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Volumn 11, Issue 3, 1999, Pages 342-346

Mechanism and regulation of transcriptional elongation by RNA polymerase II

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; RNA POLYMERASE II; TRANSCRIPTION FACTOR;

EID: 0033151808     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80047-7     Document Type: Review
Times cited : (70)

References (56)
  • 1
    • 0028236808 scopus 로고
    • Transcriptional elongation by RNA polymerase II is stimulated by transactivators
    • Yankulov K, Blau J, Purton T, Roberts S, Bentley DL: Transcriptional elongation by RNA polymerase II is stimulated by transactivators. Cell 1994, 77:749-759.
    • (1994) Cell , vol.77 , pp. 749-759
    • Yankulov, K.1    Blau, J.2    Purton, T.3    Roberts, S.4    Bentley, D.L.5
  • 2
    • 0028924386 scopus 로고
    • Promoter-proximal pausing of RNA polymerase II defines a general rate-limiting step after transcription initiation
    • Krumm A, Hickey LB, Groudine M: Promoter-proximal pausing of RNA polymerase II defines a general rate-limiting step after transcription initiation. Genes Dev 1995, 9:559-572.
    • (1995) Genes Dev , vol.9 , pp. 559-572
    • Krumm, A.1    Hickey, L.B.2    Groudine, M.3
  • 3
    • 0032101064 scopus 로고    scopus 로고
    • Transcriptional activation domains stimulate initiation and elongation at different times and via different residues
    • Brown SA, Weirich CS, Newton EM, Kingston RE: Transcriptional activation domains stimulate initiation and elongation at different times and via different residues. EMBO J 1998, 17:3146-3154. This paper presents evidence that some transcriptional activation domains have distinct subdomains responsible for their effects on transcription initiation and elongation. These findings provide important insight into the nature of DNA binding transactivators and how they function in the regulation of elongation by pol II.
    • (1998) EMBO J , vol.17 , pp. 3146-3154
    • Brown, S.A.1    Weirich, C.S.2    Newton, E.M.3    Kingston, R.E.4
  • 4
    • 0031008221 scopus 로고    scopus 로고
    • Basic mechanisms of transcript elongation and its regulation
    • Uptain SM, Kane CM, Chamberlin MJ: Basic mechanisms of transcript elongation and its regulation. Annu Rev Biochem 1997, 66:117-172.
    • (1997) Annu Rev Biochem , vol.66 , pp. 117-172
    • Uptain, S.M.1    Kane, C.M.2    Chamberlin, M.J.3
  • 5
    • 0030989229 scopus 로고    scopus 로고
    • Mechanism and regulation of transcriptional elongation and termination by RNA polymerase II
    • Shilatifard A, Conaway JW, Conaway RC: Mechanism and regulation of transcriptional elongation and termination by RNA polymerase II. Curr Opin Genet Dev 1997, 7:199-204.
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 199-204
    • Shilatifard, A.1    Conaway, J.W.2    Conaway, R.C.3
  • 6
    • 0030822591 scopus 로고    scopus 로고
    • Cockayne syndrome group B protein enhances elongation by RNA polymerase II
    • Selby CP, Sancar A: Cockayne syndrome group B protein enhances elongation by RNA polymerase II. Proc Natl Acad Sci USA 1997, 94:11205-11209. This paper reports the discovery that the CSB protein is a pol II elongation factor. The authors present evidence that CSB stimulates the overall rate of elongation by suppressing transient pausing by pol II.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11205-11209
    • Selby, C.P.1    Sancar, A.2
  • 7
    • 0032498273 scopus 로고    scopus 로고
    • FACT, a factor that facilitates transcript elongation through nucleosomes
    • Orphanides G, Leroy G, Chang CH, Luse DS, Reinberg D: FACT, a factor that facilitates transcript elongation through nucleosomes. Cell 1998, 92:105-116. See annotation [8•].
    • (1998) Cell , vol.92 , pp. 105-116
    • Orphanides, G.1    Leroy, G.2    Chang, C.H.3    Luse, D.S.4    Reinberg, D.5
  • 8
    • 0032484098 scopus 로고    scopus 로고
    • Requirement of RSF and FACT for transcription of chromatin templates in vitro
    • Leroy G, Orphanides G, Lane WS, Reinberg D: Requirement of RSF and FACT for transcription of chromatin templates in vitro. Science 1998, 282:1900-1904. These papers by Orphanides et al. [7•] and Leroy et al. [8•] report reconstitution with purified proteins of promoter-dependent transcription by pol II on nucleosomal templates. In addition, the authors report discovery of a novel elongation factor, FACT, required for this process.
    • (1998) Science , vol.282 , pp. 1900-1904
    • Leroy, G.1    Orphanides, G.2    Lane, W.S.3    Reinberg, D.4
  • 9
    • 0032190621 scopus 로고    scopus 로고
    • The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor
    • Li XY, Green MR: The HIV-1 Tat cellular coactivator Tat-Sf1 is a general transcription elongation factor. Genes Dev 1998, 12:2992-2996. This paper reports the discovery that Tat-SF1, which was originally identified as a Tat binding protein, is a pol II elongation factor. The authors present evidence that Tat-SF1 stimulates the overall rate of elongation by suppressing transient pausing by pol II.
    • (1998) Genes Dev , vol.12 , pp. 2992-2996
    • Li, X.Y.1    Green, M.R.2
  • 10
    • 0017172263 scopus 로고
    • Purification of a factor from Ehrlich Ascites tumor cells specifically stimulating RNA polymerase II
    • Sekimizu K, Kobayashi N, Mizuno D, Natori S: Purification of a factor from Ehrlich Ascites tumor cells specifically stimulating RNA polymerase II. Biochemistry 1976, 15:5064-5070.
    • (1976) Biochemistry , vol.15 , pp. 5064-5070
    • Sekimizu, K.1    Kobayashi, N.2    Mizuno, D.3    Natori, S.4
  • 11
    • 0000701273 scopus 로고
    • Nascent RNA cleavage by transcription elongation complexes
    • Edited by Conaway RC, Conaway JW. New York: Raven Press
    • Reines D: Nascent RNA cleavage by transcription elongation complexes. In Transcription: Mechanisms and Regulation. Edited by Conaway RC, Conaway JW. New York: Raven Press; 1994:263-278.
    • (1994) Transcription: Mechanisms and Regulation , pp. 263-278
    • Reines, D.1
  • 12
    • 0026672441 scopus 로고
    • Genetic interaction between transcription elongation factor TFIIS and RNA polymerase II
    • Archambault J, Lacroute F, Ruet A, Friesen JD: Genetic interaction between transcription elongation factor TFIIS and RNA polymerase II. Mol Cell Biol 1992, 12:4142-4152.
    • (1992) Mol Cell Biol , vol.12 , pp. 4142-4152
    • Archambault, J.1    Lacroute, F.2    Ruet, A.3    Friesen, J.D.4
  • 13
    • 0013623707 scopus 로고
    • 6-azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae
    • Exinger G, Lacroute F: 6-azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae. Curr Genet 1992, 142:749-759.
    • (1992) Curr Genet , vol.142 , pp. 749-759
    • Exinger, G.1    Lacroute, F.2
  • 14
    • 0029858912 scopus 로고    scopus 로고
    • In vitro characterization of mutant yeast RNA polymerase II with reduced binding for elongation factor TFIIS
    • Wu J, Awrey DE, Edwards AM, Archambault J, Friesen JD: In vitro characterization of mutant yeast RNA polymerase II with reduced binding for elongation factor TFIIS. Proc Natl Acad Sci USA 1996, 93:11552-11557.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11552-11557
    • Wu, J.1    Edwards, A.M.2    Archambault, J.3    Friesen, J.D.4
  • 16
    • 0031684847 scopus 로고    scopus 로고
    • Mutations in RNA polymerase II and elongation factor SII severely reduce mRNA levels in Saccharomyces cerevisiae
    • Lennon JC, Wind M, Saunders L, Hock MB, Reines D: Mutations in RNA polymerase II and elongation factor SII severely reduce mRNA levels in Saccharomyces cerevisiae. Mol Cell Biol 1998, 18:5771-5779. This paper reports identification of specific genes whose transcription depends upon the elongation factor SII. The authors' findings set the stage for development of gene-specific assays for SII-dependent elongation in vivo and in vitro.
    • (1998) Mol Cell Biol , vol.18 , pp. 5771-5779
    • Lennon, J.C.1    Wind, M.2    Saunders, L.3    Hock, M.B.4    Reines, D.5
  • 17
    • 0029862975 scopus 로고    scopus 로고
    • Mutations in the second largest subunit of RNA polymerase II cause 6-azauracil sensitivity in yeast and increased transcriptional arrest in vitro
    • Powell W, Reines D: Mutations in the second largest subunit of RNA polymerase II cause 6-azauracil sensitivity in yeast and increased transcriptional arrest in vitro. J Biol Chem 1996, 271:6866-6873.
    • (1996) J Biol Chem , vol.271 , pp. 6866-6873
    • Powell, W.1    Reines, D.2
  • 19
    • 0032971711 scopus 로고    scopus 로고
    • Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation
    • Otero G, Fellows J, Li Y, De Bizemont T, Dirac A, Gustafsson C, Erdjument-Bromage H, Tempst P, Svejstrup JQ: Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Mol Cell 1999. 3:125-129. These papers by Svejstrup et al. [18•] and Otero et al. [19•] report discovery and purification of elongator from yeast. Interaction of elongator with pol II is shown to be regulated by phosphorylation of the pol II CTD. In addition, the authors present genetic evidence that elongator is involved in transcription elongation and activation in vivo.
    • (1999) Mol Cell , vol.3 , pp. 125-129
    • Otero, G.1    Fellows, J.2    Li, Y.3    De Bizemont, T.4    Dirac, A.5    Gustafsson, C.6    Erdjument-Bromage, H.7    Tempst, P.8    Svejstrup, J.Q.9
  • 20
    • 0017851222 scopus 로고
    • DRB-induced premature termination of late adenovirus transcription
    • Fraser NW, Sehgal PB, Darnell JE: DRB-induced premature termination of late adenovirus transcription. Nature 1978. 272:590-593.
    • (1978) Nature , vol.272 , pp. 590-593
    • Fraser, N.W.1    Sehgal, P.B.2    Darnell, J.E.3
  • 21
    • 0024561487 scopus 로고
    • 5,6-Dichloro-1-β-D-ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro
    • Chodosh LA, Fire A, Samuels M, Sharp PA: 5,6-Dichloro-1-β-D-ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro. J Biol Chem 1989, 264:2250-2257.
    • (1989) J Biol Chem , vol.264 , pp. 2250-2257
    • Chodosh, L.A.1    Fire, A.2    Samuels, M.3    Sharp, P.A.4
  • 22
    • 0025761244 scopus 로고
    • Blocking of tat-dependent HIV-1 RNA modification by an inhibitor of RNA polymerase II processivity
    • Braddock M, Thorburn AM, Kingsman AJ, Kingsman SM: Blocking of tat-dependent HIV-1 RNA modification by an inhibitor of RNA polymerase II processivity. Nature 1991, 350:439-441.
    • (1991) Nature , vol.350 , pp. 439-441
    • Braddock, M.1    Thorburn, A.M.2    Kingsman, A.J.3    Kingsman, S.M.4
  • 23
    • 0026064723 scopus 로고
    • HIV-1 tat protein promotes formation of more-processive elongation complexes
    • Marciniak RA, Sharp PA: HIV-1 tat protein promotes formation of more-processive elongation complexes. EMBO J 1991, 10:4189-4196.
    • (1991) EMBO J , vol.10 , pp. 4189-4196
    • Marciniak, R.A.1    Sharp, P.A.2
  • 24
    • 14444275279 scopus 로고    scopus 로고
    • DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and SptS homologs
    • Wada T, Takagi T, YAmaguchi Y, Ferdous A, Imai T, Hirose S, SUgimoto S, Yano K, Hartzog GA, Winston F et al.: DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and SptS homologs. Genes Dev 1998, 12:343-356. See annotation [27•].
    • (1998) Genes Dev , vol.12 , pp. 343-356
    • Wada, T.1    Takagi, T.2    Yamaguchi, Y.3    Ferdous, A.4    Imai, T.5    Hirose, S.6    Sugimoto, S.7    Yano, K.8    Hartzog, G.A.9    Winston, F.10
  • 25
    • 0026775612 scopus 로고
    • SPT4, SPT5, and SPT6 interactions: Effects on transcription and viability in Saccharomyces cerevisiae
    • Swanson MS, Winston F: SPT4, SPT5, and SPT6 interactions: Effects on transcription and viability in Saccharomyces cerevisiae. Genetics 1992, 132:325-336.
    • (1992) Genetics , vol.132 , pp. 325-336
    • Swanson, M.S.1    Winston, F.2
  • 26
    • 0032004953 scopus 로고    scopus 로고
    • Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae
    • Hartzog GA, Wada T, HAnda H, Winston F: Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev 1998, 12:357-369. See annotation [27•].
    • (1998) Genes Dev , vol.12 , pp. 357-369
    • Hartzog, G.A.1    Wada, T.2    Handa, H.3    Winston, F.4
  • 27
    • 0032534814 scopus 로고    scopus 로고
    • Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro
    • Wada T, Takagi T, YAmaguchi Y, Watanabe D, HAnda H: Evidence that P-TEFb alleviates the negative effect of DSIF on RNA polymerase II-dependent transcription in vitro. EMBO J 1998, 17:7395-7403. Together, the papers by Wada et al. [24•,27•] and Hartzog et al. [26•] provide genetic and biochemical evidence that DSIF (Spt4-Spt5), the DRB-sensitivity inducing factor, is a negative regulator of elongation by pol II. In addition, Wada et al. [27•] demonstrate that the positive elongation factor P-TEFb functions at least in part by counteracting the activity of DSIF.
    • (1998) EMBO J , vol.17 , pp. 7395-7403
    • Wada, T.1    Takagi, T.2    Yamaguchi, Y.3    Watanabe, D.4    Handa, H.5
  • 29
    • 0032031706 scopus 로고    scopus 로고
    • Identification of multiple cyclin subunits of human P-TEFb
    • Peng J, Zhu Y, Milto JT, Price DH: Identification of multiple cyclin subunits of human P-TEFb. Genes Dev 1998, 12:755-762.
    • (1998) Genes Dev , vol.12 , pp. 755-762
    • Peng, J.1    Zhu, Y.2    Milto, J.T.3    Price, D.H.4
  • 30
    • 0032577577 scopus 로고    scopus 로고
    • Identification of a cyclin subunit required for the function of Drosophila P-TEFb
    • Peng J, Marshall NF, Price DH: Identification of a cyclin subunit required for the function of Drosophila P-TEFb. J Biol Chem 1998, 273:13855-13860.
    • (1998) J Biol Chem , vol.273 , pp. 13855-13860
    • Peng, J.1    Marshall, N.F.2    Price, D.H.3
  • 31
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase
    • Marshall NF, Peng J, Xie Z, Price DH: Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J Biol Chem 1996, 271:27176-27183.
    • (1996) J Biol Chem , vol.271 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, Z.3    Price, D.H.4
  • 32
    • 0032127436 scopus 로고    scopus 로고
    • Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages
    • Zhou Q, Chen D, Pierstorff E, Luo K: Transcription elongation factor P-TEFb mediates Tat activation of HIV-1 transcription at multiple stages. EMBO J 1998, 17:3681-3691.
    • (1998) EMBO J , vol.17 , pp. 3681-3691
    • Zhou, Q.1    Chen, D.2    Pierstorff, E.3    Luo, K.4
  • 33
    • 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 RF, Jeang KT: 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 1996, 271:27888-27894.
    • (1996) J Biol Chem , vol.271 , pp. 27888-27894
    • Chun, R.F.1    Jeang, K.T.2
  • 34
    • 0029956642 scopus 로고    scopus 로고
    • Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain
    • Parada CA, Roeder RG: Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. Nature 1996, 384:375-378.
    • (1996) Nature , vol.384 , pp. 375-378
    • Parada, C.A.1    Roeder, R.G.2
  • 35
    • 0029943536 scopus 로고    scopus 로고
    • The human immunodeficiency virus tat proteins specifically associate with TAK in vivo and require the carboxy-terminal domain of RNA polymerase II for function
    • Yang X, Herrman CH, Rice AP: The human immunodeficiency virus tat proteins specifically associate with TAK in vivo and require the carboxy-terminal domain of RNA polymerase II for function. J Virol 1996, 70:4576-4584.
    • (1996) J Virol , vol.70 , pp. 4576-4584
    • Yang, X.1    Herrman, C.H.2    Rice, A.P.3
  • 36
    • 0031958598 scopus 로고    scopus 로고
    • PITALRE, the catalytic subunit of TAK, is required for human immunodeficiency virus transactivation in vivo
    • Gold MO, Yang X, Herrmann CH, Rice AP: PITALRE, the catalytic subunit of TAK, is required for human immunodeficiency virus transactivation in vivo. J Virol 1998, 72:4448-4453.
    • (1998) J Virol , vol.72 , pp. 4448-4453
    • Gold, M.O.1    Yang, X.2    Herrmann, C.H.3    Rice, A.P.4
  • 37
    • 14444281157 scopus 로고    scopus 로고
    • P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitro
    • Mancebo HSY, Lee G, Flygare J, Tomassini J, Luu P, Zhu Y, Peng J, Blau C, Price DH, Flores O: P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitro. Genes Dev 1997, 11:2633-2644. These papers by Zhu et al. [28•] and Mancebo et al. [37•] elegantly demonstrate that the pol II CTD kinase P-TEFb plays an essential role in Tat-dependent activation of the HIV-1 mRNA synthesis. This work provides the first direct evidence that P-TEFb regulates expression of specific genes in vivo.
    • (1997) Genes Dev , vol.11 , pp. 2633-2644
    • Mancebo, H.S.Y.1    Lee, G.2    Flygare, J.3    Tomassini, J.4    Luu, P.5    Zhu, Y.6    Peng, J.7    Blau, C.8    Price, D.H.9    Flores, O.10
  • 38
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9 associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • Wei P, Garber ME, Fang S, Fischer WH, Jones KA: A novel CDK9 associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 1998, 92:451-462. See annotation [39•].
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.3    Fischer, W.H.4    Jones, K.A.5
  • 39
    • 0033574077 scopus 로고    scopus 로고
    • Interactions between human cyclin T, Tat and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T
    • Fujinaga K, Taube R, Wimmer J, Cujec TP, Peterlin BM: Interactions between human cyclin T, Tat and the transactivation response element (TAR) are disrupted by a cysteine to tyrosine substitution found in mouse cyclin T. Proc Natl Acad Sci USA 1999, 96:1285-1290. These papers by Wei et al. [38•] and Fujinaga et al. [39•] demonstrate that human, but not mouse, cyclin T interacts with the HIV-1 Tat protein and mediates its binding to the TAR element in the HIV-1 polyprotein transcript. This finding provides a mechanistic explanation for the long-standing observation that the HIV-1 is capable of infecting human but not rodent cells.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1285-1290
    • Fujinaga, K.1    Taube, R.2    Wimmer, J.3    Cujec, T.P.4    Peterlin, B.M.5
  • 40
    • 0030013201 scopus 로고    scopus 로고
    • Relationships between DNA repair and transcription
    • Friedberg EC: Relationships between DNA repair and transcription. Annu Rev Biochem 1996, 65:15-42.
    • (1996) Annu Rev Biochem , vol.65 , pp. 15-42
    • Friedberg, E.C.1
  • 42
    • 0031980940 scopus 로고    scopus 로고
    • The insertion/deletion phenotype in somatic hypermutation and a new model for somatic hypermutation
    • Wilson PC, Capra JD: The insertion/deletion phenotype in somatic hypermutation and a new model for somatic hypermutation. The Immunologist 1998, 6:48-53.
    • (1998) The Immunologist , vol.6 , pp. 48-53
    • Wilson, P.C.1    Capra, J.D.2
  • 43
    • 0021750302 scopus 로고
    • Cis-acting, recombination-stimulating activity in fragment of the ribosomal DNA of S. cerevisiae
    • Keil RL, Roeder GS: Cis-acting, recombination-stimulating activity in fragment of the ribosomal DNA of S. cerevisiae. Cell 1984, 39:377-386.
    • (1984) Cell , vol.39 , pp. 377-386
    • Keil, R.L.1    Roeder, G.S.2
  • 44
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas BJ, Rothstein R: Elevated recombination rates in transcriptionally active DNA. Cell 1989, 56:619-630.
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2
  • 45
    • 0031439267 scopus 로고    scopus 로고
    • The yeast HPR1 gene has a functional role in transcriptional elongation that uncovers a novel source of genome instability
    • Chavez S, Aguilera A: The yeast HPR1 gene has a functional role in transcriptional elongation that uncovers a novel source of genome instability. Genes Dev 1997, 11:3459-3470. See annotation [53•].
    • (1997) Genes Dev , vol.11 , pp. 3459-3470
    • Chavez, S.1    Aguilera, A.2
  • 47
    • 0030667078 scopus 로고    scopus 로고
    • Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes
    • Tantin D, Kansal A, Carey M: Recruitment of the putative transcription-repair coupling factor CSB/ERCC6 to RNA polymerase II elongation complexes. Mol Cell Biol 1997, 17:6803-6814.
    • (1997) Mol Cell Biol , vol.17 , pp. 6803-6814
    • Tantin, D.1    Kansal, A.2    Carey, M.3
  • 48
    • 0025212715 scopus 로고
    • HPR1, a novel yeast gene that prevents intrachromosomal excision recombination, shows carboxy-terminal homology to the Saccharomyces cerevisiae TOP1 gene
    • Aguilera A, Klein HL: HPR1, a novel yeast gene that prevents intrachromosomal excision recombination, shows carboxy-terminal homology to the Saccharomyces cerevisiae TOP1 gene. Mol Cell Biol 1990, 10:1439-1451.
    • (1990) Mol Cell Biol , vol.10 , pp. 1439-1451
    • Aguilera, A.1    Klein, H.L.2
  • 49
    • 0027945129 scopus 로고
    • Increase in incidence of chromosome instability and non-conservative recombination between repeats in Saccharomyces cerevisiae hpr1 delta strains
    • Santos-Rosa H, Aguilera A: Increase in incidence of chromosome instability and non-conservative recombination between repeats in Saccharomyces cerevisiae hpr1 delta strains. Mol Gen Genet 1994, 245:224-236.
    • (1994) Mol Gen Genet , vol.245 , pp. 224-236
    • Santos-Rosa, H.1    Aguilera, A.2
  • 50
    • 0010173139 scopus 로고    scopus 로고
    • A novel yeast gene, THO2, is involved in RNA pol II transcription and provides new evidence for transcriptional elongation-associated recombination
    • Piruat JI, Aguilera A: A novel yeast gene, THO2, is involved in RNA pol II transcription and provides new evidence for transcriptional elongation-associated recombination. EMBO J 1998, 17:4859-4872. See annotation [53•].
    • (1998) EMBO J , vol.17 , pp. 4859-4872
    • Piruat, J.I.1    Aguilera, A.2
  • 51
    • 0029670585 scopus 로고    scopus 로고
    • Mutations in the RNA polymerase II transcription machinery suppress the hyperrecombination mutant hpr1 delta of Saccharomyces cerevisiae
    • Fan HY, Cheng KK, Klein KL: Mutations in the RNA polymerase II transcription machinery suppress the hyperrecombination mutant hpr1 delta of Saccharomyces cerevisiae. Genetics 1996, 142:749-759.
    • (1996) Genetics , vol.142 , pp. 749-759
    • Fan, H.Y.1    Cheng, K.K.2    Klein, K.L.3
  • 52
    • 0032907104 scopus 로고    scopus 로고
    • A complex containing RNA polymerase II, paf1p, cdc73p, hpr1p, and ccr4p plays a role in protein kinase C signalling
    • Chang M, French-Cornay D, Fan H, Klein H, Denis C, Jaehning JA: A complex containing RNA polymerase II, paf1p, cdc73p, hpr1p, and ccr4p plays a role in protein kinase C signalling. Mol Cell Biol 1999, 19:1056-1067.
    • (1999) Mol Cell Biol , vol.19 , pp. 1056-1067
    • Chang, M.1    French-Cornay, D.2    Fan, H.3    Klein, H.4    Denis, C.5    Jaehning, J.A.6
  • 53
    • 0030959070 scopus 로고    scopus 로고
    • Recombination between DNA repeats in yeast hpr1δ cells is linked to transcription elongation
    • Prado F, Piruat JI, Aguilera A: Recombination between DNA repeats in yeast hpr1δ cells is linked to transcription elongation. EMBO J 1997, 16:2826-2835. Together, these papers by Chavez and Aguilera [45•], Piruat and Aguilera [50•], and Prado et al. [53•] make a strong case for a mechanistic connection between elongation by pol II, recombination, and maintenance of genome stability. In addition, the authors findings implicate the HPR1 and THO2 gene products in control of transcription elongation in cells.
    • (1997) EMBO J , vol.16 , pp. 2826-2835
    • Prado, F.1    Piruat, J.I.2    Aguilera, A.3
  • 54
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman JL, Kingston RE: Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu Rev Biochem 1998, 67:545-579.
    • (1998) Annu Rev Biochem , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 55
    • 0030713405 scopus 로고    scopus 로고
    • Disruption of downstream chromatin directed by a transcriptional activator
    • Brown SA, Kingston RE: Disruption of downstream chromatin directed by a transcriptional activator. Genes Dev 1997. 11:3116-3121.
    • (1997) Genes Dev , vol.11 , pp. 3116-3121
    • Brown, S.A.1    Kingston, R.E.2
  • 56
    • 0029759928 scopus 로고    scopus 로고
    • Activator-dependent regulation of transcriptional pausing on nucleosomal templates
    • Brown SA, Imbalzano AN, Kingston RE: Activator-dependent regulation of transcriptional pausing on nucleosomal templates. Genes Dev 1996, 10:1479-1490.
    • (1996) Genes Dev , vol.10 , pp. 1479-1490
    • Brown, S.A.1    Imbalzano, A.N.2    Kingston, R.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.