4.6 Article

Papillomavirus E1 protein binds to and stimulates human topoisomerase I

Journal

JOURNAL OF VIROLOGY
Volume 80, Issue 3, Pages 1584-1587

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.80.3.1584-1587.2006

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Funding

  1. NIAID NIH HHS [AI 07614, T32 AI007614] Funding Source: Medline
  2. NIGMS NIH HHS [R29 GM 56406, R29 GM056406] Funding Source: Medline

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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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