Affiliation:
1. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724,1 and
2. Graduate Program in Genetics, Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook, Stony Brook, New York 117942
Abstract
ABSTRACT
The bovine papillomavirus replication initiator protein E1 is an origin of replication (
ori
)-binding protein absolutely required for viral DNA replication. In the presence of the viral transcription factor E2, E1 binds to the
ori
and initiates DNA replication. To understand how the E1 initiator recognizes the
ori
and how E2 assists in this process, we have expressed and purified a 166-amino-acid fragment which corresponds to the minimal E1 DNA-binding domain (DBD). DNA binding studies using this protein demonstrate that the E1 DBD can bind to the palindromic E1 binding site in several forms but that binding of two monomers, each recognizing one half-site of the E1 palindrome, is the predominant form. This is reminiscent of the binding of the T-antigen DBD to the SV40
ori
, and interestingly, the arrangement of E1 binding sites shows striking similarities to the arrangement of T-antigen binding sites in the SV40
ori
even though the recognition sequences are unrelated. The E1 DBD is capable of interacting cooperatively with E2; however, the E2 DBD and not the E2 activation domain mediates this interaction. Furthermore, the E2 DBD stimulates binding of two monomers of the E1 DBD to the
ori
by binding cooperatively with one E1 monomer. Finally, we show that our results concerning the DNA-binding properties of the E1 DBD can be extended to full-length E1.
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Cited by
78 articles.
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