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Journal of Virology, February 2006, p. 1584-1587, Vol. 80, No. 3
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.3.1584-1587.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Papillomavirus E1 Protein Binds to and Stimulates Human Topoisomerase I

Randolph V. Clower, John C. Fisk, and Thomas Melendy*

University at Buffalo, Department of Microbiology and Immunology and Witebsky Center for Microbial Pathogenesis, 210 Biomedical Research Building, School of Medicine and Biomedical Sciences, Buffalo, New York 14214

Received 21 September 2005/ Accepted 8 November 2005

The papillomavirus (PV) E1 helicase plays a direct role in recruiting cellular DNA replication factors, such as replication protein A or polymerase {alpha}-primase, to replicate PV genomes. Here, E1 is shown to bind to human topoisomerase I and stimulate its relaxation activity up to sevenfold. The interaction between E1 and topoisomerase I was mapped to the E1 DNA binding domain and C terminus. These findings imply a mechanism for the recruitment of topoisomerase I to PV DNA replication forks and for stimulating topoisomerase I to allow for efficient relaxation of the torsional stress induced by replication fork progression.

* Corresponding author. Mailing address: University at Buffalo, Department of Microbiology & Immunology, The School of Medicine and Biomedical Sciences, 213 Biomedical Research Building, 3435 Main Street, Buffalo, NY 14214. Phone: (716) 829-3789. Fax: (716) 829-2158. E-mail: TMelendy{at}buffalo.edu.

Journal of Virology, February 2006, p. 1584-1587, Vol. 80, No. 3
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.3.1584-1587.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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