Sedman, J., Stenlund, A. (September 1996) The initiator protein E1 binds to the bovine papillomavirus origin of replication as a trimeric ring-like structure. Embo J, 15 (18). pp. 5085-92. ISSN 0261-4189 (Print)
Abstract
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.
Item Type: | Paper |
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Uncontrolled Keywords: | Base Sequence DNA Replication DNA Viral biosynthesis metabolism DNA Binding Proteins chemistry metabolism Molecular Sequence Data Molecular Weight Protein Conformation Replication Origin Research Support US Govt PHS Structure Activity Relationship Viral Proteins chemistry metabolism |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA replication bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein diseases & disorders > viral diseases > human papillomavirus |
CSHL Authors: | |
Communities: | CSHL labs > Stenlund lab |
Depositing User: | Brian Soldo |
Date: | 16 September 1996 |
Date Deposited: | 15 Mar 2012 15:25 |
Last Modified: | 14 Feb 2017 20:29 |
PMCID: | PMC452248 |
URI: | https://repository.cshl.edu/id/eprint/25196 |
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