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Journal of Virology, July 2005, p. 8661-8664, Vol. 79, No. 13
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.13.8661-8664.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Role of Papillomavirus E1 Initiator Dimerization in DNA Replication

Stephen Schuck and Arne Stenlund*

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

Received 8 November 2004/ Accepted 4 February 2005

Viral initiator proteins are polypeptides that form oligomeric complexes on the origin of DNA replication (ori). These complexes carry out a multitude of functions related to initiation of DNA replication, and although many of these functions have been characterized biochemically, little is understood about how the complexes are assembled. Here we demonstrate that loss of one particular interaction, the dimerization between E1 DNA binding domains, has a severe effect on DNA replication in vivo but has surprisingly modest effects on most individual biochemical activities in vitro. We conclude that the dimer interaction is primarily required for initial recognition of ori.

* 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, July 2005, p. 8661-8664, Vol. 79, No. 13
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.13.8661-8664.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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