The initiator protein E1 binds to the bovine papillomavirus origin of replication as a trimeric ring-like structure.
The replication initiator protein E1 binds to the origin of replication of bovine papillomavirus in several forms. E1 can bind to its recognition sequence as a monomer together with the viral transcription factor E2, or as a trimeric E1 complex. The trimerization of E1 is mediated by the sequence-specific binding of E1 to DNA, and results in an E1 complex that is linked topologically to the DNA because the three molecules of E1 form a ring-like structure that encircles the DNA. These results demonstrate that E1 utilizes unusual mechanisms for sequence-specific binding to DNA and for the generation of a structure that encircles the DNA. We believe that these forms of E1 bound to the origin of replication represent intermediates in a transition in the function of E1, from a sequence-specific origin of replication recognition protein to a form of E1 that is competent for the initiation of viral DNA replication.
Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
J
J
Sedman
A
A
Stenlund
D001483:Base Sequence; D004261:DNA Replication; D004279:DNA, Viral / Q000096:biosynthesis* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D018741:Replication Origin; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*
D004279:DNA, Viral; D004268:DNA-Binding Proteins; C069814:E1 protein, Bovine papillomavirus; C051550:E2 protein, Bovine papillomavirus; D014764:Viral Proteins