The Papillomavirus E1 Protein Forms a DNA-Dependent Hexameric Complex with ATPase and DNA Helicase Activities

ABSTRACT The E1 protein from bovine papillomavirus has site-specific DNA binding activity, DNA helicase activity, and DNA-dependent ATPase activity consistent with the properties of an initiator protein. Here we have identified and characterized a novel oligomeric form of E1 that is associated with the ATPase and DNA helicase activities and whose formation is strongly stimulated by single-stranded DNA. This oligomeric form corresponds to a hexamer of E1.

[1]  P. Lambert,et al.  Bovine papillomavirus type 1 E1 and simian virus 40 large T antigen share regions of sequence similarity required for multiple functions , 1997, Journal of virology.

[2]  A. Stenlund,et al.  Binding of the E1 and E2 proteins to the origin of replication of bovine papillomavirus , 1997, Journal of virology.

[3]  A. Stenlund 23 Papillomavirus DNA Replication , 1996 .

[4]  K. Bjornson,et al.  Mechanisms of helicase-catalyzed DNA unwinding. , 1996, Annual review of biochemistry.

[5]  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.

[6]  M. Jezewska,et al.  Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer. , 1995, Biochemistry.

[7]  E. Egelman,et al.  Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[8]  C. Bonne-Andrea,et al.  Bovine papillomavirus E1 protein binds specifically DNA polymerase alpha but not replication protein A , 1995, Journal of virology.

[9]  M. Jezewska,et al.  Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein. , 1994, The Journal of biological chemistry.

[10]  M. Botchan,et al.  The bovine papilloma virus E1 protein has ATPase activity essential to viral DNA replication and efficient transformation in cells. , 1994, Virology.

[11]  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.

[12]  M. Botchan,et al.  The cellular DNA polymerase alpha-primase is required for papillomavirus DNA replication and associates with the viral E1 helicase. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[13]  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.

[14]  T. R. Broker,et al.  Papillomavirus DNA replication. , 1994, Intervirology.

[15]  M. Hingorani,et al.  Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs. , 1993, Biochemistry.

[16]  M. Botchan,et al.  DNA-binding domain of bovine papillomavirus type 1 E1 helicase: structural and functional aspects , 1993, Journal of virology.

[17]  M. Botchan,et al.  The E1 protein of bovine papilloma virus 1 is an ATP-dependent DNA helicase. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[18]  J. Hurwitz,et al.  Isolation of helicase alpha, a DNA helicase from HeLa cells stimulated by a fork structure and signal-stranded DNA-binding proteins. , 1993, The Journal of biological chemistry.

[19]  M. Hingorani,et al.  Oligomeric structure of bacteriophage T7 DNA primase/helicase proteins. , 1993, The Journal of biological chemistry.

[20]  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.

[21]  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.

[22]  E. Fanning,et al.  Structure and function of simian virus 40 large tumor antigen. , 1992, Annual review of biochemistry.

[23]  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.

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

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

[26]  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.

[27]  P. Tegtmeyer,et al.  Three domains in the simian virus 40 core origin orchestrate the binding, melting, and DNA helicase activities of T antigen , 1990, Journal of virology.

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

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

[30]  J. Hurwitz,et al.  Localized melting and structural changes in the SV40 origin of replication induced by T‐antigen. , 1988, The EMBO journal.

[31]  I. Seif,et al.  A common function for polyoma virus large-T and papillomavirus E1 proteins? , 1984, Nature.

[32]  J. Hurwitz,et al.  Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro. , 1975, Proceedings of the National Academy of Sciences of the United States of America.