The papillomavirus E1 protein forms a DNA-dependent hexameric complex with ATPase and DNA helicase activities.
The E1 protein from bovine papillomavirus has site-specific DNA binding activity, DNA helicase activity, and DNA-dependent ATPase activity consistent with the properties of an initiator protein. Here we have identified and characterized a novel oligomeric form of E1 that is associated with the ATPase and DNA helicase activities and whose formation is strongly stimulated by single-stranded DNA. This oligomeric form corresponds to a hexamer of E1.
Sedman
J
J
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.
Stenlund
A
A
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D052688:Bovine papillomavirus 1 / Q000378:metabolism*; D002417:Cattle; D004247:DNA / Q000378:metabolism; D004265:DNA Helicases / Q000378:metabolism*; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; C069814:E1 protein, Bovine papillomavirus; D014764:Viral Proteins; D004247:DNA; D000251:Adenosine Triphosphatases; D004265:DNA Helicases