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Journal of Virology, August 2006, p. 7491-7499, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00435-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Surface Mutagenesis of the Bovine Papillomavirus E1 DNA Binding Domain Reveals Residues Required for Multiple Functions Related to DNA Replication

Stephen Schuck and Arne Stenlund*

Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724

Received 3 March 2006/ Accepted 9 May 2006

The E1 protein from papillomaviruses is a multifunctional protein with complex functions required for the initiation of viral DNA replication. We have performed a surface mutagenesis of the well-characterized E1 DNA binding domain (DBD). We demonstrate that substitutions of multiple residues on the surface of the E1 DBD are defective for DNA replication without affecting the DNA binding activity of the protein. The defects of individual substitutions include failure to form the double trimer that melts the ori and failure to form the double hexamer that unwinds the ori. These results demonstrate that the DBD plays an essential role in multiple DNA replication-related processes apart from DNA binding.

* Corresponding author. Mailing address: Cold Spring Harbor Laboratory, 1 Bungtown Road, P.O. Box 100, Cold Spring Harbor, NY 11724. Phone: (516) 367-8407. Fax: (516) 367-8454. E-mail: Stenlund{at}cshl.edu.

Journal of Virology, August 2006, p. 7491-7499, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00435-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Schuck, S., Stenlund, A. (2007). ATP-Dependent Minor Groove Recognition of TA Base Pairs Is Required for Template Melting by the E1 Initiator Protein. J. Virol. 81: 3293-3302 [Abstract] [Full Text]  


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