title: Role of papillomavirus E1 initiator dimerization in DNA replication.
abstract: Viral initiator proteins are polypeptides that form oligomeric complexes on the origin of DNA replication (ori). These complexes carry out a multitude of functions related to initiation of DNA replication, and although many of these functions have been characterized biochemically, little is understood about how the complexes are assembled. Here we demonstrate that loss of one particular interaction, the dimerization between E1 DNA binding domains, has a severe effect on DNA replication in vivo but has surprisingly modest effects on most individual biochemical activities in vitro. We conclude that the dimer interaction is primarily required for initial recognition of ori.
authors.affiliation: Cold Spring Harbor Laboratory, 1 Bungtown Road, P.O. Box 100, Cold Spring Harbor, New York 11724, USA.
authors.forename: Stephen
authors.initials: S
authors.lastname: Schuck
authors.forename: Arne
authors.initials: A
authors.lastname: Stenlund
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D052688:Bovine papillomavirus 1 / Q000235:genetics*; D002417:Cattle; D004261:DNA Replication; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D027383:Papillomaviridae / Q000235:genetics*; D011994:Recombinant Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism
chemical_list: D004268:DNA-Binding Proteins; C069814:E1 protein, Bovine papillomavirus; D011994:Recombinant Proteins; D014764:Viral Proteins