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Updated: Aug 13, 2026

In situ Subcellular Fractionation of Adherent and Non-adherent Mammalian Cells
Published on: July 23, 2010
Papillomavirus E1 protein binds to and stimulates human topoisomerase I
Randolph V Clower1, John C Fisk, Thomas Melendy
1Department of Microbiology & Immunology, The School of Medicine and Biomedical Sciences, University at Buffalo, 213 Biomedical Research Building, 3435 Main Street, Buffalo, NY 14214, USA.
Abstract:
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.
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