Open AccessPapillomavirus E1 Protein Binds to and Stimulates Human Topoisomerase I
Author(s) -
Randolph V. Clower,
John D. Fisk,
Thomas Melendy
Publication year - 2006
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.80.3.1584-1587.2006
Subject(s) - biology , topoisomerase , dna replication , helicase , dna polymerase , ter protein , microbiology and biotechnology , primase , replication factor c , eukaryotic dna replication , replication protein a , dna , genetics , dna binding protein , gene , reverse transcriptase , transcription factor , rna
The papillomavirus (PV) E1 helicase plays a direct role in recruiting cellular DNA replication factors, such as replication protein A or polymerase α-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.