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Journal of Virology, February 2000, p. 1506-1512, Vol. 74, No. 3
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Two Patches of Amino Acids on the E2 DNA Binding Domain Define the Surface for Interaction with E1

Grace Chen1,2 and Arne Stenlund1,*

Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724,1 and Graduate Program in Genetics, Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook, Stony Brook, New York 117942

Received 9 August 1999/Accepted 2 November 1999

The E1 and E2 proteins from bovine papillomavirus bind cooperatively to the viral origin of DNA replication (ori), forming a complex which is essential for initiation of DNA replication. Cooperative binding has two components, in which (i) the DNA binding domains (DBDs) of the two proteins interact with each other and (ii) the E2 transactivation domain interacts with the helicase domain of E1. By generating specific point mutations in the DBD of E2, we have defined two patches of amino acids that are involved in the interaction with the E1 DBD. These same mutations, when introduced into the viral genome, result in severely reduced replication of the viral genome, as well as failure to transform mouse cells in tissue culture. Thus, the interaction between the E1 and E2 DBDs is important for the establishment of the viral genome as an episome and most likely contributes to the formation of a preinitiation complex on the viral ori.

* Corresponding author. Mailing address: Cold Spring Harbor Laboratory, P.O. Box 100, Cold Spring Harbor, NY 11724. Phone: (516) 367-8407. Fax: (516) 367-8454. E-mail: stenlund{at}cshl.org.

Journal of Virology, February 2000, p. 1506-1512, Vol. 74, No. 3
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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