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Journal of Virology, September 1998, p. 7255-7262, Vol. 72, No. 9
Centre de Recherches de Biochimie
Macromoléculaire,
Received 20 March 1998/Accepted 28 May 1998
We have found that the replicative helicase E1 of bovine
papillomavirus type 1 (BPV-1) interacts with a key cell cycle regulator of S phase, the cyclin E-Cdk2 kinase. The E1 helicase, which interacts with cyclin E and not with Cdk2, presents the highest affinity for
catalytically active kinase complexes. In addition, E1, cyclin E, and
Cdk2 expressed in Xenopus egg extracts are quantitatively coimmunoprecipitated from crude extracts by either anti-Cdk2 or anti-E1
antibodies. E1 protein is also a substrate of the cyclin E-Cdk2 kinase
in vitro. Using the viral components required for in vitro BPV-1
replication and free-membrane cytosol from Xenopus eggs, we
show that efficient replication of BPV plasmids is dependent on the
addition of E1-cyclin E-Cdk2 complexes. Thus, the BPV initiator of
replication and cyclin E-Cdk2 are likely to function together as a
protein complex which may be the key to the cell cycle regulation of
papillomavirus replication.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Functional Interaction between the Bovine
Papillomavirus Virus Type 1 Replicative Helicase E1 and Cyclin
E-Cdk2

*
Corresponding author. Mailing address: Centre de
Recherches de Biochimie Macromoléculaire, CNRS, UPR 1086, 1919 route de Mende, 34293 Montpellier Cedex 5, France. Phone: 33 4 67 61 33 32. Fax: 33 4 67 52 15 59. E-mail:
catherin{at}crbm.cnrs-mop.fr.
Dedicated to the memory of Jean-Claude Cavadore.
Present address: Institut de Génétique
Moléculaire, CNRS, 34033 Montpellier, France.
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