-transparent.png){kind=logo}
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.
Related Publications
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
January 1993,
Proceedings of the National Academy of Sciences of the United States of America,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
April 1993,
Proceedings of the National Academy of Sciences of the United States of America,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
February 1997,
Virology,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
May 1995,
The Journal of general virology,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
June 1993,
Proceedings of the National Academy of Sciences of the United States of America,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
February 1994,
Virology,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
June 1995,
Proceedings of the National Academy of Sciences of the United States of America,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
September 1963,
Nature,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
April 1992,
Journal of virology,
P MacPherson, and
L Thorner, and
L M Parker, and
M Botchan
May 1964,
Nature,
