Keywords
cooperative binding; DNA bending; papillomavirus
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Funding
- NCI NIH HHS [CA13106, P01 CA013106] Funding Source: Medline
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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 binding of the two DBDs generates a sharp bend in the DNA that is required for interaction between the E2 activation domain and E1. This indicates that interaction between the two DBDs plays an architectural role, 'triggering' a productive interaction between the E2 transactivation domain and E1 through introduction of a sharp bend in the DNA. This two-step mechanism may be a required feature for cooperative DNA binding to proximal binding sites.
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