The bovine papilloma virus E1 protein has ATPase activity essential to viral DNA replication and efficient transformation in cells.
The bovine papilloma virus (BPV) E1 protein essential to viral DNA replication has recently been shown to associate via direct protein-DNA interactions with the viral origin of replication and to be an ATP-dependent helicase. We show here that in accordance with the latter function, the E1 gene product has intrinsic ATPase activity. Mutations placed throughout the nucleotide binding consensus element abolish the ATPase activity of E1 and render BPV genomes harboring such mutations defective for episomal replication and impaired for oncogenic transformation.
MacPherson
P
P
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Thorner
L
L
Parker
L M
LM
Botchan
M
M
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D001483:Base Sequence; D001665:Binding Sites; D052688:Bovine papillomavirus 1 / Q000201:enzymology* / Q000502:physiology; D002417:Cattle; D002460:Cell Line; D002471:Cell Transformation, Neoplastic; D002472:Cell Transformation, Viral; D016384:Consensus Sequence; D004261:DNA Replication / Q000502:physiology*; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D009036:Moths; D009154:Mutation; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D014779:Virus Replication / Q000502:physiology
D004268:DNA-Binding Proteins; C069814:E1 protein, Bovine papillomavirus; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; D000251:Adenosine Triphosphatases