메뉴 건너뛰기




Volumn 277, Issue 2, 1998, Pages 179-197

Role of the human homolog of the yeast transcription factor SPT5 in HIV-1 Tat-activation

Author keywords

HIV; RNA polymerase II; SPT5 and SPT6 proteins; Tat; Transcriptional regulation

Indexed keywords

ELONGATION FACTOR; ETOPOSIDE; RNA POLYMERASE II; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SPT5; UNCLASSIFIED DRUG;

EID: 0032571254     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1601     Document Type: Article
Times cited : (63)

References (70)
  • 1
    • 0029095126 scopus 로고
    • Requirement for TFIIH kinase activity in transcription by RNA polymerase II
    • Akoulitchev S., Makela T.P., Weinberg R.A., Reinberg D. Requirement for TFIIH kinase activity in transcription by RNA polymerase II. Nature. 377:1995;557-560
    • (1995) Nature , vol.377 , pp. 557-560
    • Akoulitchev, S.1    Makela, T.P.2    Weinberg, R.A.3    Reinberg, D.4
  • 2
    • 0029084914 scopus 로고
    • Elongin (SIII) a multisubunit regulator of elongation by RNA polymerase II
    • Aso T., Lane W.S., Conaway J.W., Conaway R.C. Elongin (SIII) a multisubunit regulator of elongation by RNA polymerase II. Science. 269:1995;1439-1443
    • (1995) Science , vol.269 , pp. 1439-1443
    • Aso, T.1    Lane, W.S.2    Conaway, J.W.3    Conaway, R.C.4
  • 3
    • 0026065031 scopus 로고
    • Role of the mammalian transcription factors IIF, IIS, and IIX during elongation by RNA polymerase II
    • Bengal E., Flores O., Krauskopf A., Reinberg D., Aloni Y. Role of the mammalian transcription factors IIF, IIS, and IIX during elongation by RNA polymerase II. Mol. Cell. Biol. 11:1991;1195-1206
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1195-1206
    • Bengal, E.1    Flores, O.2    Krauskopf, A.3    Reinberg, D.4    Aloni, Y.5
  • 5
    • 0029890667 scopus 로고    scopus 로고
    • Evidence that spt6p controls chromatin structure by a direct interaction with histones
    • Bortvin A., Winston F. Evidence that spt6p controls chromatin structure by a direct interaction with histones. Science. 272:1996;1473-1476
    • (1996) Science , vol.272 , pp. 1473-1476
    • Bortvin, A.1    Winston, F.2
  • 6
    • 0023656260 scopus 로고
    • Messenger RNA synthesis in mammalian cells is catalyzed by the phosphorylated form of RNA polymerase II
    • Cadena D., Dahmus M.J. Messenger RNA synthesis in mammalian cells is catalyzed by the phosphorylated form of RNA polymerase II. J. Biol. Chem. 262:1987;12468-12474
    • (1987) J. Biol. Chem. , vol.262 , pp. 12468-12474
    • Cadena, D.1    Dahmus, M.J.2
  • 10
    • 0029909605 scopus 로고    scopus 로고
    • Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1
    • Chun R.F., Jeang K.T. Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1. J. Biol. Chem. 271:1996;27888-27894
    • (1996) J. Biol. Chem. , vol.271 , pp. 27888-27894
    • Chun, R.F.1    Jeang, K.T.2
  • 11
    • 0030901305 scopus 로고    scopus 로고
    • The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme
    • Cujec T.P., Maldonado E., Meyer J., Reinberg D., Peterlin B.M. The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. Mol. Cell. Biol. 17:1997;1817-1823
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1817-1823
    • Cujec, T.P.1    Maldonado, E.2    Meyer, J.3    Reinberg, D.4    Peterlin, B.M.5
  • 12
    • 0030856701 scopus 로고    scopus 로고
    • The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II
    • Cujec T.P., Okamoto H., Fujinaga K., Meyer J., Chamberlin H., Morgan D.O., Peterlin B.M. The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II. Genes Dev. 11:1997;2645-2657
    • (1997) Genes Dev. , vol.11 , pp. 2645-2657
    • Cujec, T.P.1    Okamoto, H.2    Fujinaga, K.3    Meyer, J.4    Chamberlin, H.5    Morgan, D.O.6    Peterlin, B.M.7
  • 13
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J.D., Lebovitz R.M., Roeder R.G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucl. Acids Res. 11:1983;1475-1489
    • (1983) Nucl. Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 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., Baltimore D., Frankel A.D. The role of Tat in the human immunodeficiency virus life cycle indicates a primary effect on transcriptional elongation. Proc. Natl Acad. Sci. USA. 88:1991;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
    • 0023876147 scopus 로고
    • HIV-1 Tat trans-activation requires the loop sequence within TAR
    • Feng S., Holland E.C. HIV-1 Tat trans-activation requires the loop sequence within TAR. Nature. 334:1988;165-167
    • (1988) Nature , vol.334 , pp. 165-167
    • Feng, S.1    Holland, E.C.2
  • 17
    • 0029563181 scopus 로고
    • TAT functions to stimulate the elongation properties of transcription complexes paused by the duplicated TAR RNA element of human immunodeficiency virus 2
    • García-Martínez L.F., Mavankal G., Peters P., Wu-Baer F., Gaynor R.B. TAT functions to stimulate the elongation properties of transcription complexes paused by the duplicated TAR RNA element of human immunodeficiency virus 2. J. Mol. Biol. 254:1995;350-363
    • (1995) J. Mol. Biol. , vol.254 , pp. 350-363
    • García-Martínez, L.F.1    Mavankal, G.2    Peters, P.3    Wu-Baer, F.4    Gaynor, R.B.5
  • 18
    • 0030936357 scopus 로고    scopus 로고
    • Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes
    • García-Martínez L.F., Ivanov D., Gaynor R.B. Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. J. Biol. Chem. 272:1997;6951-6958
    • (1997) J. Biol. Chem. , vol.272 , pp. 6951-6958
    • García-Martínez, L.F.1    Ivanov, D.2    Gaynor, R.B.3
  • 19
    • 0039243885 scopus 로고    scopus 로고
    • Purification of a Tat associated kinase reveals a TFIIH complex that modulates HIV-1 transcription
    • García-Martínez L.F., Mavankal G., Neveu J., Lane W., Sigman D., Ivanov D., Gaynor R.B. Purification of a Tat associated kinase reveals a TFIIH complex that modulates HIV-1 transcription. EMBO J. 16:1997;2836-2850
    • (1997) EMBO J. , vol.16 , pp. 2836-2850
    • García-Martínez, L.F.1    Mavankal, G.2    Neveu, J.3    Lane, W.4    Sigman, D.5    Ivanov, D.6    Gaynor, R.B.7
  • 20
    • 0028352861 scopus 로고
    • Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II
    • Goodrich J.A., Tijan R. Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II. Cell. 77:1994;145-156
    • (1994) Cell , vol.77 , pp. 145-156
    • Goodrich, J.A.1    Tijan, R.2
  • 21
    • 0027193751 scopus 로고
    • Human immunodeficiency virus type-1 trans-activatory protein, tat, stimulates transcriptional read-through of distal terminator sequences in vitro
    • Graeble M.A., Churcher M.J., Lowe A.D., Gait M.J., Karn J. Human immunodeficiency virus type-1 trans-activatory protein, tat, stimulates transcriptional read-through of distal terminator sequences in vitro. Proc. Natl Acad. Sci. USA. 90:1993;6184-6188
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6184-6188
    • Graeble, M.A.1    Churcher, M.J.2    Lowe, A.D.3    Gait, M.J.4    Karn, J.5
  • 23
    • 0029896450 scopus 로고    scopus 로고
    • Identification and analysis of a functional human homolog of the spt4 gene of Saccharomyces cerevisiae
    • Hartzog G.A., Basrai M.A., Ricupero-Hovasse S.L., Hieter P., Winston F. Identification and analysis of a functional human homolog of the spt4 gene of Saccharomyces cerevisiae. Mol. Cell Biol. 16:1996;2848-2856
    • (1996) Mol. Cell Biol. , vol.16 , pp. 2848-2856
    • Hartzog, G.A.1    Basrai, M.A.2    Ricupero-Hovasse, S.L.3    Hieter, P.4    Winston, F.5
  • 24
    • 0028983813 scopus 로고
    • Improvement of an in gel digestion procedure for the micro-preparation of internal protein fragments for amino acid sequencing
    • Hellman U., Wernstedt C., Gonez J., Heldin C.H. Improvement of an in gel digestion procedure for the micro-preparation of internal protein fragments for amino acid sequencing. Anal. Biochem. 224:1995;451-455
    • (1995) Anal. Biochem. , vol.224 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 25
    • 0028831057 scopus 로고
    • Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: Candidate for a Tat cofactor
    • Herrmann C.H., Rice A.P. Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II candidate for a Tat cofactor. J. Virol. 69:1995;1612-1620
    • (1995) J. Virol. , vol.69 , pp. 1612-1620
    • Herrmann, C.H.1    Rice, A.P.2
  • 26
    • 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., Gold M.O., Rice A.P. Viral transactivators specifically target distinct cellular protein kinases that phosphorylate the RNA polymerase II C-terminal domain. Nucl. Acids Res. 24:1996;501-508
    • (1996) Nucl. Acids Res. , vol.24 , pp. 501-508
    • Herrmann, C.H.1    Gold, M.O.2    Rice, A.P.3
  • 27
    • 0028290825 scopus 로고
    • Control of RNA initiation and elongation at the HIV-1 promoter
    • Jones K.A., Peterlin B.M. Control of RNA initiation and elongation at the HIV-1 promoter. Annu. Rev. Biochem. 63:1994;717-743
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 717-743
    • Jones, K.A.1    Peterlin, B.M.2
  • 28
    • 0023513563 scopus 로고
    • Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product
    • Kao S.Y., Calnan A.F., Luciw P.A., Peterlin B.M. Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product. Nature. 330:1987;489-493
    • (1987) Nature , vol.330 , pp. 489-493
    • Kao, S.Y.1    Calnan, A.F.2    Luciw, P.A.3    Peterlin, B.M.4
  • 29
    • 0026568822 scopus 로고
    • HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors
    • Kato H., Sumimoto H., Pognonec P., Chen C.H., Rosen C.A., Roeder R.G. HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors. Genes Dev. 6:1992;655-666
    • (1992) Genes Dev. , vol.6 , pp. 655-666
    • Kato, H.1    Sumimoto, H.2    Pognonec, P.3    Chen, C.H.4    Rosen, C.A.5    Roeder, R.G.6
  • 30
    • 0029975982 scopus 로고    scopus 로고
    • Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex
    • Keen N.J., Gait M.J., Karn J. Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex. Proc. Natl Acad. Sci. USA. 93:1996;2505-2510
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2505-2510
    • Keen, N.J.1    Gait, M.J.2    Karn, J.3
  • 31
    • 0030864512 scopus 로고    scopus 로고
    • Transfer of Tat and release of TAR RNA during the activation of the immunodeficiency virus type-1 transcriptional elongation complex
    • Keen N.J., Churcher M.J., Karn J. Transfer of Tat and release of TAR RNA during the activation of the immunodeficiency virus type-1 transcriptional elongation complex. EMBO J. 16:1997;5260-5272
    • (1997) EMBO J. , vol.16 , pp. 5260-5272
    • Keen, N.J.1    Churcher, M.J.2    Karn, J.3
  • 32
    • 0028282551 scopus 로고
    • A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II
    • Kim Y.-J., Bjorklund S., Li Y., Sayre M.H., Kornberg R.D. A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II. Cell. 77:1994;599-608
    • (1994) Cell , vol.77 , pp. 599-608
    • Kim, Y.-J.1    Bjorklund, S.2    Li, Y.3    Sayre, M.H.4    Kornberg, R.D.5
  • 33
    • 0028924386 scopus 로고
    • Promoter-proximal pausing of RNA polymerase II defines a general rate-limiting step after transcription initiation
    • Krumm A., Hickey L.B., Groudine M. Promoter-proximal pausing of RNA polymerase II defines a general rate-limiting step after transcription initiation. Genes Dev. 9:1995;559-572
    • (1995) Genes Dev. , vol.9 , pp. 559-572
    • Krumm, A.1    Hickey, L.B.2    Groudine, M.3
  • 34
    • 0030296854 scopus 로고    scopus 로고
    • KOW: A novel motif linking a bacterial transcription factor with ribosomal proteins
    • Kyrpides N.C., Woese C.R., Ouzounis C.A. KOW a novel motif linking a bacterial transcription factor with ribosomal proteins. Trends Biochem. Sci. 21:1996;423-424
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 423-424
    • Kyrpides, N.C.1    Woese, C.R.2    Ouzounis, C.A.3
  • 35
    • 0025869741 scopus 로고
    • Complete amino acid sequence of the FK506 and rapamycin binding protein, FKBP, isolated from calf thymus
    • Lane W.S., Galat A., Harding M.W., Schreiber S.L. Complete amino acid sequence of the FK506 and rapamycin binding protein, FKBP, isolated from calf thymus. J. Proteins Chem. 10:1991;151-160
    • (1991) J. Proteins Chem. , vol.10 , pp. 151-160
    • Lane, W.S.1    Galat, A.2    Harding, M.W.3    Schreiber, S.L.4
  • 36
    • 0024414213 scopus 로고
    • HIV-1 Tat protein increases transcriptional initiation and stabilizes elongation
    • Laspia M.F., Rice A.P., Mathews M.B. HIV-1 Tat protein increases transcriptional initiation and stabilizes elongation. Cell. 59:1989;283-292
    • (1989) Cell , vol.59 , pp. 283-292
    • Laspia, M.F.1    Rice, A.P.2    Mathews, M.B.3
  • 37
    • 0024571802 scopus 로고
    • Transcription activation by the adenovirus E1A protein
    • Lillie J.W., Green M.R. Transcription activation by the adenovirus E1A protein. Nature. 338:1989;39-44
    • (1989) Nature , vol.338 , pp. 39-44
    • Lillie, J.W.1    Green, M.R.2
  • 38
    • 0027523232 scopus 로고
    • Molecular and genetic characterization of SPT4, a gene important for transcription initiation in Saccharomyces cerevisiae
    • Malone E.A., Fassler J.S., Winston F. Molecular and genetic characterization of SPT4, a gene important for transcription initiation in Saccharomyces cerevisiae. Mol. Gen. Genet. 237:1993;449-459
    • (1993) Mol. Gen. Genet. , vol.237 , pp. 449-459
    • Malone, E.A.1    Fassler, J.S.2    Winston, F.3
  • 40
    • 0026064723 scopus 로고
    • HIV-1 Tat protein promotes formation of more-processive elongation complexes
    • Marciniak R.A., Sharp P.A. HIV-1 Tat protein promotes formation of more-processive elongation complexes. EMBO J. 10:1991;4189-4196
    • (1991) EMBO J. , vol.10 , pp. 4189-4196
    • Marciniak, R.A.1    Sharp, P.A.2
  • 41
    • 0025248378 scopus 로고
    • HIV-1 Tat protein trans-activates transcription in vitro
    • Marciniak R.A., Calnan B.J., Frankel A.D., Sharp P.A. HIV-1 Tat protein trans-activates transcription in vitro. Cell. 63:1990;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
  • 42
    • 0029011873 scopus 로고
    • Purification of P-TEFb, a transcription factor required for the transition into productive elongation
    • Marshall N.F., Price D.H. Purification of P-TEFb, a transcription factor required for the transition into productive elongation. J. Biol. Chem. 270:1995;12335-12338
    • (1995) J. Biol. Chem. , vol.270 , pp. 12335-12338
    • Marshall, N.F.1    Price, D.H.2
  • 43
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall N.F., Peng J., Xie P., Price D.H. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271:1996;27176-27183
    • (1996) J. Biol. Chem. , vol.271 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, P.3    Price, D.H.4
  • 45
    • 0030605415 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. V. the coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1
    • Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N. Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 3:1996;17-24
    • (1996) DNA Res. , vol.3 , pp. 17-24
    • Nagase, T.1    Seki, N.2    Ishikawa, K.3    Tanaka, A.4    Nomura, N.5
  • 46
    • 0028305843 scopus 로고
    • Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation
    • O'Brien T., Hardin S., Greenleaf A., Lis J.T. Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation. Nature. 370:1994;75-77
    • (1994) Nature , vol.370 , pp. 75-77
    • O'Brien, T.1    Hardin, S.2    Greenleaf, A.3    Lis, J.T.4
  • 47
    • 0029969105 scopus 로고    scopus 로고
    • Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II
    • Okamoto H., Sheline C.T., Corden J.L., Jones K.A., Peterlin B.M. Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II. Proc. Natl Acad. Sci. USA. 93:1996;11575-11579
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11575-11579
    • Okamoto, H.1    Sheline, C.T.2    Corden, J.L.3    Jones, K.A.4    Peterlin, B.M.5
  • 48
    • 0029956642 scopus 로고    scopus 로고
    • Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain
    • Parada C.A., Roeder R.G. Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. Nature. 384:1996;375-378
    • (1996) Nature , vol.384 , pp. 375-378
    • Parada, C.A.1    Roeder, R.G.2
  • 49
    • 0024408630 scopus 로고
    • The transition of RNA polymerase II from initiation to elongation is associated with phosphorylation of the carboxyl-terminal domain of subunit IIa
    • Payne J.M., Laybourn P.J., Dahmus M.E. The transition of RNA polymerase II from initiation to elongation is associated with phosphorylation of the carboxyl-terminal domain of subunit IIa. J. Biol. Chem. 264:1989;19621-19629
    • (1989) J. Biol. Chem. , vol.264 , pp. 19621-19629
    • Payne, J.M.1    Laybourn, P.J.2    Dahmus, M.E.3
  • 50
    • 0025602656 scopus 로고
    • The HIV-1 long terminal repeat contains an unusual element that induces the synthesis of short RNAs from various mRNA and snRNA promoters
    • Ratnasabapathy R., Sheldon M., Johal L., Hernandez N. The HIV-1 long terminal repeat contains an unusual element that induces the synthesis of short RNAs from various mRNA and snRNA promoters. Genes Dev. 4:1990;2061-2074
    • (1990) Genes Dev. , vol.4 , pp. 2061-2074
    • Ratnasabapathy, R.1    Sheldon, M.2    Johal, L.3    Hernandez, N.4
  • 51
    • 0027447687 scopus 로고
    • Elongation factor SII-dependent transcription by RNA polymerase II through a sequence-specific DNA-binding protein
    • Reines D., Mote J.J. Elongation factor SII-dependent transcription by RNA polymerase II through a sequence-specific DNA-binding protein. Proc. Natl Acad. Sci. USA. 90:1993;1917-1921
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1917-1921
    • Reines, D.1    Mote, J.J.2
  • 53
    • 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., Sodoroski J.G., Haseltine W.A. The location of cis-acting regulatory sequences in the human T cell lymphotropic virus type III (HTLV-III/LAV) long terminal repeat. Cell. 41:1985;813-823
    • (1985) Cell , vol.41 , pp. 813-823
    • Rosen, C.A.1    Sodoroski, J.G.2    Haseltine, W.A.3
  • 55
  • 56
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D.B., Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene Dev. 67:1988;31-40
    • (1988) Gene Dev. , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 57
    • 0026775612 scopus 로고
    • SPT4, spt5 and spt6 interactions: Effects on transcription and viability in Saccharomyces cerevisiae
    • Swanson M.S., Winston F. SPT4, spt5 and spt6 interactions effects on transcription and viability in Saccharomyces cerevisiae. Genetics. 132:1992;325-336
    • (1992) Genetics , vol.132 , pp. 325-336
    • Swanson, M.S.1    Winston, F.2
  • 58
    • 0025117930 scopus 로고
    • SPT6, an essential gene that effects transcription in Saccharomyces cerevisiae, encodes a nuclear protein with an extremely acidic amino terminus
    • Swanson M.S., Carlson M., Winston F. SPT6, an essential gene that effects transcription in Saccharomyces cerevisiae, encodes a nuclear protein with an extremely acidic amino terminus. Mol. Cell Biol. 10:1990;4935-4941
    • (1990) Mol. Cell Biol. , vol.10 , pp. 4935-4941
    • Swanson, M.S.1    Carlson, M.2    Winston, F.3
  • 59
    • 0026208983 scopus 로고
    • SPT5, an essential gene important for normal transcription in Saccharomyces cerevisiae, encodes an acidic nuclear protein with a carboxy-terminal repeat
    • Swanson M.S., Malone E.A., Winston F. SPT5, an essential gene important for normal transcription in Saccharomyces cerevisiae, encodes an acidic nuclear protein with a carboxy-terminal repeat. Mol. Cell Biol. 11:1991;3009-3019
    • (1991) Mol. Cell Biol. , vol.11 , pp. 3009-3019
    • Swanson, M.S.1    Malone, E.A.2    Winston, F.3
  • 60
    • 0027253864 scopus 로고
    • A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast
    • Thompson C.M., Koleske A.J., Chao D.M., Young R.A. A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast. Cell. 73:1993;1361-1375
    • (1993) Cell , vol.73 , pp. 1361-1375
    • Thompson, C.M.1    Koleske, A.J.2    Chao, D.M.3    Young, R.A.4
  • 61
    • 0027135208 scopus 로고
    • Locus-specific variation in phosphorylation state of RNA polymerase II in vivo: Correlations with gene activity and transcript processing
    • Weeks J.R., Hardin S.E., Shen J., Lee J.M., Greenleaf A.L. Locus-specific variation in phosphorylation state of RNA polymerase II in vivo correlations with gene activity and transcript processing. Genes Dev. 7:1993;2329-2344
    • (1993) Genes Dev. , vol.7 , pp. 2329-2344
    • Weeks, J.R.1    Hardin, S.E.2    Shen, J.3    Lee, J.M.4    Greenleaf, A.L.5
  • 62
    • 0026066839 scopus 로고
    • Tat regulates binding of the human immunodeficiency virus trans-activating RNA loop-binding protein TRP-185
    • Wu F., Garcia J., Sigman D., Gaynor R.B. Tat regulates binding of the human immunodeficiency virus trans-activating RNA loop-binding protein TRP-185. Genes Dev. 5:1991;2128-2140
    • (1991) Genes Dev. , vol.5 , pp. 2128-2140
    • Wu, F.1    Garcia, J.2    Sigman, D.3    Gaynor, R.B.4
  • 63
    • 0028844508 scopus 로고
    • The cellular factor TRP-185 regulates RNA polymerase II binding to HIV-1 TAR RNA
    • Wu-Baer F., Lane W., Gaynor R.B. The cellular factor TRP-185 regulates RNA polymerase II binding to HIV-1 TAR RNA. EMBO J. 14:1995;5995-6009
    • (1995) EMBO J. , vol.14 , pp. 5995-6009
    • Wu-Baer, F.1    Lane, W.2    Gaynor, R.B.3
  • 64
    • 0029080295 scopus 로고
    • Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat
    • Wu-Baer F., Sigman D., Gaynor R.B. Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat. Proc. Natl Acad. Sci. USA. 92:1995;6213-6217
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6213-6217
    • Wu-Baer, F.1    Sigman, D.2    Gaynor, R.B.3
  • 66
    • 0029943536 scopus 로고    scopus 로고
    • The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function
    • Yang X., Herrmann C.H., Rice A.P. The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function. J. Virol. 70:1996;4576-4584
    • (1996) J. Virol. , vol.70 , pp. 4576-4584
    • Yang, X.1    Herrmann, C.H.2    Rice, A.P.3
  • 67
    • 0028236808 scopus 로고
    • Transcriptional elongation by RNA polymerase II is stimulated by transactivators
    • Yankulov K., Blau J., Purton T., Roberts S., Bentley D.L. Transcriptional elongation by RNA polymerase II is stimulated by transactivators. Cell. 77:1994;749-759
    • (1994) Cell , vol.77 , pp. 749-759
    • Yankulov, K.1    Blau, J.2    Purton, T.3    Roberts, S.4    Bentley, D.L.5
  • 68
    • 0028859150 scopus 로고
    • Novel mechanism and factor for regulation by HIV-1 Tat
    • Zhou Q., Sharp P.A. Novel mechanism and factor for regulation by HIV-1 Tat. EMBO J. 14:1995;321-328
    • (1995) EMBO J. , vol.14 , pp. 321-328
    • Zhou, Q.1    Sharp, P.A.2
  • 69
    • 0029834383 scopus 로고    scopus 로고
    • Tat-SF1: Cofactor for stimulation of transcriptional elongation by HIV-1 Tat
    • Zhou Q., Sharp P.A. Tat-SF1 cofactor for stimulation of transcriptional elongation by HIV-1 Tat. Science. 274:1996;605-610
    • (1996) Science , vol.274 , pp. 605-610
    • Zhou, Q.1    Sharp, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.