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Volumn 70, Issue 7, 1996, Pages 4193-4199

Genetic analysis of the activation domain of bovine papillomavirus protein E2: Its role in transcription and replication

Author keywords

[No Author keywords available]

Indexed keywords

HELICASE; TRANSCRIPTION FACTOR; VIRUS PROTEIN;

EID: 0029903007     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.7.4193-4199.1996     Document Type: Article
Times cited : (63)

References (47)
  • 1
    • 0028020032 scopus 로고
    • Targeting of DNA polymerase to the adenovirus origin of DNA replication by interaction with nuclear factor 1
    • Armentero, M., M. Horwitz, and N. Mermod. 1994. Targeting of DNA polymerase to the adenovirus origin of DNA replication by interaction with nuclear factor 1. Proc. Natl. Acad. Sci. USA 91:11537-11541.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11537-11541
    • Armentero, M.1    Horwitz, M.2    Mermod, N.3
  • 2
    • 0029073168 scopus 로고
    • Amino-terminal domains of the bovine papillomavirus type I E1 and E2 proteins participate in complex formation
    • Benson, J. D., and P. M. Howley. 1995. Amino-terminal domains of the bovine papillomavirus type I E1 and E2 proteins participate in complex formation. J. Virol. 69:4364-4372.
    • (1995) J. Virol. , vol.69 , pp. 4364-4372
    • Benson, J.D.1    Howley, P.M.2
  • 3
    • 0029656196 scopus 로고    scopus 로고
    • Amino acids critical for the functions of the bovine papillomavirus type 1 E2 transactivator
    • Brokaw, J. L., M. Blanco, and A. McBride. 1996. Amino acids critical for the functions of the bovine papillomavirus type 1 E2 transactivator. J. Virol. 70:23-29.
    • (1996) J. Virol. , vol.70 , pp. 23-29
    • Brokaw, J.L.1    Blanco, M.2    McBride, A.3
  • 4
    • 0025187879 scopus 로고
    • Protein-protein interactions between adenovirus DNA polymerase and nuclear factor I mediate formation of the DNA replication preinitiation complex
    • Chen, M., N. Mermod, and M. S. Horwitz. 1990. Protein-protein interactions between adenovirus DNA polymerase and nuclear factor I mediate formation of the DNA replication preinitiation complex. J. Biol. Chem. 265:18634-18642.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18634-18642
    • Chen, M.1    Mermod, N.2    Horwitz, M.S.3
  • 5
    • 0026806749 scopus 로고
    • Control of human papillomavirus type 11 origin of replication by the E2 family of regulatory proteins
    • Chiang, C. M., G. Dong, T. R. Broker, and L. T. Chow. 1992. Control of human papillomavirus type 11 origin of replication by the E2 family of regulatory proteins. J. Virol. 66:5224-5231.
    • (1992) J. Virol. , vol.66 , pp. 5224-5231
    • Chiang, C.M.1    Dong, G.2    Broker, T.R.3    Chow, L.T.4
  • 6
    • 0026769936 scopus 로고
    • Viral E1 and E2 proteins support replication of homologous and heterologous papillomaviral origins
    • Chiang, C. M., M. Ustav, A. Stenlund, T. F. Ho, T. R. Broker, and L. T. Chow. 1992. Viral E1 and E2 proteins support replication of homologous and heterologous papillomaviral origins. Proc. Natl. Acad. Sci. USA 89:5799-5803.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5799-5803
    • Chiang, C.M.1    Ustav, M.2    Stenlund, A.3    Ho, T.F.4    Broker, T.R.5    Chow, L.T.6
  • 7
    • 0024556457 scopus 로고
    • Bovine papillomavirus type 1 encodes two forms of a transcriptional repressor: Structural and functional analysis of new viral cDNAs
    • Choe, J., P. Vaillancourt, A. Stenlund, and M. Botchan. 1989. Bovine papillomavirus type 1 encodes two forms of a transcriptional repressor: structural and functional analysis of new viral cDNAs. J. Virol. 63:1743-1755.
    • (1989) J. Virol. , vol.63 , pp. 1743-1755
    • Choe, J.1    Vaillancourt, P.2    Stenlund, A.3    Botchan, M.4
  • 10
    • 0023993334 scopus 로고
    • Bovine papillomavirus mutant temperature sensitive for transformation, replication, and transactivation
    • DiMaio, D., and J. Settleman. 1988. Bovine papillomavirus mutant temperature sensitive for transformation, replication, and transactivation. EMBO J. 7:1197-1204.
    • (1988) EMBO J. , vol.7 , pp. 1197-1204
    • Dimaio, D.1    Settleman, J.2
  • 11
    • 0342317574 scopus 로고
    • Trans-pliction factors?
    • Dutta, A. 1993. Trans-pliction factors? Curr. Biol. 3:709-711.
    • (1993) Curr. Biol. , vol.3 , pp. 709-711
    • Dutta, A.1
  • 12
    • 0024076907 scopus 로고
    • Structural and mutational analysis of E2 transactivating proteins of papillomaviruses reveals three distinct functional domains
    • Girl, I., and M. Yaniv. 1988. Structural and mutational analysis of E2 transactivating proteins of papillomaviruses reveals three distinct functional domains. EMBO J. 7:2823-2829.
    • (1988) EMBO J. , vol.7 , pp. 2823-2829
    • Girl, I.1    Yaniv, M.2
  • 13
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • Gorman, C. M., L. F. Moffat, and B. H. Howard. 1982. Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol. Cell. Biol. 2:1044-1051.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 1044-1051
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 14
    • 0028107658 scopus 로고
    • Cooperativity in vivo between the E2 transactivator and the TATA box binding protein depends on core promoter structure
    • Ham, J., G. Steger, and M. Yaniv. 1994. Cooperativity in vivo between the E2 transactivator and the TATA box binding protein depends on core promoter structure. EMBO J. 13:147-157.
    • (1994) EMBO J. , vol.13 , pp. 147-157
    • Ham, J.1    Steger, G.2    Yaniv, M.3
  • 15
    • 0028596398 scopus 로고
    • Transcription-coupled repair and human disease
    • Hanawalt, P. C. 1994. Transcription-coupled repair and human disease. Science 266:1957-1958.
    • (1994) Science , vol.266 , pp. 1957-1958
    • Hanawalt, P.C.1
  • 16
    • 0024293554 scopus 로고
    • Sequence-specific and general transcriptional activation by the bovine papillomavirus-1 E2 transactivator requires an N-terminal amphipathic helix-containing E2 domain
    • Haugen, T. H., L. P. Turek, F. M. Mercurio, T. P. Cripe, B. J. Olson, R. D. Anderson, D. Seidl, M. Karin, and J. Schiller. 1988. Sequence-specific and general transcriptional activation by the bovine papillomavirus-1 E2 transactivator requires an N-terminal amphipathic helix-containing E2 domain. EMBO J. 7:4245-4253.
    • (1988) EMBO J. , vol.7 , pp. 4245-4253
    • Haugen, T.H.1    Turek, L.P.2    Mercurio, F.M.3    Cripe, T.P.4    Olson, B.J.5    Anderson, R.D.6    Seidl, D.7    Karin, M.8    Schiller, J.9
  • 17
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain hound to its DNA target
    • Hegde, R. S., S. R. Grossman, L. A. Laimins, and P. B. Sigler. 1992. Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain hound to its DNA target. Nature (London) 359:505-512.
    • (1992) Nature (London) , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 18
    • 0024404111 scopus 로고
    • Bovine papilloma virus encoded E2 activates lymphokine genes through DNA elements, distinct from the consensus motif, in the long control region of its own genome
    • Heike, T., S. Miyatake, M. Yoshida, K. Arai, and N. Arai. 1989. Bovine papilloma virus encoded E2 activates lymphokine genes through DNA elements, distinct from the consensus motif, in the long control region of its own genome. EMBO J. 8:1411-1417.
    • (1989) EMBO J. , vol.8 , pp. 1411-1417
    • Heike, T.1    Miyatake, S.2    Yoshida, M.3    Arai, K.4    Arai, N.5
  • 19
    • 0026871077 scopus 로고
    • Transcription factors and the control of DNA replication
    • Heintz, N. H. 1992. Transcription factors and the control of DNA replication. Curr. Opin. Cell Biol. 4:459-467.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 459-467
    • Heintz, N.H.1
  • 20
    • 0024587891 scopus 로고
    • Functional analysis of the papillomavirus E2 transactivator in Saccharomyces cerevisiae
    • Lambert, P. F., N. Postatni, A. McBride, M. Yaniv, P. M. Howley, and B. Arcangioli. 1989. Functional analysis of the papillomavirus E2 transactivator in Saccharomyces cerevisiae. Genes Dev. 3:38-48.
    • (1989) Genes Dev. , vol.3 , pp. 38-48
    • Lambert, P.F.1    Postatni, N.2    McBride, A.3    Yaniv, M.4    Howley, P.M.5    Arcangioli, B.6
  • 21
    • 0027195936 scopus 로고
    • The acidic transcriptional activation domains of VP16 and p53 bind the cellular replication protein A and stimulate in vitro BPV-1 DNA replication
    • Li, R., and M. R. Botchan. 1993. The acidic transcriptional activation domains of VP16 and p53 bind the cellular replication protein A and stimulate in vitro BPV-1 DNA replication. Cell 73:1207-1221.
    • (1993) Cell , vol.73 , pp. 1207-1221
    • Li, R.1    Botchan, M.R.2
  • 22
    • 0028226007 scopus 로고
    • Acidic transcription factors alleviate nucleosome-mediated repression of BPV-1 DNA replication
    • Li, R., and M. R. Botchan. 1994. Acidic transcription factors alleviate nucleosome-mediated repression of BPV-1 DNA replication. Proc. Natl. Acad. Sci. USA 91:7051-7055.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7051-7055
    • Li, R.1    Botchan, M.R.2
  • 23
    • 0025828042 scopus 로고
    • Direct interaction between Sp1 and the BPV enhancer E2 protein mediates synergistic activation of transcription
    • Li, R., J. D. Knight, S. P. Jackson, R. Tjian, and M. R. Botchan. 1991. Direct interaction between Sp1 and the BPV enhancer E2 protein mediates synergistic activation of transcription. Cell 65:493-505.
    • (1991) Cell , vol.65 , pp. 493-505
    • Li, R.1    Knight, J.D.2    Jackson, S.P.3    Tjian, R.4    Botchan, M.R.5
  • 25
    • 1842367150 scopus 로고
    • E2 polypeptides encoded by bovine papillomavirus 1 form dimers through the carboxy-terminal DNA-binding domain: Transactivation is mediated through the aminoterminal domain
    • McBride, A. A., J. C. Byrne, and P. M. Howley. 1989. E2 polypeptides encoded by bovine papillomavirus 1 form dimers through the carboxy-terminal DNA-binding domain: transactivation is mediated through the aminoterminal domain. Proc. Natl. Acad. Sci. USA 86:510-514.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 510-514
    • McBride, A.A.1    Byrne, J.C.2    Howley, P.M.3
  • 26
    • 0025613266 scopus 로고
    • Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transactivator
    • Mohr, I. J., R. Clark, S. Sun, E. J. Androphy, P. MacPherson, and M. R. Botchan. 1990. Targeting the E1 replication protein to the papillomavirus origin of replication by complex formation with the E2 transactivator. Science 250:1694-1699.
    • (1990) Science , vol.250 , pp. 1694-1699
    • Mohr, I.J.1    Clark, R.2    Sun, S.3    Androphy, E.J.4    MacPherson, P.5    Botchan, M.R.6
  • 27
    • 0022390906 scopus 로고
    • A general method for saturation mutagenesis of clone DNA fragments
    • Myers, R. M., L. S. Lerman, and T. Maniatis. 1985. A general method for saturation mutagenesis of clone DNA fragments. Science 229:242-247.
    • (1985) Science , vol.229 , pp. 242-247
    • Myers, R.M.1    Lerman, L.S.2    Maniatis, T.3
  • 28
    • 0028133256 scopus 로고
    • The cellular DNA polymerase alpha-primase is required for papilloma replication, and it interacts with the viral E1 helicase
    • Park, P., L. Yang, T. Wang, and M. Botchan. 1994. The cellular DNA polymerase alpha-primase is required for papilloma replication, and it interacts with the viral E1 helicase. Proc. Natl. Acad. Sci. USA 91:8700-8704.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8700-8704
    • Park, P.1    Yang, L.2    Wang, T.3    Botchan, M.4
  • 29
    • 8944250776 scopus 로고    scopus 로고
    • Unpublished observations
    • Parker, L., and M. Botchan. Unpublished observations.
    • Parker, L.1    Botchan, M.2
  • 30
    • 0029130075 scopus 로고
    • Bovine papillomavirus type 1 E2 transcriptional regulators directly bind two cellular transcription factors, TFIID and TFIIB
    • Rank, N. M., and P. F. Lambert. 1995. Bovine papillomavirus type 1 E2 transcriptional regulators directly bind two cellular transcription factors, TFIID and TFIIB. J. Virol. 69:6323-6334.
    • (1995) J. Virol. , vol.69 , pp. 6323-6334
    • Rank, N.M.1    Lambert, P.F.2
  • 31
    • 0028977962 scopus 로고
    • Cis-acting components of human papillomavirus (HPV) DNA replication: Linker substitution analysis of the HPV type 11 origin
    • Russell, J., and M. R. Botchan. 1995. cis-acting components of human papillomavirus (HPV) DNA replication: linker substitution analysis of the HPV type 11 origin. J. Virol. 69:651-660.
    • (1995) J. Virol. , vol.69 , pp. 651-660
    • Russell, J.1    Botchan, M.R.2
  • 32
    • 0030069004 scopus 로고    scopus 로고
    • Targeted mutagenesis of the human papillomavirus type 16 E2 transactivation domain reveals separable transcriptional activation and DNA replication functions
    • Sakai, H., T. Yasugi, J. D. Benson, J. J. Dowhanick, and P. M. Howley. 1996. Targeted mutagenesis of the human papillomavirus type 16 E2 transactivation domain reveals separable transcriptional activation and DNA replication functions. J. Virol. 70:1602-1611.
    • (1996) J. Virol. , vol.70 , pp. 1602-1611
    • Sakai, H.1    Yasugi, T.2    Benson, J.D.3    Dowhanick, J.J.4    Howley, P.M.5
  • 33
    • 0029617680 scopus 로고
    • Co-operative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro
    • Sedman, J., and A. Stenlund. 1995. Co-operative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro. EMBO J. 14:6218-6228.
    • (1995) EMBO J. , vol.14 , pp. 6218-6228
    • Sedman, J.1    Stenlund, A.2
  • 34
    • 0027400464 scopus 로고
    • Bovine papilloma virus (BPV)-encoded E2 protein enhances binding of E1 protein to the BPV replication origin
    • Seo, Y.-S., F. Muller, M. Lusky, E. Gibbs, H.-Y. Kim, and J. Hurwitz. 1993. Bovine papilloma virus (BPV)-encoded E2 protein enhances binding of E1 protein to the BPV replication origin. Proc. Natl. Acad. Sci. USA 90:2865-2869.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2865-2869
    • Seo, Y.-S.1    Muller, F.2    Lusky, M.3    Gibbs, E.4    Kim, H.-Y.5    Hurwitz, J.6
  • 35
    • 0030044371 scopus 로고    scopus 로고
    • The bovine papillomavirus type 1 E2 transactivator and repressor proteins use different nuclear localization signals
    • Skiadopoulos, M. H., and A. A. McBride. 1996. The bovine papillomavirus type 1 E2 transactivator and repressor proteins use different nuclear localization signals. J. Virol. 70:1117-1124.
    • (1996) J. Virol. , vol.70 , pp. 1117-1124
    • Skiadopoulos, M.H.1    McBride, A.A.2
  • 36
    • 0027217598 scopus 로고
    • Binding of bovine papillomavirus E1 to the origin is not sufficient for DNA replication
    • Spalholz, B. A., A. A. McBride, T. Sarafi, and J. Quintero. 1993. Binding of bovine papillomavirus E1 to the origin is not sufficient for DNA replication. Virology 193:201-212.
    • (1993) Virology , vol.193 , pp. 201-212
    • Spalholz, B.A.1    McBride, A.A.2    Sarafi, T.3    Quintero, J.4
  • 37
    • 0028870107 scopus 로고
    • The bovine papillomavirus 1 E2 protein contains two activation domains: One that interacts with TBP and another that functions after TBP binding
    • Steger, G., J. Ham, O. Lefebvre, and M. Yaniv. 1995. The bovine papillomavirus 1 E2 protein contains two activation domains: one that interacts with TBP and another that functions after TBP binding. EMBO J. 14:329-340.
    • (1995) EMBO J. , vol.14 , pp. 329-340
    • Steger, G.1    Ham, J.2    Lefebvre, O.3    Yaniv, M.4
  • 38
    • 0025098820 scopus 로고
    • The E2 transactivator can act as a repressor by interfering with a cellular transcription factor
    • Stenlund, A., and M. Botchan. 1990. The E2 transactivator can act as a repressor by interfering with a cellular transcription factor. Genes Dev. 4:123-136.
    • (1990) Genes Dev. , vol.4 , pp. 123-136
    • Stenlund, A.1    Botchan, M.2
  • 39
    • 0025186708 scopus 로고
    • Differential transcriptional activation by Oct-1 and Oct-2: Interdependent activation domains induce Oct-2 phosphorylation
    • Tanaka, M., and W. Herr. 1990. Differential transcriptional activation by Oct-1 and Oct-2: interdependent activation domains induce Oct-2 phosphorylation. Cell 60:375-386.
    • (1990) Cell , vol.60 , pp. 375-386
    • Tanaka, M.1    Herr, W.2
  • 40
    • 0027313580 scopus 로고
    • DNA-binding domain of bovine papillomavirus type 1 E1 helicase: Structural and functional aspects
    • Thorner, L., D. Lim, and M. R. Botchan. 1993. DNA-binding domain of bovine papillomavirus type 1 E1 helicase: structural and functional aspects. J. Virol. 67:6000-6014.
    • (1993) J. Virol. , vol.67 , pp. 6000-6014
    • Thorner, L.1    Lim, D.2    Botchan, M.R.3
  • 41
    • 0028970090 scopus 로고
    • Structure and function of transcriptional activation domains
    • Triezenberg, S. J. 1995. Structure and function of transcriptional activation domains. Curr. Opin. Genes Dev. 5:190-196.
    • (1995) Curr. Opin. Genes Dev. , vol.5 , pp. 190-196
    • Triezenberg, S.J.1
  • 42
    • 0028168757 scopus 로고
    • Trans activation by the full-length E2 proteins of human papillomavirus type 16 and bovine papillomavirus type 1 in vitro and in vivo: Cooperation with activation domains of cellular transcription factors
    • Ushikai, M., M. J. Lace, Y. Yamakawa, M. Kono, J. Anson, T. Ishiji, S. Parkkinen, N. Wicker, M. Valentine, I. Davidson, L. P. Turek, and T. H. Haugen. 1994. trans activation by the full-length E2 proteins of human papillomavirus type 16 and bovine papillomavirus type 1 in vitro and in vivo: cooperation with activation domains of cellular transcription factors. J. Virol. 68:6655-6666.
    • (1994) J. Virol. , vol.68 , pp. 6655-6666
    • Ushikai, M.1    Lace, M.J.2    Yamakawa, Y.3    Kono, M.4    Anson, J.5    Ishiji, T.6    Parkkinen, S.7    Wicker, N.8    Valentine, M.9    Davidson, I.10    Turek, L.P.11    Haugen, T.H.12
  • 43
    • 0027398356 scopus 로고
    • The bovine papillomavirus origin of replication requires a binding site for the E2 transcriptional activator
    • Ustav, E., M. Ustav, P. Szymanski, and A. Stenlund. 1993. The bovine papillomavirus origin of replication requires a binding site for the E2 transcriptional activator. Proc. Natl. Acad. Sci. USA 90:898-902.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 898-902
    • Ustav, E.1    Ustav, M.2    Szymanski, P.3    Stenlund, A.4
  • 44
    • 0026034125 scopus 로고
    • Transient replication of BPV-1 requires two viral polypeptides encoded by the E1 and E2 open reading frames
    • Ustav, M., and A. Stenlund. 1991. Transient replication of BPV-1 requires two viral polypeptides encoded by the E1 and E2 open reading frames. EMBO J. 10:449-457.
    • (1991) EMBO J. , vol.10 , pp. 449-457
    • Ustav, M.1    Stenlund, A.2
  • 45
    • 0026758384 scopus 로고
    • Separation of the transcriptional activation and replication functions of the bovine papillomavirus-1 E2 protein
    • Winokur, P. L., and A. A. McBride. 1992. Separation of the transcriptional activation and replication functions of the bovine papillomavirus-1 E2 protein. EMBO J. 11:4111-4118.
    • (1992) EMBO J. , vol.11 , pp. 4111-4118
    • Winokur, P.L.1    McBride, A.A.2
  • 46
    • 0025989907 scopus 로고
    • Activation of BPV-1 replication in vitro by the transcription factor E2
    • Yang, L., R. Li, I. J. Mohr, R. Clark, and M. R. Botchan. 1991. Activation of BPV-1 replication in vitro by the transcription factor E2. Nature (London) 353:628-633.
    • (1991) Nature (London) , vol.353 , pp. 628-633
    • Yang, L.1    Li, R.2    Mohr, I.J.3    Clark, R.4    Botchan, M.R.5
  • 47
    • 0026378446 scopus 로고
    • The transcription factor E2 regulates BPV-1 DNA replication in vitro by direct protein-protein interaction
    • Yang, L., I. Mohr, R. Li, T. Nottoli, S. Sun, and M. Botchan. 1991. The transcription factor E2 regulates BPV-1 DNA replication in vitro by direct protein-protein interaction. Cold Spring Harbor Symp. Quant. Biol. 56:335-346.
    • (1991) Cold Spring Harbor Symp. Quant. Biol. , vol.56 , pp. 335-346
    • Yang, L.1    Mohr, I.2    Li, R.3    Nottoli, T.4    Sun, S.5    Botchan, M.6


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