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Volumn 70, Issue 7, 1996, Pages 4576-4584

The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl- terminal domain of RNA polymerase II for function

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SERINE THREONINE KINASE; RNA POLYMERASE II; TAK PROTEIN; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 0029943536     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.7.4576-4584.1996     Document Type: Article
Times cited : (124)

References (52)
  • 1
    • 0028301838 scopus 로고
    • Cellular latency in human immunodeficiency virus-infected individuals with high CD4 levels can he detected by the presence of promoter-proximal transcripts
    • Adams, M., L. Sharmeen, J. Kimplon, J. M. Romeo, J. V. Garcia, B. M. Peterlin, M. Groudine, and M. Emerman. 1994. Cellular latency in human immunodeficiency virus-infected individuals with high CD4 levels can he detected by the presence of promoter-proximal transcripts. Proc. Natl. Acad. Sci. USA 91:3862-3866.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3862-3866
    • Adams, M.1    Sharmeen, L.2    Kimplon, J.3    Romeo, J.M.4    Garcia, J.V.5    Peterlin, B.M.6    Groudine, M.7    Emerman, M.8
  • 2
    • 0028351327 scopus 로고
    • A sensitive reporter cell line for HIV-1 tat activity, HIV-1 inhibitors, and T cell activation effects
    • Aguilar-Cordova, E., J. Chinen, L. Donehower, D. E. Lewis, and J. W. Belmont. 1994. A sensitive reporter cell line for HIV-1 tat activity, HIV-1 inhibitors, and T cell activation effects. AIDS Res. Hum. Retroviruses 10: 295-301.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 295-301
    • Aguilar-Cordova, E.1    Chinen, J.2    Donehower, L.3    Lewis, D.E.4    Belmont, J.W.5
  • 3
    • 0027478063 scopus 로고
    • Modification of the megaprimer method of PCR mutagenesis: Improved amplification of the final product
    • Aiyar, A., and J. Leis. 1993. Modification of the megaprimer method of PCR mutagenesis: improved amplification of the final product. BioTechniques 14:366-369.
    • (1993) BioTechniques , vol.14 , pp. 366-369
    • Aiyar, A.1    Leis, J.2
  • 4
    • 0025761244 scopus 로고
    • Blocking of Tat-dependent HIV-1 RNA modification by an inhibitor of RNA polymerase II processivity
    • Braddock, M., A. M. Thorburn, A. J. Kingsman, and S. M. Kingsman. 1991. Blocking of Tat-dependent HIV-1 RNA modification by an inhibitor of RNA polymerase II processivity. Nature (London) 350:439-441.
    • (1991) Nature (London) , vol.350 , pp. 439-441
    • Braddock, M.1    Thorburn, A.M.2    Kingsman, A.J.3    Kingsman, S.M.4
  • 5
    • 0025169844 scopus 로고
    • Characterization of murine monoclonal antibodies to the tat protein from human immunodeficiency virus type 1
    • Brake, D. A., J. Goudsmit, W. J. Krone, P. Schammel, N. Appleby, R. H. Meloen, and C. Debouck. 1990. Characterization of murine monoclonal antibodies to the tat protein from human immunodeficiency virus type 1. J. Virol. 64:962-965.
    • (1990) J. Virol. , vol.64 , pp. 962-965
    • Brake, D.A.1    Goudsmit, J.2    Krone, W.J.3    Schammel, P.4    Appleby, N.5    Meloen, R.H.6    Debouck, C.7
  • 6
    • 0025771419 scopus 로고
    • Identification of lentivirus tat functional domains through generation of equine infectious anemia virus/human immunodeficiency virus type 1 tat gene chimeras
    • Carroll, R., L. Martarano, and D. Derse. 1991. Identification of lentivirus tat functional domains through generation of equine infectious anemia virus/human immunodeficiency virus type 1 tat gene chimeras. J. Virol. 65:3460-3467.
    • (1991) J. Virol. , vol.65 , pp. 3460-3467
    • Carroll, R.1    Martarano, L.2    Derse, D.3
  • 7
    • 0026558060 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 Tat activity by coexpression of heterologous trans activators
    • Carroll, R., B. M. Peterlin, and D. Derse. 1992. Inhibition of human immunodeficiency virus type 1 Tat activity by coexpression of heterologous trans activators. J. Virol. 66:2000-2007.
    • (1992) J. Virol. , vol.66 , pp. 2000-2007
    • Carroll, R.1    Peterlin, B.M.2    Derse, D.3
  • 8
    • 0027457660 scopus 로고
    • RNA polymerase II transcription cycles
    • Corden, J. L. 1993. RNA polymerase II transcription cycles. Curr. Opin. Genet. Dev. 3:213-218.
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 213-218
    • Corden, J.L.1
  • 9
    • 0023005976 scopus 로고
    • Trans-activation of human immunodeficiency virus occurs via a bimodal mechanism
    • Cullen, B. R. 1986. Trans-activation of human immunodeficiency virus occurs via a bimodal mechanism. Cell 46:973-982.
    • (1986) Cell , vol.46 , pp. 973-982
    • Cullen, B.R.1
  • 10
    • 0001888446 scopus 로고
    • Regulation of HIV gene expression
    • Cullen, B. R. 1995. Regulation of HIV gene expression. AIDS 9(Suppl. A):S19-S32.
    • (1995) AIDS , vol.9 , Issue.SUPPL. A
    • Cullen, B.R.1
  • 11
    • 0028139742 scopus 로고
    • The role of multisite phosphorylation in the regulation of RNA polymerase II activity
    • Dahmus, M. E. 1994. The role of multisite phosphorylation in the regulation of RNA polymerase II activity. Prog. Nucleic Acid Res. Mol. Biol. 48:143-179.
    • (1994) Prog. Nucleic Acid Res. Mol. Biol. , vol.48 , pp. 143-179
    • Dahmus, M.E.1
  • 12
    • 0022500166 scopus 로고
    • The trans-activator gene of the human T cell lymphotropic virus type III is required for replication
    • Dayton, A. I., J. G. Sodroski, C. A. Rosen, W. C. Goh, and W. A. Haseltine. 1986. The trans-activator gene of the human T cell lymphotropic virus type III is required for replication. Cell 44:941-947.
    • (1986) Cell , vol.44 , pp. 941-947
    • Dayton, A.I.1    Sodroski, J.G.2    Rosen, C.A.3    Goh, W.C.4    Haseltine, W.A.5
  • 13
    • 0028173857 scopus 로고
    • Construction and characterization of a potent HIV-2 Tat transdominant mutant protein
    • Echetebu, C. O., H. Rhim, C. H. Herrmann, and A. P. Rice. 1994. Construction and characterization of a potent HIV-2 Tat transdominant mutant protein. J. Acquired Immune Defic. Syndr. 7:655-664.
    • (1994) J. Acquired Immune Defic. Syndr. , vol.7 , pp. 655-664
    • Echetebu, C.O.1    Rhim, H.2    Herrmann, C.H.3    Rice, A.P.4
  • 14
    • 0023494758 scopus 로고
    • The specificity of the human immunodeficiency virus type 2 transactivator is different from that of human immunodeficiency virus type 1
    • Emerman, M., M. Guyader, L. Monlagnier, D. Baltimore, and M. A. Muesing. 1987. The specificity of the human immunodeficiency virus type 2 transactivator is different from that of human immunodeficiency virus type 1. EMBO J. 6:3755-3760.
    • (1987) EMBO J. , vol.6 , pp. 3755-3760
    • Emerman, M.1    Guyader, M.2    Monlagnier, L.3    Baltimore, D.4    Muesing, M.A.5
  • 15
    • 0025817413 scopus 로고
    • The role of Tat in the human immunodeficiency virus life cycle indicates a primary effect on transcriptional elongation
    • Feinberg, M. B., D. Baltimore, and A. D. Frankel. 1991. The role of Tat in the human immunodeficiency virus life cycle indicates a primary effect on transcriptional elongation. Proc. Natl. Acad. Sci. USA 88:4045-4049.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4045-4049
    • Feinberg, M.B.1    Baltimore, D.2    Frankel, A.D.3
  • 16
    • 0024459228 scopus 로고
    • Functional analysis of the Tat trans activator of human immunodeficiency virus type 2
    • Fenrick, R., M. H. Malim, J. Hauber, S. Y. Le, J. Maizel, and B. R. Cullen. 1989. Functional analysis of the Tat trans activator of human immunodeficiency virus type 2. J. Virol. 63:5006-5012.
    • (1989) J. Virol. , vol.63 , pp. 5006-5012
    • Fenrick, R.1    Malim, M.H.2    Hauber, J.3    Le, S.Y.4    Maizel, J.5    Cullen, B.R.6
  • 18
    • 0023990358 scopus 로고
    • Tat protein from human immunodeficiency virus forms a metal-linked dimer
    • Frankel, A. D., D. S. Bredl, and C. O. Pabo. 1988. Tat protein from human immunodeficiency virus forms a metal-linked dimer. Science 240:70-73.
    • (1988) Science , vol.240 , pp. 70-73
    • Frankel, A.D.1    Bredl, D.S.2    Pabo, C.O.3
  • 19
    • 0027196104 scopus 로고
    • RNA recognition by the human immunodeficiency virus Tat and Rev proteins
    • Gait, M. J., and J. Karn. 1993. RNA recognition by the human immunodeficiency virus Tat and Rev proteins. Trends Biochem. Sci. 18:255-259.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 255-259
    • Gait, M.J.1    Karn, J.2
  • 21
    • 0028097472 scopus 로고
    • Pharmaceutical research in molecular oncology
    • Gibbs, J. B., and A. Oliff. 1994. Pharmaceutical research in molecular oncology. Cell 79:193-198.
    • (1994) Cell , vol.79 , pp. 193-198
    • Gibbs, J.B.1    Oliff, A.2
  • 23
    • 0024211669 scopus 로고
    • Phosphorylation of the rev gene product of human immunodeficiency virus type 1
    • Hauber, J., M. Bouvier, M. H. Malim, and B. R. Cullen. 1988. Phosphorylation of the rev gene product of human immunodeficiency virus type 1. J. Virol. 62:4801-4804.
    • (1988) J. Virol. , vol.62 , pp. 4801-4804
    • Hauber, J.1    Bouvier, M.2    Malim, M.H.3    Cullen, B.R.4
  • 24
    • 0029915296 scopus 로고    scopus 로고
    • Viral transactivators specifically target distinct cellular protein kinases that phosphorylate the RNA polymerase II C-terminal domain
    • Herrmann, C. H., M. O. Gold, and A. P. Rice. 1996. Viral transactivators specifically target distinct cellular protein kinases that phosphorylate the RNA polymerase II C-terminal domain. Nucleic Acids Res. 24:501-509.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 501-509
    • Herrmann, C.H.1    Gold, M.O.2    Rice, A.P.3
  • 25
    • 0027438621 scopus 로고
    • Specific interaction of the human immunodeficiency virus Tat proteins with a cellular protein kinase
    • Herrmann, C. H., and A. P. Rice. 1993. Specific interaction of the human immunodeficiency virus Tat proteins with a cellular protein kinase. Virology 197:601-608.
    • (1993) Virology , vol.197 , pp. 601-608
    • Herrmann, C.H.1    Rice, A.P.2
  • 26
    • 0028831057 scopus 로고
    • Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carhoxyl-terminal domain of the large suhunit of RNA polymerase II: Candidate for a Tat cofactor
    • Herrmann, C. H., and A. P. Rice. 1995. Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carhoxyl-terminal domain of the large suhunit of RNA polymerase II: candidate for a Tat cofactor. J. Virol. 69:1612-1620.
    • (1995) J. Virol. , vol.69 , pp. 1612-1620
    • Herrmann, C.H.1    Rice, A.P.2
  • 27
    • 0028290825 scopus 로고
    • Control of RNA initiation and elongation at the HIV-1 promoter
    • Jones, K. A., and B. M. Peterlin. 1994. Control of RNA initiation and elongation at the HIV-1 promoter. Annu. Rev. Biochem. 63:717-743.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 717-743
    • Jones, K.A.1    Peterlin, B.M.2
  • 28
    • 0023513563 scopus 로고
    • Antitermination of transcription within the long terminal repeat of HIV-1 by tat gene product
    • Kao, S. Y., A. F. Calman, P. A. Luciw, and B. M. Peterlin. 1987. Antitermination of transcription within the long terminal repeat of HIV-1 by tat gene product. Nature (London) 338:489-493.
    • (1987) Nature (London) , vol.338 , pp. 489-493
    • Kao, S.Y.1    Calman, A.F.2    Luciw, P.A.3    Peterlin, B.M.4
  • 29
    • 0024591269 scopus 로고
    • Multiple functional domains of Tat, the trans-activator of HIV-1, denned by mutational analysis
    • Kuppuswamy, M., T. Subramanian, A. Srinivasan, and G. Chinnadurai. 1989. Multiple functional domains of Tat, the trans-activator of HIV-1, denned by mutational analysis. Nucleic Acids Res. 17:3551-3561.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3551-3561
    • Kuppuswamy, M.1    Subramanian, T.2    Srinivasan, A.3    Chinnadurai, G.4
  • 30
    • 0024414213 scopus 로고
    • HIV-1 Tat protein increases transcriptional initiation and stabilizes elongation
    • Laspia, M. F., A. P. Rice, and M. B. Mathews. 1989. HIV-1 Tat protein increases transcriptional initiation and stabilizes elongation. Cell 59:283-292.
    • (1989) Cell , vol.59 , pp. 283-292
    • Laspia, M.F.1    Rice, A.P.2    Mathews, M.B.3
  • 31
    • 0010564030 scopus 로고
    • Construction of plasmids that express E. coli beta-galactosidase in mammalian cells
    • MacGregor, G. R., and C. T. Caskey. 1989. Construction of plasmids that express E. coli beta-galactosidase in mammalian cells. Nucleic Acids Res. 17:2365.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 2365
    • MacGregor, G.R.1    Caskey, C.T.2
  • 32
    • 0027310927 scopus 로고
    • Genetic analysis of the cofactor requirement for human immunodeficiency virus type 1 Tat function
    • Madore, S. J., and B. R. Cullen. 1993. Genetic analysis of the cofactor requirement for human immunodeficiency virus type 1 Tat function. J. Virol. 67:3703-3711.
    • (1993) J. Virol. , vol.67 , pp. 3703-3711
    • Madore, S.J.1    Cullen, B.R.2
  • 33
    • 0025248378 scopus 로고
    • HIV-1 Tat protein trans-activates transcription in vitro
    • Marciniak, R. A., B. J. Calnan, A. D. Frankel, and P. A. Sharp. 1990. HIV-1 Tat protein trans-activates transcription in vitro. Cell 63:791-802.
    • (1990) Cell , vol.63 , pp. 791-802
    • Marciniak, R.A.1    Calnan, B.J.2    Frankel, A.D.3    Sharp, P.A.4
  • 34
    • 0026064723 scopus 로고
    • HIV-1 Tat protein promotes formation of more-processive elongation complexes
    • Marciniak, R. A., and P. A. Sharp. 1991. HIV-1 Tat protein promotes formation of more-processive elongation complexes. EMBO J. 10:4189-4196.
    • (1991) EMBO J. , vol.10 , pp. 4189-4196
    • Marciniak, R.A.1    Sharp, P.A.2
  • 35
    • 0026725368 scopus 로고
    • Control of formation of two distinct classes of RNA polymerase II elongation complexes
    • Marshall, N. F., and D. H. Price. 1992. Control of formation of two distinct classes of RNA polymerase II elongation complexes. Mol. Cell. Biol. 12: 2078-2090.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2078-2090
    • Marshall, N.F.1    Price, D.H.2
  • 36
    • 0029011873 scopus 로고
    • Purification of P-TEFh, a transcription factor required for the transition into productive elongation
    • Marshall, N. F., and D. H. Price. 1995. Purification of P-TEFh, a transcription factor required for the transition into productive elongation. J. Biol. Chem. 270:12335-12338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 38
    • 0026552386 scopus 로고
    • DNA binding provides a signal for phosphorylation of the RNA polymerase II heptapeptide repeats
    • Peterson, S. R., A. Dvir, C. W. Anderson, and W. S. Dynan. 1992. DNA binding provides a signal for phosphorylation of the RNA polymerase II heptapeptide repeats. Genes Dev. 6:426-438.
    • (1992) Genes Dev. , vol.6 , pp. 426-438
    • Peterson, S.R.1    Dvir, A.2    Anderson, C.W.3    Dynan, W.S.4
  • 39
    • 0027551310 scopus 로고
    • Rapid purification of monomer HIV-2 Tat protein expressed in Escherichia coli
    • Rhim, H., F. Chan, C. O. Echetebu, and A. P. Rice. 1993. Rapid purification of monomer HIV-2 Tat protein expressed in Escherichia coli. Protein Expression Purif. 4:24-31.
    • (1993) Protein Expression Purif. , vol.4 , pp. 24-31
    • Rhim, H.1    Chan, F.2    Echetebu, C.O.3    Rice, A.P.4
  • 40
    • 0028170786 scopus 로고
    • Wild-type and mutant HIV-1 and HIV-2 Tat proteins expressed in Escherichia coli as fusions with glutathione S-transferase
    • Rhim, H., C. O. Echetebu, C. H. Herrmann, and A. P. Rice. 1994. Wild-type and mutant HIV-1 and HIV-2 Tat proteins expressed in Escherichia coli as fusions with glutathione S-transferase. J. Acquired Immune Defic. Syndr. 7:1116-1121.
    • (1994) J. Acquired Immune Defic. Syndr. , vol.7 , pp. 1116-1121
    • Rhim, H.1    Echetebu, C.O.2    Herrmann, C.H.3    Rice, A.P.4
  • 41
    • 0028099293 scopus 로고
    • Exon 2 of HIV-2 Tat contributes to transactivation of the HIV-2 LTR by increasing binding affinity to HIV-2 TAR RNA
    • Rhim, H., and A. P. Rice. 1994. Exon 2 of HIV-2 Tat contributes to transactivation of the HIV-2 LTR by increasing binding affinity to HIV-2 TAR RNA. Nucleic Acids Res. 22:4405-4413.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4405-4413
    • Rhim, H.1    Rice, A.P.2
  • 42
    • 0028015897 scopus 로고
    • Functional significance of the dinucleotide bulge in stem-loop 1 and stem-loop 2 of HIV-2 TAR RNA
    • Rhim, H., and A. P. Rice. 1994. Functional significance of the dinucleotide bulge in stem-loop 1 and stem-loop 2 of HIV-2 TAR RNA. Virology 202: 202-211.
    • (1994) Virology , vol.202 , pp. 202-211
    • Rhim, H.1    Rice, A.P.2
  • 44
    • 0025240436 scopus 로고
    • Mutational analysis of the conserved cysteine-rich region of the human immunodeficiency virus type 1 Tat protein
    • Rice, A. P., and F. Carlotti. 1990. Mutational analysis of the conserved cysteine-rich region of the human immunodeficiency virus type 1 Tat protein. J. Virol. 64:1864-1868.
    • (1990) J. Virol. , vol.64 , pp. 1864-1868
    • Rice, A.P.1    Carlotti, F.2
  • 45
    • 0025223467 scopus 로고
    • Structural analysis of wild-type and mutant human immunodeficiency virus type 1 Tat proteins
    • Rice, A. P., and F. Carlotti. 1990. Structural analysis of wild-type and mutant human immunodeficiency virus type 1 Tat proteins. J. Virol. 64:6018-6026.
    • (1990) J. Virol. , vol.64 , pp. 6018-6026
    • Rice, A.P.1    Carlotti, F.2
  • 46
    • 0022006369 scopus 로고
    • The location of cis-acting regulatory sequences in the human T cell lymphotropic virus type III (HTLV-III/LAV) long terminal repeat
    • Rosen, C. A., J. G. Sodroski, and W. A. Haseltine. 1985. The location of cis-acting regulatory sequences in the human T cell lymphotropic virus type III (HTLV-III/LAV) long terminal repeat. Cell 41:813-823.
    • (1985) Cell , vol.41 , pp. 813-823
    • Rosen, C.A.1    Sodroski, J.G.2    Haseltine, W.A.3
  • 47
    • 0039089706 scopus 로고
    • Missense mutations in an infectious human immunodeficiency viral genome: Functional mapping of tat and identification of the rev splice acceptor
    • Sadaie, M. R., J. Rappaport, T. Benter, S. F. Josephs, R. Willis, and F. Wong-Staal. 1988. Missense mutations in an infectious human immunodeficiency viral genome: functional mapping of tat and identification of the rev splice acceptor. Proc. Natl. Acad. Sci. USA 85:9224-9228.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9224-9228
    • Sadaie, M.R.1    Rappaport, J.2    Benter, T.3    Josephs, S.F.4    Willis, R.5    Wong-Staal, F.6
  • 48
    • 0028063434 scopus 로고
    • Interaction of v-rel oncoprotein with cellular transcription factor Spl
    • Sif, S., and T. D. Gilmore. 1994. Interaction of v-rel oncoprotein with cellular transcription factor Spl. J. Virol. 68:7131-7138.
    • (1994) J. Virol. , vol.68 , pp. 7131-7138
    • Sif, S.1    Gilmore, T.D.2
  • 49
    • 0026309016 scopus 로고
    • The HIV-1 Tat protein activates transcription from an upstream DNA-binding site: Implications for Tat function
    • Southgate, C. D., and M. R. Green. 1991. The HIV-1 Tat protein activates transcription from an upstream DNA-binding site: implications for Tat function. Genes Dev. 5:2496-2507.
    • (1991) Genes Dev. , vol.5 , pp. 2496-2507
    • Southgate, C.D.1    Green, M.R.2
  • 50
    • 0027751895 scopus 로고
    • A quantitative assay for trans-activation by HIV-1 Tat, using liposome-mediated DNA uptake and a parallel ELISA system
    • Watson, M. E., and M. Moore. 1993. A quantitative assay for trans-activation by HIV-1 Tat, using liposome-mediated DNA uptake and a parallel ELISA system. AIDS Res. Hum. Retroviruses 9:861-867.
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 861-867
    • Watson, M.E.1    Moore, M.2
  • 52
    • 0027354762 scopus 로고
    • Initiation of transcription by RNA polymerase II: A multi-step process
    • Zawel, L., and D. Reinberg. 1993. Initiation of transcription by RNA polymerase II: a multi-step process. Prog. Nucleic Acid Res. Mol. Biol. 44:67-108.
    • (1993) Prog. Nucleic Acid Res. Mol. Biol. , vol.44 , pp. 67-108
    • Zawel, L.1    Reinberg, D.2


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