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Research paper thumbnail of Downloaded from www.microbiologyresearch.org by

Bovine papillomavirus type 1 E1 ATPase activity does not depend on

Research paper thumbnail of Etude des proprietes biochimiques d'une proteine virale essentielle pour la replication du papillomavirus bovin de type 1

L'essentiel de nos connaissances, concernant les mecanismes moleculaires mis en jeu lors de l... more L'essentiel de nos connaissances, concernant les mecanismes moleculaires mis en jeu lors de la replication de l'adn chez les eucaryotes, repose sur l'etude de la replication de petits virus a adn. Parmi ces virus, le papillomavirus bovin de type 1 (bpv1), qui est capable de transformer in vitro des fibroblastes de rongeurs, presente la particularite de maintenir ses genomes viraux (molecules d'adn circulaires et autonomes) en nombre constant au cours des generations cellulaires successives. Lorsque nous avons commence le travail presente dans cette these, differentes analyses genetiques suggeraient que le produit de traduction de l'orf e1 de bpv1 etait directement implique dans la replication virale. Nos travaux ont permis d'identifier et d'avancer la caracterisation de la proteine codee par l'orf e1. Cette phosphoproteine de 72 kda est presente en faible quantite dans le noyau des cellules transformees par bpv1. Afin de caracteriser les activites bio...

Research paper thumbnail of Etude des proprietes biochimiques d'une proteine virale essentielle pour la replication du papillomavirus bovin de type 1

Research paper thumbnail of Bovine Papillomavirus E1 Protein Can, by Itself, Efficiently Drive Multiple Rounds of DNA Synthesis In Vitro

Bovine papillomavirus E1 protein was found to be as efficient as the simian virus 40 large T anti... more Bovine papillomavirus E1 protein was found to be as efficient as the simian virus 40 large T antigen in initiating DNA synthesis in a cell-free system derived from COS1 cells. Multiple rounds of DNA synthesis occur, initiated at the bovine papillomavirus type 1 origin. Therefore, E1 functions in vitro as a lytic virus initiator.

Research paper thumbnail of Bovine Papillomavirus (BPV1) Replication Protein E1: Associated ATPase and Binding to the Viral E2 Transactivator

DNA Replication: The Regulatory Mechanisms, 1992

Research paper thumbnail of Bovine papillomavirus type 1 E1 ATPase activity does not depend on binding to DNA nor to viral E2 protein

The Journal of general virology, 1995

Replication of bovine papillomavirus type 1 (BPV-1) DNA has been shown to require two viral prote... more Replication of bovine papillomavirus type 1 (BPV-1) DNA has been shown to require two viral proteins known to interact in a molecular complex: E2, a transcription activator, and E1, another nuclear phosphoprotein, which binds to the replication origin and for which helicase/ATPase activities have previously been reported. Here we characterize the BPV-1 E1 ATPase activity. In contrast to Seo et al. (Proceedings of the National Academy of Sciences, USA, 90, 702-706, 1993), we were able to detect this activity in the absence of nucleic acid in partially purified preparations of either E1 protein or of E1-E2 protein complex. Measurements of specific activity and kinetic parameters gave similar values for preparations of various kinds. ATPase activity was quantitatively retained by immunoprecipitates obtained by using anti-E1 or, in the case of E1-E2 complex, anti-E2 antibodies. Significantly, preparations of bacterially expressed glutathione S-transferase-E1 fusion protein exhibited lev...

Research paper thumbnail of Downloaded from www.microbiologyresearch.org by

Bovine papillomavirus type 1 E1 ATPase activity does not depend on

Research paper thumbnail of Etude des proprietes biochimiques d'une proteine virale essentielle pour la replication du papillomavirus bovin de type 1

L'essentiel de nos connaissances, concernant les mecanismes moleculaires mis en jeu lors de l... more L'essentiel de nos connaissances, concernant les mecanismes moleculaires mis en jeu lors de la replication de l'adn chez les eucaryotes, repose sur l'etude de la replication de petits virus a adn. Parmi ces virus, le papillomavirus bovin de type 1 (bpv1), qui est capable de transformer in vitro des fibroblastes de rongeurs, presente la particularite de maintenir ses genomes viraux (molecules d'adn circulaires et autonomes) en nombre constant au cours des generations cellulaires successives. Lorsque nous avons commence le travail presente dans cette these, differentes analyses genetiques suggeraient que le produit de traduction de l'orf e1 de bpv1 etait directement implique dans la replication virale. Nos travaux ont permis d'identifier et d'avancer la caracterisation de la proteine codee par l'orf e1. Cette phosphoproteine de 72 kda est presente en faible quantite dans le noyau des cellules transformees par bpv1. Afin de caracteriser les activites bio...

Research paper thumbnail of Etude des proprietes biochimiques d'une proteine virale essentielle pour la replication du papillomavirus bovin de type 1

Research paper thumbnail of Bovine Papillomavirus E1 Protein Can, by Itself, Efficiently Drive Multiple Rounds of DNA Synthesis In Vitro

Bovine papillomavirus E1 protein was found to be as efficient as the simian virus 40 large T anti... more Bovine papillomavirus E1 protein was found to be as efficient as the simian virus 40 large T antigen in initiating DNA synthesis in a cell-free system derived from COS1 cells. Multiple rounds of DNA synthesis occur, initiated at the bovine papillomavirus type 1 origin. Therefore, E1 functions in vitro as a lytic virus initiator.

Research paper thumbnail of Bovine Papillomavirus (BPV1) Replication Protein E1: Associated ATPase and Binding to the Viral E2 Transactivator

DNA Replication: The Regulatory Mechanisms, 1992

Research paper thumbnail of Bovine papillomavirus type 1 E1 ATPase activity does not depend on binding to DNA nor to viral E2 protein

The Journal of general virology, 1995

Replication of bovine papillomavirus type 1 (BPV-1) DNA has been shown to require two viral prote... more Replication of bovine papillomavirus type 1 (BPV-1) DNA has been shown to require two viral proteins known to interact in a molecular complex: E2, a transcription activator, and E1, another nuclear phosphoprotein, which binds to the replication origin and for which helicase/ATPase activities have previously been reported. Here we characterize the BPV-1 E1 ATPase activity. In contrast to Seo et al. (Proceedings of the National Academy of Sciences, USA, 90, 702-706, 1993), we were able to detect this activity in the absence of nucleic acid in partially purified preparations of either E1 protein or of E1-E2 protein complex. Measurements of specific activity and kinetic parameters gave similar values for preparations of various kinds. ATPase activity was quantitatively retained by immunoprecipitates obtained by using anti-E1 or, in the case of E1-E2 complex, anti-E2 antibodies. Significantly, preparations of bacterially expressed glutathione S-transferase-E1 fusion protein exhibited lev...

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