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Volumn 1677, Issue 1-3, 2004, Pages 64-73

The RNA polymerase II transcription cycle: Cycling through chromatin

Author keywords

C terminal domain (CTD); Promoter clearance; RNA processing; Transcript elongation; Transcription cycle

Indexed keywords

RNA POLYMERASE II;

EID: 1542328272     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbaexp.2003.10.012     Document Type: Review
Times cited : (75)

References (115)
  • 1
    • 0036901957 scopus 로고    scopus 로고
    • Cyclin dependent kinases and cell cycle control (nobel lecture)
    • Nurse P. Cyclin dependent kinases and cell cycle control (nobel lecture). ChemBioChem. 3:2002;596-603.
    • (2002) ChemBioChem , vol.3 , pp. 596-603
    • Nurse, P.1
  • 3
    • 0025844906 scopus 로고
    • Structural changes in nucleosomes during transcription: Strip, split or flip?
    • Thoma F. Structural changes in nucleosomes during transcription: strip, split or flip? Trends Genet. 7:1991;175-177.
    • (1991) Trends Genet. , vol.7 , pp. 175-177
    • Thoma, F.1
  • 4
  • 5
    • 0037326318 scopus 로고    scopus 로고
    • Rescue of arrested RNA polymerase II complexes
    • Svejstrup J.Q. Rescue of arrested RNA polymerase II complexes. J. Cell Sci. 116:2003;447-451.
    • (2003) J. Cell Sci. , vol.116 , pp. 447-451
    • Svejstrup, J.Q.1
  • 6
    • 0036591882 scopus 로고    scopus 로고
    • The mRNA assembly line: Transcription and processing machines in the same factory
    • Bentley D. The mRNA assembly line: transcription and processing machines in the same factory. Curr. Opin. Cell Biol. 14:2002;336-342.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 336-342
    • Bentley, D.1
  • 7
    • 0037154967 scopus 로고    scopus 로고
    • Integrating mRNA processing with transcription
    • Proudfoot N.J., Furger A., Dye M.J. Integrating mRNA processing with transcription. Cell. 108:2002;501-512.
    • (2002) Cell , vol.108 , pp. 501-512
    • Proudfoot, N.J.1    Furger, A.2    Dye, M.J.3
  • 8
    • 0034826968 scopus 로고    scopus 로고
    • The eukaryotic gene transcription machinery
    • Kornberg R.D. The eukaryotic gene transcription machinery. Biol. Chem. 382:2001;1103-1107.
    • (2001) Biol. Chem. , vol.382 , pp. 1103-1107
    • Kornberg, R.D.1
  • 9
    • 0032450899 scopus 로고    scopus 로고
    • Role of general and gene-specific cofactors in the regulation of eukaryotic transcription
    • Roeder R.G. Role of general and gene-specific cofactors in the regulation of eukaryotic transcription. Cold Spring Harbor Symp. Quant. Biol. 63:1998;201-218.
    • (1998) Cold Spring Harbor Symp. Quant. Biol. , vol.63 , pp. 201-218
    • Roeder, R.G.1
  • 11
    • 0033542484 scopus 로고    scopus 로고
    • Enhancement of TBP binding by activators and general transcription factors
    • Li X.Y., Virbasius A., Zhu X., Green M.R. Enhancement of TBP binding by activators and general transcription factors. Nature. 399:1999;605-609.
    • (1999) Nature , vol.399 , pp. 605-609
    • Li, X.Y.1    Virbasius, A.2    Zhu, X.3    Green, M.R.4
  • 12
    • 0033542436 scopus 로고    scopus 로고
    • Binding of TBP to promoters in vivo is stimulated by activators and requires Pol II holoenzyme
    • Kuras L., Struhl K. Binding of TBP to promoters in vivo is stimulated by activators and requires Pol II holoenzyme. Nature. 399:1999;609-613.
    • (1999) Nature , vol.399 , pp. 609-613
    • Kuras, L.1    Struhl, K.2
  • 13
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • McNally J.G., Muller W.G., Walker D., Wolford R., Hager G.L. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science. 287:2000;1262-1265.
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 15
    • 0033681250 scopus 로고    scopus 로고
    • Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter
    • Agalioti T., Lomvardas S., Parekh B., Yie J., Maniatis T., Thanos D. Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter. Cell. 103:2000;667-678.
    • (2000) Cell , vol.103 , pp. 667-678
    • Agalioti, T.1    Lomvardas, S.2    Parekh, B.3    Yie, J.4    Maniatis, T.5    Thanos, D.6
  • 16
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer P., Bushnell D.A., Kornberg R.D. Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science. 292:2001;1863-1876.
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 17
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 a resolution
    • Gnatt A.L., Cramer P., Fu J., Bushnell D.A., Kornberg R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 A resolution. Science. 292:2001;1876-1882.
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 18
    • 0030014797 scopus 로고    scopus 로고
    • Two-dimensional crystallography of TFIIB- and IIE-RNA polymerase II complexes: Implications for start site selection and initiation complex formation
    • Leuther K.K., Bushnell D.A., Kornberg R.D. Two-dimensional crystallography of TFIIB- and IIE-RNA polymerase II complexes: implications for start site selection and initiation complex formation. Cell. 85:1996;773-779.
    • (1996) Cell , vol.85 , pp. 773-779
    • Leuther, K.K.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 19
    • 0029807310 scopus 로고    scopus 로고
    • A minimal set of RNA polymerase II transcription protein interactions
    • Bushnell D.A., Bamdad C., Kornberg R.D. A minimal set of RNA polymerase II transcription protein interactions. J. Biol. Chem. 271:1996;20170-20174.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20170-20174
    • Bushnell, D.A.1    Bamdad, C.2    Kornberg, R.D.3
  • 20
    • 0026731557 scopus 로고
    • Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II
    • Lu H., Zawel L., Fisher L., Egly J.M., Reinberg D. Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II. Nature. 358:1992;641-645.
    • (1992) Nature , vol.358 , pp. 641-645
    • Lu, H.1    Zawel, L.2    Fisher, L.3    Egly, J.M.4    Reinberg, D.5
  • 21
    • 0028293210 scopus 로고
    • Regulation of TFIIH ATPase and kinase activities by TFIIE during active initiation complex formation
    • Ohkuma Y., Roeder R.G. Regulation of TFIIH ATPase and kinase activities by TFIIE during active initiation complex formation. Nature. 368:1994;160-163.
    • (1994) Nature , vol.368 , pp. 160-163
    • Ohkuma, Y.1    Roeder, R.G.2
  • 22
    • 0032059891 scopus 로고    scopus 로고
    • An activator target in the RNA polymerase II holoenzyme
    • Koh S.S., Ansari A.Z., Ptashne M., Young R.A. An activator target in the RNA polymerase II holoenzyme. Mol. Cell. 1:1998;895-904.
    • (1998) Mol. Cell , vol.1 , pp. 895-904
    • Koh, S.S.1    Ansari, A.Z.2    Ptashne, M.3    Young, R.A.4
  • 23
    • 0030033699 scopus 로고    scopus 로고
    • RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling
    • Wilson C.J., Chao D.M., Imbalzano A.N., Schnitzler G.R., Kingston R.E., Young R.A. RNA polymerase II holoenzyme contains SWI/SNF regulators involved in chromatin remodeling. Cell. 84:1996;235-244.
    • (1996) Cell , vol.84 , pp. 235-244
    • Wilson, C.J.1    Chao, D.M.2    Imbalzano, A.N.3    Schnitzler, G.R.4    Kingston, R.E.5    Young, R.A.6
  • 24
    • 15844390393 scopus 로고    scopus 로고
    • A human RNA polymerase II complex associated with SRB and DNA-repair proteins [published erratum appears in Nature 1996 Nov 28;384(6607):384]
    • Maldonado E., Shiekhattar R., Sheldon M., Cho H., Drapkin R., Rickert P., Lees E., Anderson C.W., Linn S., Reinberg D. A human RNA polymerase II complex associated with SRB and DNA-repair proteins [published erratum appears in Nature 1996 Nov 28;384(6607):384]. Nature. 381:1996;86-89.
    • (1996) Nature , vol.381 , pp. 86-89
    • Maldonado, E.1    Shiekhattar, R.2    Sheldon, M.3    Cho, H.4    Drapkin, R.5    Rickert, P.6    Lees, E.7    Anderson, C.W.8    Linn, S.9    Reinberg, D.10
  • 25
    • 0028832869 scopus 로고
    • A mammalian RNA polymerase II holoenzyme containing all components required for promoter-specific transcription initiation
    • Ossipow V., Tassan J.P., Nigg E.A., Schibler U. A mammalian RNA polymerase II holoenzyme containing all components required for promoter-specific transcription initiation. Cell. 83:1995;137-146.
    • (1995) Cell , vol.83 , pp. 137-146
    • Ossipow, V.1    Tassan, J.P.2    Nigg, E.A.3    Schibler, U.4
  • 26
    • 0029074137 scopus 로고
    • Recycling of the general transcription factors during RNA polymerase II transcription
    • Zawel L., Kumar K.P., Reinberg D. Recycling of the general transcription factors during RNA polymerase II transcription. Genes Dev. 9:1995;1479-1490.
    • (1995) Genes Dev. , vol.9 , pp. 1479-1490
    • Zawel, L.1    Kumar, K.P.2    Reinberg, D.3
  • 27
    • 0036241663 scopus 로고    scopus 로고
    • Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo
    • Pokholok D.K., Hannett N.M., Young R.A. Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo. Mol. Cell. 9:2002;799-809.
    • (2002) Mol. Cell , vol.9 , pp. 799-809
    • Pokholok, D.K.1    Hannett, N.M.2    Young, R.A.3
  • 28
    • 0034626731 scopus 로고    scopus 로고
    • A transcription reinitiation intermediate that is stabilized by activator
    • Yudkovsky N., Ranish J.A., Hahn S. A transcription reinitiation intermediate that is stabilized by activator. Nature. 408:2000;225-229.
    • (2000) Nature , vol.408 , pp. 225-229
    • Yudkovsky, N.1    Ranish, J.A.2    Hahn, S.3
  • 30
    • 0036052014 scopus 로고    scopus 로고
    • CTD phosphatase: Role in RNA polymerase II cycling and the regulation of transcript elongation
    • Lin P.S., Marshall N.F., Dahmus M.E. CTD phosphatase: role in RNA polymerase II cycling and the regulation of transcript elongation. Prog. Nucleic Acid Res. Mol. Biol. 72:2002;333-365.
    • (2002) Prog. Nucleic Acid Res. Mol. Biol. , vol.72 , pp. 333-365
    • Lin, P.S.1    Marshall, N.F.2    Dahmus, M.E.3
  • 31
    • 0029760928 scopus 로고    scopus 로고
    • Reversible phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus M.E. Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J. Biol. Chem. 271:1996;19009-19012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19009-19012
    • Dahmus, M.E.1
  • 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
    • 0034964368 scopus 로고    scopus 로고
    • Cdk1 triggers association of RNA polymerase to cell cycle promoters only after recruitment of the mediator by SBF
    • Cosma M.P., Panizza S., Nasmyth K. Cdk1 triggers association of RNA polymerase to cell cycle promoters only after recruitment of the mediator by SBF. Mol. Cell. 7:2001;1213-1220.
    • (2001) Mol. Cell , vol.7 , pp. 1213-1220
    • Cosma, M.P.1    Panizza, S.2    Nasmyth, K.3
  • 34
    • 0036606879 scopus 로고    scopus 로고
    • Human CRSP interacts with RNA polymerase II CTD and adopts a specific CTD-bound conformation
    • Naar A.M., Taatjes D.J., Zhai W., Nogales E., Tjian R. Human CRSP interacts with RNA polymerase II CTD and adopts a specific CTD-bound conformation. Genes Dev. 16:2002;1339-1344.
    • (2002) Genes Dev. , vol.16 , pp. 1339-1344
    • Naar, A.M.1    Taatjes, D.J.2    Zhai, W.3    Nogales, E.4    Tjian, R.5
  • 35
    • 0026715819 scopus 로고
    • Specific interaction between the nonphosphorylated form of RNA polymerase II and the TATA-binding protein
    • Usheva A., Maldonado E., Goldring A., Lu H., Houbavi C., Reinberg D., Aloni Y. Specific interaction between the nonphosphorylated form of RNA polymerase II and the TATA-binding protein. Cell. 69:1992;871-881.
    • (1992) Cell , vol.69 , pp. 871-881
    • Usheva, A.1    Maldonado, E.2    Goldring, A.3    Lu, H.4    Houbavi, C.5    Reinberg, D.6    Aloni, Y.7
  • 36
    • 0030660264 scopus 로고    scopus 로고
    • Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
    • Yue Z., Maldonado E., Pillutla R., Cho H., Reinberg D., Shatkin A.J. Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II. Proc. Natl. Acad. Sci. U. S. A. 94:1997;12898-12903.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12898-12903
    • Yue, Z.1    Maldonado, E.2    Pillutla, R.3    Cho, H.4    Reinberg, D.5    Shatkin, A.J.6
  • 37
    • 0031453408 scopus 로고    scopus 로고
    • MRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Cho E.J., Takagi T., Moore C.R., Buratowski S. mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev. 11:1997;3319-3326.
    • (1997) Genes Dev. , vol.11 , pp. 3319-3326
    • Cho, E.J.1    Takagi, T.2    Moore, C.R.3    Buratowski, S.4
  • 38
    • 0033986862 scopus 로고    scopus 로고
    • Kin28, the TFIIH-associated carboxy-terminal domain kinase, facilitates the recruitment of mRNA processing machinery to RNA polymerase II
    • Rodriguez C.R., Cho E.J., Keogh M.C., Moore C.L., Greenleaf A.L., Buratowski S. Kin28, the TFIIH-associated carboxy-terminal domain kinase, facilitates the recruitment of mRNA processing machinery to RNA polymerase II. Mol. Cell. Biol. 20:2000;104-112.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 104-112
    • Rodriguez, C.R.1    Cho, E.J.2    Keogh, M.C.3    Moore, C.L.4    Greenleaf, A.L.5    Buratowski, S.6
  • 39
    • 0038374526 scopus 로고    scopus 로고
    • Transcriptional elongation control and histone methylation
    • Gerber M., Shilatifard A. Transcriptional elongation control and histone methylation. J. Biol. Chem. 278:2003;26303-26306.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26303-26306
    • Gerber, M.1    Shilatifard, A.2
  • 40
    • 0038740693 scopus 로고    scopus 로고
    • Tails of Intrigue. Phosphorylation of RNA Polymerase II Mediates Histone Methylation
    • Hampsey M., Reinberg D. Tails of Intrigue. Phosphorylation of RNA Polymerase II Mediates Histone Methylation. Cell. 113:2003;429-432.
    • (2003) Cell , vol.113 , pp. 429-432
    • Hampsey, M.1    Reinberg, D.2
  • 42
    • 0033515521 scopus 로고    scopus 로고
    • NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation
    • Yamaguchi Y., Takagi T., Wada T., Yano K., Furuya A., Sugimoto S., Hasegawa J., Handa H. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell. 97:1999;41-51.
    • (1999) Cell , vol.97 , pp. 41-51
    • Yamaguchi, Y.1    Takagi, T.2    Wada, T.3    Yano, K.4    Furuya, A.5    Sugimoto, S.6    Hasegawa, J.7    Handa, H.8
  • 44
    • 0033920260 scopus 로고    scopus 로고
    • Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription
    • Zhou M., Halanski M.A., Radonovich M.F., Kashanchi F., Peng J., Price D.H., Brady J.N. Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription. Mol. Cell. Biol. 20:2000;5077-5086.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5077-5086
    • Zhou, M.1    Halanski, M.A.2    Radonovich, M.F.3    Kashanchi, F.4    Peng, J.5    Price, D.H.6    Brady, J.N.7
  • 45
    • 0035853736 scopus 로고    scopus 로고
    • Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase
    • Kim J.B., Sharp P.A. Positive transcription elongation factor B phosphorylates hSPT5 and RNA polymerase II carboxyl-terminal domain independently of cyclin-dependent kinase-activating kinase. J. Biol. Chem. 276:2001;12317-12323.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12317-12323
    • Kim, J.B.1    Sharp, P.A.2
  • 48
    • 0037470160 scopus 로고    scopus 로고
    • Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality control
    • Pei Y., Schwer B., Shuman S. Interactions between fission yeast Cdk9, its cyclin partner Pch1, and mRNA capping enzyme Pct1 suggest an elongation checkpoint for mRNA quality control. J. Biol. Chem. 278:2003;7180-7188.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7180-7188
    • Pei, Y.1    Schwer, B.2    Shuman, S.3
  • 49
    • 0037205456 scopus 로고    scopus 로고
    • Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5
    • Pei Y., Shuman S. Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5. J. Biol. Chem. 277:2002;19639-19648.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19639-19648
    • Pei, Y.1    Shuman, S.2
  • 50
    • 0033566042 scopus 로고    scopus 로고
    • Transcription elongation factor hSPT5 stimulates mRNA capping
    • Wen Y., Shatkin A.J. Transcription elongation factor hSPT5 stimulates mRNA capping. Genes Dev. 13:1999;1774-1779.
    • (1999) Genes Dev. , vol.13 , pp. 1774-1779
    • Wen, Y.1    Shatkin, A.J.2
  • 51
    • 0242584447 scopus 로고    scopus 로고
    • Regulation of elongating RNA polymerase II by forkhead transcription factors in yeast
    • Morillon A., O'Sullivan J., Azad A., Proudfoot N., Mellor J. Regulation of elongating RNA polymerase II by forkhead transcription factors in yeast. Science. 300:2003;492-495.
    • (2003) Science , vol.300 , pp. 492-495
    • Morillon, A.1    O'Sullivan, J.2    Azad, A.3    Proudfoot, N.4    Mellor, J.5
  • 52
    • 0035963372 scopus 로고    scopus 로고
    • Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms
    • Nguyen V.Q., Co C., Li J.J. Cyclin-dependent kinases prevent DNA re-replication through multiple mechanisms. Nature. 411:2001;1068-1073.
    • (2001) Nature , vol.411 , pp. 1068-1073
    • Nguyen, V.Q.1    Co, C.2    Li, J.J.3
  • 53
    • 0033538531 scopus 로고    scopus 로고
    • Fundamentally different logic of gene regulation in eukaryotes and prokaryotes
    • Struhl K. Fundamentally different logic of gene regulation in eukaryotes and prokaryotes. Cell. 98:1999;1-4.
    • (1999) Cell , vol.98 , pp. 1-4
    • Struhl, K.1
  • 54
    • 0034667792 scopus 로고    scopus 로고
    • Orchestrated response: A symphony of transcription factors for gene control
    • Lemon B., Tjian R. Orchestrated response: a symphony of transcription factors for gene control. Genes Dev. 14:2000;2551-2569.
    • (2000) Genes Dev. , vol.14 , pp. 2551-2569
    • Lemon, B.1    Tjian, R.2
  • 55
    • 0033617334 scopus 로고    scopus 로고
    • Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter
    • Cosma M.P., Tanaka T., Nasmyth K. Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter. Cell. 97:1999;299-311.
    • (1999) Cell , vol.97 , pp. 299-311
    • Cosma, M.P.1    Tanaka, T.2    Nasmyth, K.3
  • 56
    • 0037040550 scopus 로고    scopus 로고
    • Coordination of PIC assembly and chromatin remodeling during differentiation-induced gene activation
    • Soutoglou E., Talianidis I. Coordination of PIC assembly and chromatin remodeling during differentiation-induced gene activation. Science. 295:2002;1901-1904.
    • (2002) Science , vol.295 , pp. 1901-1904
    • Soutoglou, E.1    Talianidis, I.2
  • 57
    • 0036923739 scopus 로고    scopus 로고
    • Dynamics of enhancer-promoter communication during differentiation- induced gene activation
    • Hatzis P., Talianidis I. Dynamics of enhancer-promoter communication during differentiation-induced gene activation. Mol. Cell. 10:2002;1467-1477.
    • (2002) Mol. Cell , vol.10 , pp. 1467-1477
    • Hatzis, P.1    Talianidis, I.2
  • 58
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., Allis C.D. The language of covalent histone modifications. Nature. 403:2000;41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 59
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner B.M. Histone acetylation and an epigenetic code. BioEssays. 22:2000;836-845.
    • (2000) BioEssays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 61
    • 0028053812 scopus 로고
    • Purification and characterization of a phosphatase from HeLa cells which dephosphorylates the C-terminal domain of RNA polymerase II
    • Chambers R.S., Dahmus M.E. Purification and characterization of a phosphatase from HeLa cells which dephosphorylates the C-terminal domain of RNA polymerase II. J. Biol. Chem. 269:1994;26243-26248.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26243-26248
    • Chambers, R.S.1    Dahmus, M.E.2
  • 62
    • 0029043588 scopus 로고
    • The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB
    • Chambers R.S., Wang B.Q., Burton Z.F., Dahmus M.E. The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB. J. Biol. Chem. 270:1995;14962-14969.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14962-14969
    • Chambers, R.S.1    Wang, B.Q.2    Burton, Z.F.3    Dahmus, M.E.4
  • 63
    • 2242454131 scopus 로고    scopus 로고
    • TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphoserines 2 and 5 of RNA polymerase II
    • Lin P.S., Dubois M.F., Dahmus M.E. TFIIF-associating carboxyl-terminal domain phosphatase dephosphorylates phosphoserines 2 and 5 of RNA polymerase II. J. Biol. Chem. 277:2002;45949-45956.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45949-45956
    • Lin, P.S.1    Dubois, M.F.2    Dahmus, M.E.3
  • 65
    • 0029748541 scopus 로고    scopus 로고
    • Purification and characterization of an RNA polymerase II phosphatase from yeast
    • Chambers R.S., Kane C.M. Purification and characterization of an RNA polymerase II phosphatase from yeast. J. Biol. Chem. 271:1996;24498-24504.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24498-24504
    • Chambers, R.S.1    Kane, C.M.2
  • 66
    • 0034685880 scopus 로고    scopus 로고
    • The sensitivity of RNA polymerase II in elongation complexes to C-terminal domain phosphatase
    • Lehman A.L., Dahmus M.E. The sensitivity of RNA polymerase II in elongation complexes to C-terminal domain phosphatase. J. Biol. Chem. 275:2000;14923-14932.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14923-14932
    • Lehman, A.L.1    Dahmus, M.E.2
  • 67
    • 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
  • 68
    • 0024561487 scopus 로고
    • 5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro
    • Chodosh L.A., Fire A., Samuels M., Sharp P.A. 5,6-Dichloro-1-beta-D- ribofuranosylbenzimidazole inhibits transcription elongation by RNA polymerase II in vitro. J. Biol. Chem. 264:1989;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
  • 69
    • 0028787404 scopus 로고
    • The transcriptional elongation inhibitor 5,6-dichloro-1-beta-D- ribofuranosylbenzimidazole inhibits transcription factor IIH-associated protein kinase
    • Yankulov K., Yamashita K., Roy R., Egly J.M., Bentley D.L. The transcriptional elongation inhibitor 5,6-dichloro-1-beta-D- ribofuranosylbenzimidazole inhibits transcription factor IIH-associated protein kinase. J. Biol. Chem. 270:1995;23922-23925.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23922-23925
    • Yankulov, K.1    Yamashita, K.2    Roy, R.3    Egly, J.M.4    Bentley, D.L.5
  • 70
    • 0029942906 scopus 로고    scopus 로고
    • TFIIH functions in regulating transcriptional elongation by RNA polymerase II in Xenopus oocytes
    • Yankulov K.Y., Pandes M., McCracken S., Bouchard D., Bentley D.L. TFIIH functions in regulating transcriptional elongation by RNA polymerase II in Xenopus oocytes. Mol. Cell. Biol. 16:1996;3291-3299.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3291-3299
    • Yankulov, K.Y.1    Pandes, M.2    McCracken, S.3    Bouchard, D.4    Bentley, D.L.5
  • 71
    • 0000337142 scopus 로고    scopus 로고
    • Modulation of RNA polymerase II elongation efficiency by C-terminal heptapeptide repeat domain kinase I
    • Lee J.M., Greenleaf A.L. Modulation of RNA polymerase II elongation efficiency by C-terminal heptapeptide repeat domain kinase I. J. Biol. Chem. 272:1997;10990-10993.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10990-10993
    • Lee, J.M.1    Greenleaf, A.L.2
  • 72
    • 0035893314 scopus 로고    scopus 로고
    • Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain
    • Cho E.J., Kobor M.S., Kim M., Greenblatt J., Buratowski S. Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain. Genes Dev. 15:2001;3319-3329.
    • (2001) Genes Dev. , vol.15 , pp. 3319-3329
    • Cho, E.J.1    Kobor, M.S.2    Kim, M.3    Greenblatt, J.4    Buratowski, S.5
  • 73
    • 0038168110 scopus 로고    scopus 로고
    • A novel RNA polymeras II C-terminal domain phosphatase that preferentially dephosphorylates serine 5
    • Yeo M., Lin P.S., Dahmus M.E., Gill G.N. A novel RNA polymeras II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. J. Biol. Chem. 278:2003;26078-26085.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26078-26085
    • Yeo, M.1    Lin, P.S.2    Dahmus, M.E.3    Gill, G.N.4
  • 75
    • 0034329461 scopus 로고    scopus 로고
    • A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae
    • Chavez S., Beilharz T., Rondon A.G., Erdjument-Bromage H., Tempst P., Svejstrup J.Q., Lithgow T., Aguilera A. A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae. EMBO J. 19:2000;5824-5834.
    • (2000) EMBO J. , vol.19 , pp. 5824-5834
    • Chavez, S.1    Beilharz, T.2    Rondon, A.G.3    Erdjument-Bromage, H.4    Tempst, P.5    Svejstrup, J.Q.6    Lithgow, T.7    Aguilera, A.8
  • 76
    • 0141819093 scopus 로고    scopus 로고
    • Co-transcriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination
    • Huertas P., Aguilera A. Co-transcriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination. Mol. Cell. 12:2003;711-721.
    • (2003) Mol. Cell , vol.12 , pp. 711-721
    • Huertas, P.1    Aguilera, A.2
  • 77
    • 0036469913 scopus 로고    scopus 로고
    • The connection between transcription and genomic instability
    • Aguilera A. The connection between transcription and genomic instability. EMBO J. 21:2002;195-201.
    • (2002) EMBO J. , vol.21 , pp. 195-201
    • Aguilera, A.1
  • 78
    • 0141638443 scopus 로고    scopus 로고
    • Keeping RNA and DNA apart during transcription
    • Svejstrup J.Q. Keeping RNA and DNA apart during transcription. Mol. Cell. 12:2003;538-539.
    • (2003) Mol. Cell , vol.12 , pp. 538-539
    • Svejstrup, J.Q.1
  • 79
    • 0033151808 scopus 로고    scopus 로고
    • Mechanism and regulation of transcriptional elongation by RNA polymerase II
    • Reines D., Conaway R.C., Conaway J.W. Mechanism and regulation of transcriptional elongation by RNA polymerase II. Curr. Opin. Cell Biol. 11:1999;342-346.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 342-346
    • Reines, D.1    Conaway, R.C.2    Conaway, J.W.3
  • 80
    • 0037610786 scopus 로고    scopus 로고
    • The initiation-elongation transition: Lateral mobility of RNA in RNA polymerase II complexes is greatly reduced at +8/+9 and absent by +23
    • Pal M., Luse D.S. The initiation-elongation transition: lateral mobility of RNA in RNA polymerase II complexes is greatly reduced at +8/+9 and absent by +23. Proc. Natl. Acad. Sci. U. S. A. 100:2003;5700-5705.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5700-5705
    • Pal, M.1    Luse, D.S.2
  • 81
    • 0034903279 scopus 로고    scopus 로고
    • Promoter clearance by RNA polymerase II is an extended, multistep process strongly affected by sequence
    • Pal M., McKean D., Luse D.S. Promoter clearance by RNA polymerase II is an extended, multistep process strongly affected by sequence. Mol. Cell. Biol. 21:2001;5815-5825.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5815-5825
    • Pal, M.1    McKean, D.2    Luse, D.S.3
  • 82
    • 0026629273 scopus 로고
    • Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates
    • Izban M.G., Luse D.S. Factor-stimulated RNA polymerase II transcribes at physiological elongation rates on naked DNA but very poorly on chromatin templates. J. Biol. Chem. 267:1992;13647-13655.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13647-13655
    • Izban, M.G.1    Luse, D.S.2
  • 83
    • 0025877255 scopus 로고
    • Transcription on nucleosomal templates by RNA polymerase II in vitro: Inhibition of elongation with enhancement of sequence-specific pausing
    • Izban M.G., Luse D.S. Transcription on nucleosomal templates by RNA polymerase II in vitro: inhibition of elongation with enhancement of sequence-specific pausing. Genes Dev. 5:1991;683-696.
    • (1991) Genes Dev. , vol.5 , pp. 683-696
    • Izban, M.G.1    Luse, D.S.2
  • 84
    • 0032498273 scopus 로고    scopus 로고
    • FACT, a factor that facilitates transcript elongation through nucleosomes
    • Orphanides G., LeRoy G., Chang C.H., Luse D.S., Reinberg D. FACT, a factor that facilitates transcript elongation through nucleosomes. Cell. 92:1998;105-116.
    • (1998) Cell , vol.92 , pp. 105-116
    • Orphanides, G.1    Leroy, G.2    Chang, C.H.3    Luse, D.S.4    Reinberg, D.5
  • 85
    • 0031027465 scopus 로고    scopus 로고
    • Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex distinct from the Srbp-containing holoenzyme
    • Shi X., Chang M., Wolf A.J., Chang C.H., Frazer-Abel A.A., Wade P.A., Burton Z.F., Jaehning J.A. Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex distinct from the Srbp-containing holoenzyme. Mol. Cell. Biol. 17:1997;1160-1169.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1160-1169
    • Shi, X.1    Chang, M.2    Wolf, A.J.3    Chang, C.H.4    Frazer-Abel, A.A.5    Wade, P.A.6    Burton, Z.F.7    Jaehning, J.A.8
  • 90
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • Ng H.H., Robert F., Young R.A., Struhl K. Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol. Cell. 11:2003;709-719.
    • (2003) Mol. Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 91
    • 0033566129 scopus 로고    scopus 로고
    • The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins
    • Orphanides G., Wu W.H., Lane W.S., Hampsey M., Reinberg D. The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Nature. 400:1999;284-288.
    • (1999) Nature , vol.400 , pp. 284-288
    • Orphanides, G.1    Wu, W.H.2    Lane, W.S.3    Hampsey, M.4    Reinberg, D.5
  • 92
    • 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
  • 93
    • 0041828953 scopus 로고    scopus 로고
    • Transcription elongation factors repress transcription initiation from cryptic sites
    • Kaplan C.D., Laprade L., Winston F. Transcription elongation factors repress transcription initiation from cryptic sites. Science. 301:2003;1096-1099.
    • (2003) Science , vol.301 , pp. 1096-1099
    • Kaplan, C.D.1    Laprade, L.2    Winston, F.3
  • 97
    • 0037022226 scopus 로고    scopus 로고
    • Human Elongator facilitates RNA polymerase II transcription through chromatin
    • Kim J.H., Lane W.S., Reinberg D. Human Elongator facilitates RNA polymerase II transcription through chromatin. Proc. Natl. Acad. Sci. U. S. A. 99:2002;1241-1246.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1241-1246
    • Kim, J.H.1    Lane, W.S.2    Reinberg, D.3
  • 98
    • 0037155793 scopus 로고    scopus 로고
    • The Rpb9 subunit of RNA polymerase II binds transcription factor TFIIE and interferes with the SAGA and elongator histone acetyltransferases
    • VanMullem V., Wery M., Werner M., Vandenhaute J., Thuriaux P. The Rpb9 subunit of RNA polymerase II binds transcription factor TFIIE and interferes with the SAGA and elongator histone acetyltransferases. J. Biol. Chem. 277:2002;10220-10225.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10220-10225
    • Vanmullem, V.1    Wery, M.2    Werner, M.3    Vandenhaute, J.4    Thuriaux, P.5
  • 99
    • 0035804653 scopus 로고    scopus 로고
    • Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in transcription elongation in vivo
    • Jona G., Wittschieben B.O., Svejstrup J.Q., Gileadi O. Involvement of yeast carboxy-terminal domain kinase I (CTDK-I) in transcription elongation in vivo. Gene. 267:2001;31-36.
    • (2001) Gene , vol.267 , pp. 31-36
    • Jona, G.1    Wittschieben, B.O.2    Svejstrup, J.Q.3    Gileadi, O.4
  • 100
    • 0036964090 scopus 로고    scopus 로고
    • Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway polymerase passage may degrade chromatin structure
    • Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y., Rhoades A.R., Kaufman P.D., Stillman D.J. Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway polymerase passage may degrade chromatin structure. Genetics. 162:2002;1557-1571.
    • (2002) Genetics , vol.162 , pp. 1557-1571
    • Formosa, T.1    Ruone, S.2    Adams, M.D.3    Olsen, A.E.4    Eriksson, P.5    Yu, Y.6    Rhoades, A.R.7    Kaufman, P.D.8    Stillman, D.J.9
  • 101
    • 0034660330 scopus 로고    scopus 로고
    • Overlapping roles for the histone acetyltransferase activities of SAGA and elongator in vivo
    • Wittschieben B.O., Fellows J., Du W., Stillman D.J., Svejstrup J.Q. Overlapping roles for the histone acetyltransferase activities of SAGA and elongator in vivo. EMBO J. 19:2000;3060-3068.
    • (2000) EMBO J. , vol.19 , pp. 3060-3068
    • Wittschieben, B.O.1    Fellows, J.2    Du, W.3    Stillman, D.J.4    Svejstrup, J.Q.5
  • 103
    • 0037111879 scopus 로고    scopus 로고
    • Requirement of Hos2 histone deacetylase for gene activity in yeast
    • Wang A., Kurdistani S.K., Grunstein M. Requirement of Hos2 histone deacetylase for gene activity in yeast. Science. 298:2002;1412-1414.
    • (2002) Science , vol.298 , pp. 1412-1414
    • Wang, A.1    Kurdistani, S.K.2    Grunstein, M.3
  • 104
    • 0035801706 scopus 로고    scopus 로고
    • Increasing the rate of chromatin remodeling and gene activation-a novel role for the histone acetyltransferase Gcn5
    • Barbaric S., Walker J., Schmid A., Svejstrup J.Q., Horz W. Increasing the rate of chromatin remodeling and gene activation-a novel role for the histone acetyltransferase Gcn5. EMBO J. 20:2001;4944-4951.
    • (2001) EMBO J. , vol.20 , pp. 4944-4951
    • Barbaric, S.1    Walker, J.2    Schmid, A.3    Svejstrup, J.Q.4    Horz, W.5
  • 105
    • 0042431717 scopus 로고    scopus 로고
    • Transcription. Histones face the FACT
    • Svejstrup J.Q. Transcription. Histones face the FACT. Science. 301:2003;1053-1055.
    • (2003) Science , vol.301 , pp. 1053-1055
    • Svejstrup, J.Q.1
  • 106
    • 0038623298 scopus 로고    scopus 로고
    • Localized recruitment of a chromatin-remodeling activity by an activator in vivo drives transcriptional elongation
    • Corey L.L., Weirich C.S., Benjamin I.J., Kingston R.E. Localized recruitment of a chromatin-remodeling activity by an activator in vivo drives transcriptional elongation. Genes Dev. 17:2003;1392-1401.
    • (2003) Genes Dev. , vol.17 , pp. 1392-1401
    • Corey, L.L.1    Weirich, C.S.2    Benjamin, I.J.3    Kingston, R.E.4
  • 107
    • 0032101064 scopus 로고    scopus 로고
    • Transcriptional activation domains stimulate initiation and elongation at different times and via different residues
    • Brown S.A., Weirich C.S., Newton E.M., Kingston R.E. Transcriptional activation domains stimulate initiation and elongation at different times and via different residues. EMBO J. 17:1998;3146-3154.
    • (1998) EMBO J. , vol.17 , pp. 3146-3154
    • Brown, S.A.1    Weirich, C.S.2    Newton, E.M.3    Kingston, R.E.4
  • 108
    • 0033854297 scopus 로고    scopus 로고
    • Genetic interactions between TFIIS and the Swi-Snf chromatin-remodeling complex
    • Davie J.K., Kane C.M. Genetic interactions between TFIIS and the Swi-Snf chromatin-remodeling complex. Mol. Cell. Biol. 20:2000;5960-5973.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5960-5973
    • Davie, J.K.1    Kane, C.M.2
  • 109
    • 0027315423 scopus 로고
    • Poly(A) signals and transcriptional pause sites combine to prevent interference between RNA polymerase II promoters
    • Eggermont J., Proudfoot N.J. Poly(A) signals and transcriptional pause sites combine to prevent interference between RNA polymerase II promoters. EMBO J. 12:1993;2539-2548.
    • (1993) EMBO J. , vol.12 , pp. 2539-2548
    • Eggermont, J.1    Proudfoot, N.J.2
  • 110
    • 0032541403 scopus 로고    scopus 로고
    • Poly(A) signals control both transcriptional termination and initiation between the tandem GAL10 and GAL7 genes of Saccharomyces cerevisiae
    • Greger I.H., Proudfoot N.J. Poly(A) signals control both transcriptional termination and initiation between the tandem GAL10 and GAL7 genes of Saccharomyces cerevisiae. EMBO J. 17:1998;4771-4779.
    • (1998) EMBO J. , vol.17 , pp. 4771-4779
    • Greger, I.H.1    Proudfoot, N.J.2
  • 111
    • 0030798246 scopus 로고    scopus 로고
    • Transcription factor TFIID recruits factor CPSF for formation of 3′ end of mRNA
    • Dantonel J.C., Murthy K.G., Manley J.L., Tora L. Transcription factor TFIID recruits factor CPSF for formation of 3′ end of mRNA. Nature. 389:1997;399-402.
    • (1997) Nature , vol.389 , pp. 399-402
    • Dantonel, J.C.1    Murthy, K.G.2    Manley, J.L.3    Tora, L.4
  • 112
    • 0036928142 scopus 로고    scopus 로고
    • A role for chromatin remodeling in transcriptional termination by RNA polymerase II
    • Alen C., Kent N.A., Jones H.S., O'Sullivan J., Aranda A., Proudfoot N.J. A role for chromatin remodeling in transcriptional termination by RNA polymerase II. Mol. Cell. 10:2002;1441-1452.
    • (2002) Mol. Cell , vol.10 , pp. 1441-1452
    • Alen, C.1    Kent, N.A.2    Jones, H.S.3    O'Sullivan, J.4    Aranda, A.5    Proudfoot, N.J.6
  • 113
    • 0027905034 scopus 로고
    • Molecular mechanism of transcription-repair coupling
    • Selby C.P., Sancar A. Molecular mechanism of transcription-repair coupling. Science. 260:1993;53-58.
    • (1993) Science , vol.260 , pp. 53-58
    • Selby, C.P.1    Sancar, A.2
  • 114
    • 0037073063 scopus 로고    scopus 로고
    • Rho-dependent termination and ATPases in transcript termination
    • Richardson J.P. Rho-dependent termination and ATPases in transcript termination. Biochim. Biophys. Acta. 1577:2002;251-260.
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 251-260
    • Richardson, J.P.1
  • 115
    • 0031438709 scopus 로고    scopus 로고
    • Drosophila factor 2, an RNA polymerase II transcript release factor, has DNA-dependent ATPase activity
    • Xie Z., Price D. Drosophila factor 2, an RNA polymerase II transcript release factor, has DNA-dependent ATPase activity. J. Biol. Chem. 272:1997;31902-31907.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31902-31907
    • Xie, Z.1    Price, D.2


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