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

Gillitzer, E., Chen, G., Stenlund, A. (2000) Separate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding. Embo Journal, 19 (12). pp. 3069-3079. ISSN 0261-4189

URL: https://www.ncbi.nlm.nih.gov/pubmed/10856250
DOI: 10.1093/emboj/19.12.3069

Abstract

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.

Item Type: Paper
Uncontrolled Keywords: cooperative binding DNA bending papillomavirus SITE SPECIFIC RECOMBINATION site specific recombination BOVINE PAPILLOMAVIRUS bovine papillomavirus CRYSTAL STRUCTURE crystal structure COMPLEX FORMATION complex formation TRANSCRIPTIONAL ACTIVATOR transcriptional activator HOMEODOMAIN PROTEINS homeodomain proteins INITIATOR E1 initiator REPLICATION replication REQUIRES ORIGIN origin
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA replication
organism description > virus > papillomavirus
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Stenlund lab
Depositing User: Brian Soldo
Date Deposited: 14 Mar 2012 16:57
Last Modified: 14 Feb 2017 20:16
PMCID: PMC203343
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25188

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