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.

[1]  S. Holt,et al.  Mutational analysis of the 18-base-pair inverted repeat element at the bovine papillomavirus origin of replication: identification of critical sequences for E1 binding and in vivo replication , 1995, Journal of virology.

[2]  John Kuriyan,et al.  Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA , 1994, Cell.

[3]  T. Gillette,et al.  Induction of structural changes in the bovine papillomavirus type 1 origin of replication by the viral E1 and E2 proteins. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[4]  J. Hurwitz,et al.  The bovine papillomavirus E2 protein modulates the assembly of but is not stably maintained in a replication-competent multimeric E1-replication origin complex. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[5]  M. O’Donnell,et al.  An explanation for lagging strand replication: Polymerase hopping among DNA sliding clamps , 1994, Cell.

[6]  S. West,et al.  The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[7]  S. Holt,et al.  DNA binding specificity of the bovine papillomavirus E1 protein is determined by sequences contained within an 18-base-pair inverted repeat element at the origin of replication , 1994, Journal of virology.

[8]  M. Yaniv,et al.  The bovine papillomavirus type 1 (BPV1) replication protein E1 modulates transcriptional activation by interacting with BPV1 E2 , 1994, Journal of virology.

[9]  J. Kuriyan,et al.  Sliding clamps of DNA polymerases. , 1993, Journal of molecular biology.

[10]  P. Burgers,et al.  ATP-independent loading of the proliferating cell nuclear antigen requires DNA ends. , 1993, The Journal of biological chemistry.

[11]  J. Hurwitz,et al.  Bovine papilloma virus (BPV)-encoded E2 protein enhances binding of E1 protein to the BPV replication origin. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[12]  M. Ustav,et al.  The bovine papillomavirus origin of replication requires a binding site for the E2 transcriptional activator. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[13]  J. Hurwitz,et al.  Bovine papilloma virus (BPV)-encoded E1 protein contains multiple activities required for BPV DNA replication. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[14]  D. Latchman,et al.  Transcription factors : a practical approach , 1993 .

[15]  J. Schweizer,et al.  Simian virus 40 T-antigen DNA helicase is a hexamer which forms a binary complex during bidirectional unwinding from the viral origin of DNA replication , 1992, Journal of virology.

[16]  M. Ustav,et al.  Identification of the origin of replication of bovine papillomavirus and characterization of the viral origin recognition factor E1. , 1991, The EMBO journal.

[17]  M. Botchan,et al.  Activation of BPV-1 replication in vitro by the transcription factor E2 , 1991, Nature.

[18]  J. Ludes-Meyers,et al.  A bovine papillomavirus E1-related protein binds specifically to bovine papillomavirus DNA , 1991, Journal of virology.

[19]  M. Lusky,et al.  Formation of the complex of bovine papillomavirus E1 and E2 proteins is modulated by E2 phosphorylation and depends upon sequences within the carboxyl terminus of E1. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[20]  M. Ustav,et al.  Transient replication of BPV‐1 requires two viral polypeptides encoded by the E1 and E2 open reading frames. , 1991, The EMBO journal.

[21]  J. Hayes,et al.  Hydroxyl radical footprinting. , 1991, Methods in enzymology.

[22]  F. Dean,et al.  Binding and unwinding—How T antigen engages the SV40 origin of DNA replication , 1990, Cell.

[23]  P. Hough,et al.  ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication , 1989, Nature.

[24]  M. Scheffner,et al.  Sequence independent duplex DNA opening reaction catalysed by SV40 large tumor antigen. , 1989, Nucleic acids research.

[25]  F. Dean,et al.  Unwinding of duplex DNA from the SV40 origin of replication by T antigen. , 1987, Science.

[26]  D. Lowy,et al.  Bovine papillomavirus E2 trans-activating gene product binds to specific sites in papillomavirus DNA , 1987, Nature.