Premium
Separate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding
Author(s) -
Gillitzer Eric,
Chen Grace,
Stenlund Arne
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.12.3069
Subject(s) - biology , dna , dna binding protein , computational biology , plasma protein binding , evolutionary biology , genetics , microbiology and biotechnology , transcription factor , gene
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.