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Volumn 1677, Issue 1-3, 2004, Pages 79-86

Transcriptional elongation control by RNA polymerase II: A new frontier

Author keywords

Control; RNA polymerase II; Transcriptional elongation

Indexed keywords

HISTONE; MESSENGER RNA; METHYLTRANSFERASE; RNA POLYMERASE II; TRANSCRIPTION ELONGATION FACTOR;

EID: 1542328270     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbaexp.2003.11.013     Document Type: Review
Times cited : (50)

References (80)
  • 2
    • 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
  • 3
    • 0031763366 scopus 로고    scopus 로고
    • Factors regulating the transcriptional elongation activity of RNA polymerase II
    • Shilatifard A. Factors regulating the transcriptional elongation activity of RNA polymerase II. FASEB J. 12:1998;1437-1446.
    • (1998) FASEB J. , vol.12 , pp. 1437-1446
    • Shilatifard, A.1
  • 5
    • 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
  • 6
    • 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 Z., 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, Z.3    Price, D.H.4
  • 7
    • 0032031706 scopus 로고    scopus 로고
    • Identification of multiple cyclin subunits of human P-TEFb
    • Peng J., Zhu Y., Milto J.T., Price D.H. Identification of multiple cyclin subunits of human P-TEFb. Genes Dev. 12:1998;755-762.
    • (1998) Genes Dev. , vol.12 , pp. 755-762
    • Peng, J.1    Zhu, Y.2    Milto, J.T.3    Price, D.H.4
  • 8
    • 0027447687 scopus 로고
    • Elongation factor SII-dependent transcription by RNA polymerase II through a sequence-specific DNA-binding protein
    • Reines D., Mote J. Jr. Elongation factor SII-dependent transcription by RNA polymerase II through a sequence-specific DNA-binding protein. Proc. Natl. Acad. Sci. U. S. A. 90:1993;1917-1921.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1917-1921
    • Reines, D.1    Mote, J.Jr.2
  • 9
    • 0029930503 scopus 로고    scopus 로고
    • Spermatocyte-specific expression of the gene for mouse testis-specific transcription elongation factor S-II
    • Ito T., Xu Q., Takeuchi H., Kubo T., Natori S. Spermatocyte-specific expression of the gene for mouse testis-specific transcription elongation factor S-II. FEBS Lett. 385:1996;21-24.
    • (1996) FEBS Lett. , vol.385 , pp. 21-24
    • Ito, T.1    Xu, Q.2    Takeuchi, H.3    Kubo, T.4    Natori, S.5
  • 10
    • 0027739408 scopus 로고
    • Transcription elongation by RNA polymerase II: Mechanism of SII activation
    • Reines D., Ghanouni P., Gu W., Mote J. Jr., Powell W. Transcription elongation by RNA polymerase II: mechanism of SII activation. Cell. Mol. Biol. Res. 39:1993;331-338.
    • (1993) Cell. Mol. Biol. Res. , vol.39 , pp. 331-338
    • Reines, D.1    Ghanouni, P.2    Gu, W.3    Mote, J.Jr.4    Powell, W.5
  • 11
    • 0028230037 scopus 로고
    • A DNA minor groove-binding ligand both potentiates and arrests transcription by RNA polymerase II. Elongation factor SII enables readthrough at arrest sites
    • Mote J. Jr., Ghanouni P., Reines D. A DNA minor groove-binding ligand both potentiates and arrests transcription by RNA polymerase II. Elongation factor SII enables readthrough at arrest sites. J. Mol. Biol. 236:1994;725-737.
    • (1994) J. Mol. Biol. , vol.236 , pp. 725-737
    • Mote, J.Jr.1    Ghanouni, P.2    Reines, D.3
  • 12
    • 0034111019 scopus 로고    scopus 로고
    • P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II
    • Price D.H. P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol. Cell. Biol. 8:2000;2629-2634.
    • (2000) Mol. Cell. Biol. , vol.8 , pp. 2629-2634
    • Price, D.H.1
  • 13
    • 0028837312 scopus 로고
    • The human dystrophin gene requires 16 hours to be transcribed and is cotranscriptionally spliced
    • Tennyson C.N., Klamut H.J., Worton R.G. The human dystrophin gene requires 16 hours to be transcribed and is cotranscriptionally spliced. Nat. Genet. 9:1995;184-190.
    • (1995) Nat. Genet. , vol.9 , pp. 184-190
    • Tennyson, C.N.1    Klamut, H.J.2    Worton, R.G.3
  • 14
    • 0021268344 scopus 로고
    • Early events in the stimulation of mammary tumor virus RNA synthesis by glucocorticoids, novel assays of transcription rates
    • Ucker D.S., Yamamoto K.R. Early events in the stimulation of mammary tumor virus RNA synthesis by glucocorticoids, novel assays of transcription rates. J. Biol. Chem. 259:1984;7416-7420.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7416-7420
    • Ucker, D.S.1    Yamamoto, K.R.2
  • 15
    • 0025232290 scopus 로고
    • Spatial and temporal patterns of E74 transcription during Drosophila development
    • Thummel C.S., Burtis K.C., Hogness D.D. Spatial and temporal patterns of E74 transcription during Drosophila development. Cell. 61:1990;101-111.
    • (1990) Cell , vol.61 , pp. 101-111
    • Thummel, C.S.1    Burtis, K.C.2    Hogness, D.D.3
  • 16
    • 0024504832 scopus 로고
    • Dynamic interaction between a Drosophila transcription factor and RNA polymerase II
    • Price D.H., Sluder A.E., Greenleaf A.L. Dynamic interaction between a Drosophila transcription factor and RNA polymerase II. Mol. Cell. Biol. 9:1989;1465-1475.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1465-1475
    • Price, D.H.1    Sluder, A.E.2    Greenleaf, A.L.3
  • 17
    • 0029055758 scopus 로고
    • Identification of a decay in transcription potential that results in elongation factor dependence of Pol II
    • Gu W., Reines D. Identification of a decay in transcription potential that results in elongation factor dependence of Pol II. J. Biol. Chem. 270:1995;11238-11244.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11238-11244
    • Gu, W.1    Reines, D.2
  • 18
    • 0027378324 scopus 로고
    • RNA polymerase II transcription factor SIII. I. Identification, purification, and properties
    • Bradsher J.N., Jackson K.W., Conaway R.C., Conaway J.W. RNA polymerase II transcription factor SIII. I. Identification, purification, and properties. J. Biol. Chem. 268:1993;25587-25593.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25587-25593
    • Bradsher, J.N.1    Jackson, K.W.2    Conaway, R.C.3    Conaway, J.W.4
  • 21
    • 0034010131 scopus 로고    scopus 로고
    • Identification and characterization of Elongin A2, a new member of the Elongin family of transcription elongation factors, specifically expressed in the testis
    • Aso T., Yamazaki K., Amimoto K., Kuroiwa A., Higashi H., Matsuda Y., Kitajima S., Hatakeyama M. Identification and characterization of Elongin A2, a new member of the Elongin family of transcription elongation factors, specifically expressed in the testis. J. Biol. Chem. 275:2000;6546-6552.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6546-6552
    • Aso, T.1    Yamazaki, K.2    Amimoto, K.3    Kuroiwa, A.4    Higashi, H.5    Matsuda, Y.6    Kitajima, S.7    Hatakeyama, M.8
  • 22
    • 0037135594 scopus 로고    scopus 로고
    • Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3
    • Yamazaki K., Guo L., Sugahara K., Zhang C., Enzan H., Nakabeppu Y., Kitajima S., Aso T. Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3. J. Biol. Chem. 277:2002;26444- 26451.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26444-26451
    • Yamazaki, K.1    Guo, L.2    Sugahara, K.3    Zhang, C.4    Enzan, H.5    Nakabeppu, Y.6    Kitajima, S.7    Aso, T.8
  • 24
    • 0032004953 scopus 로고    scopus 로고
    • Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae
    • Hartzog G.A., Wada T., Handa H., Winston F. Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev. 12:1998;357-369.
    • (1998) Genes Dev. , vol.12 , pp. 357-369
    • Hartzog, G.A.1    Wada, T.2    Handa, H.3    Winston, F.4
  • 25
    • 0034667949 scopus 로고    scopus 로고
    • High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: Roles in promoter proximal pausing and transcription elongation
    • Andrulis E.D., Guzman E., Doring P., Werner J., Lis J.T. High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: roles in promoter proximal pausing and transcription elongation. Genes Dev. 14:2000;2635-2649.
    • (2000) Genes Dev. , vol.14 , pp. 2635-2649
    • Andrulis, E.D.1    Guzman, E.2    Doring, P.3    Werner, J.4    Lis, J.T.5
  • 26
    • 0034667805 scopus 로고    scopus 로고
    • Spt5 and spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster
    • Kaplan C.D., Morris J.R., Wu C., Winston F. Spt5 and spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster. Genes Dev. 14:2000;2623-2634.
    • (2000) Genes Dev. , vol.14 , pp. 2623-2634
    • Kaplan, C.D.1    Morris, J.R.2    Wu, C.3    Winston, F.4
  • 27
    • 0030822591 scopus 로고    scopus 로고
    • Cockayne syndrome group B protein enhances elongation by RNA polymerase II
    • Selby C.P., Sancar A. Cockayne syndrome group B protein enhances elongation by RNA polymerase II. Proc. Natl. Acad. Sci. U. S. A. 94:1997;11205-11209.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11205-11209
    • Selby, C.P.1    Sancar, A.2
  • 30
    • 0034644734 scopus 로고    scopus 로고
    • Identification, cloning, expression, and biochemical characterization of the testis-specific RNA polymerase II elongation factor ELL3
    • Miller T., Williams K., Johnstone R.W., Shilatifard A. Identification, cloning, expression, and biochemical characterization of the testis-specific RNA polymerase II elongation factor ELL3. J. Biol. Chem. 275:2000;32052-32056.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32052-32056
    • Miller, T.1    Williams, K.2    Johnstone, R.W.3    Shilatifard, A.4
  • 31
    • 0035503319 scopus 로고    scopus 로고
    • Drosophila ELL is associated with actively elongating RNA polymerase II on transcriptionally active sites in vivo
    • Gerber M., Ma J., Dean K., Eissenberg J.C., Shilatifard A. Drosophila ELL is associated with actively elongating RNA polymerase II on transcriptionally active sites in vivo. EMBO J. 20:2001;6104-6114.
    • (2001) EMBO J. , vol.20 , pp. 6104-6114
    • Gerber, M.1    Ma, J.2    Dean, K.3    Eissenberg, J.C.4    Shilatifard, A.5
  • 33
    • 0030802398 scopus 로고    scopus 로고
    • Identification of RTF1, a novel gene important for TATA site selection by TATA box-binding protein in Saccharomyces cerevisiae
    • Stolinski L.A., Eisenmann D.M., Arndt K.M. Identification of RTF1, a novel gene important for TATA site selection by TATA box-binding protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 17:1997;4490-4500.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4490-4500
    • Stolinski, L.A.1    Eisenmann, D.M.2    Arndt, K.M.3
  • 34
    • 0033790999 scopus 로고    scopus 로고
    • Synthetic lethal interactions suggest a role for the Saccharomyces cerevisiae Rtf1 protein in transcription elongation
    • Costa P.J., Arndt K.M. Synthetic lethal interactions suggest a role for the Saccharomyces cerevisiae Rtf1 protein in transcription elongation. Genetics. 156:2000;535-547.
    • (2000) Genetics , vol.156 , pp. 535-547
    • Costa, P.J.1    Arndt, K.M.2
  • 35
    • 0036123253 scopus 로고    scopus 로고
    • Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex
    • Mueller C.L., Jaehning J.A. Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex. Mol. Cell. Biol. 22:2002;1971-1980.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1971-1980
    • Mueller, C.L.1    Jaehning, J.A.2
  • 36
    • 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
  • 39
    • 0038374526 scopus 로고    scopus 로고
    • Transcriptional elongation control and histone methylation
    • Gerber M.A., 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.A.1    Shilatifard, A.2
  • 40
    • 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
  • 41
    • 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
  • 42
    • 0025739871 scopus 로고
    • RNA polymerase II
    • Young R.A. RNA polymerase II. Annu. Rev. Biochem. 60:1991;689-715.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 689-715
    • Young, R.A.1
  • 43
    • 0023651270 scopus 로고
    • Functional redundancy and structural polymorphism in the large subunit of RNA polymerase II
    • Nonet M., Sweetser D., Young R.A. Functional redundancy and structural polymorphism in the large subunit of RNA polymerase II. Cell. 50:1987;909-915.
    • (1987) Cell , vol.50 , pp. 909-915
    • Nonet, M.1    Sweetser, D.2    Young, R.A.3
  • 44
    • 0023737652 scopus 로고
    • Genetic analysis of the repetitive carboxyl-terminal domain of the largest subunit of mouse RNA polymerase II
    • Bartolomei M.S., Halden N.F., Cullen C.R., Corden J.L. Genetic analysis of the repetitive carboxyl-terminal domain of the largest subunit of mouse RNA polymerase II. Mol. Cell. Biol. 8:1988;330-339.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 330-339
    • Bartolomei, M.S.1    Halden, N.F.2    Cullen, C.R.3    Corden, J.L.4
  • 45
    • 0034307008 scopus 로고    scopus 로고
    • Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription
    • Komarnitsky P., Cho E.J., Buratowski S. Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription. Genes Dev. 14:2000;452-460.
    • (2000) Genes Dev. , vol.14 , pp. 452-460
    • Komarnitsky, P.1    Cho, E.J.2    Buratowski, S.3
  • 46
    • 0017851222 scopus 로고
    • DRB-induced premature termination of late adenovirus transcription
    • Fraser N.W., Sehgal P.B., Darnell J.E. DRB-induced premature termination of late adenovirus transcription. Nature. 272:1978;590-593.
    • (1978) Nature , vol.272 , pp. 590-593
    • Fraser, N.W.1    Sehgal, P.B.2    Darnell, J.E.3
  • 47
    • 0023000520 scopus 로고
    • Casein kinase type II is involved in the inhibition by 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole of specific RNA polymerase II transcription
    • Zandomeni R., Zandomeni M.C., Shugar D., Weinmann R. Casein kinase type II is involved in the inhibition by 5,6-dichloro-1-beta-D- ribofuranosylbenzimidazole of specific RNA polymerase II transcription. J. Biol. Chem. 261:1986;3414-3419.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3414-3419
    • Zandomeni, R.1    Zandomeni, M.C.2    Shugar, D.3    Weinmann, R.4
  • 48
    • 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
  • 49
    • 0026725368 scopus 로고
    • Control of formation of two distinct classes of RNA polymerase II elongation complexes
    • Marshall N.F., Price D.H. Control of formation of two distinct classes of RNA polymerase II elongation complexes. Mol. Cell. Biol. 12:1992;2078-2090.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2078-2090
    • Marshall, N.F.1    Price, D.H.2
  • 50
    • 0037102566 scopus 로고    scopus 로고
    • CDK-9/cyclin T (P-TEFb) is required in two postinitiation pathways for transcription in the C. elegans embryo
    • Shim E.Y., Walker A.K., Shi Y., Blackwell T.K. CDK-9/cyclin T (P-TEFb) is required in two postinitiation pathways for transcription in the C. elegans embryo. Genes Dev. 16:2002;2135-2146.
    • (2002) Genes Dev. , vol.16 , pp. 2135-2146
    • Shim, E.Y.1    Walker, A.K.2    Shi, Y.3    Blackwell, T.K.4
  • 51
    • 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
  • 52
    • 0342748478 scopus 로고    scopus 로고
    • Domains in the SPT5 protein that modulate its transcriptional regulatory properties
    • Ivanov D., Kwak Y.T., Guo J., Gaynor R.B. Domains in the SPT5 protein that modulate its transcriptional regulatory properties. Mol. Cell. Biol. 20:2000;2970-2983.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2970-2983
    • Ivanov, D.1    Kwak, Y.T.2    Guo, J.3    Gaynor, R.B.4
  • 53
    • 0034175631 scopus 로고    scopus 로고
    • P-TEFb kinase recruitment and function at heat shock loci
    • Lis J.T., Mason P., Peng J., Price D.H., Werner J. P-TEFb kinase recruitment and function at heat shock loci. Genes Dev. 14:2000;792-803.
    • (2000) Genes Dev. , vol.14 , pp. 792-803
    • Lis, J.T.1    Mason, P.2    Peng, J.3    Price, D.H.4    Werner, J.5
  • 54
    • 0016221697 scopus 로고
    • Chromatin structure: A repeating unit of histones and DNA
    • Kornberg R.D. Chromatin structure: a repeating unit of histones and DNA. Science. 184:1974;868-871.
    • (1974) Science , vol.184 , pp. 868-871
    • Kornberg, R.D.1
  • 55
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 a resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature. 389:1997;251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 56
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • Arents G., Moudrianakis E.N. The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proc. Natl. Acad. Sci. U. S. A. 92:1995;11170-11174.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.N.2
  • 57
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman J.L., Kingston R.E. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Ann. Rev. Biochem. 67:1998;545-579.
    • (1998) Ann. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 58
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science. 293:2001;1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 59
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner B.M. Cellular memory and the histone code. Cell. 111:2002;285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 63
    • 0037126594 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4
    • Roguev A., Schaft D., Shevchenko A., Pijnappel W.W., Wilm M., Aasland R., Stewart A.F. The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4. EMBO J. 20:2001;7137-7148.
    • (2001) EMBO J. , vol.20 , pp. 7137-7148
    • Roguev, A.1    Schaft, D.2    Shevchenko, A.3    Pijnappel, W.W.4    Wilm, M.5    Aasland, R.6    Stewart, A.F.7
  • 64
    • 0037039309 scopus 로고    scopus 로고
    • A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3
    • Nagy P.L., Griesenbeck J., Kornberg R.D., Cleary M.L. A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3. Proc. Natl. Acad. Sci. U. S. A. 99:2002;90-94.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 90-94
    • Nagy, P.L.1    Griesenbeck, J.2    Kornberg, R.D.3    Cleary, M.L.4
  • 66
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun Z.W., Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature. 418:2002;104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 69
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F., Gafken P.R., Gottschling D.E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell. 109:2002;745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 70
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev. 16:2002;1518-1527.
    • (2002) Genes Dev. , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 71
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • Ng H.H., Xu R.M., Zhang Y., Struhl K. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. J. Biol. Chem. 277:2002;34655-34657.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 72
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides T. Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12:2002;198-209.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 74
    • 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
  • 75
    • 0037147121 scopus 로고    scopus 로고
    • Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation
    • Li J., Moazed D., Gygi S.P. Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation. J. Biol. Chem. 277:2002;49383-49388.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49383-49388
    • Li, J.1    Moazed, D.2    Gygi, S.P.3
  • 76
    • 0037512273 scopus 로고    scopus 로고
    • The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain fo RNA polymerase II
    • Li B., Howe L., Anderson S., Yates J.R., Workman J.L. The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain fo RNA polymerase II. J. Biol. Chem. 278:2003;8897-8903.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8897-8903
    • Li, B.1    Howe, L.2    Anderson, S.3    Yates, J.R.4    Workman, J.L.5
  • 79
    • 0034548830 scopus 로고    scopus 로고
    • A carboxy-terminal domain of ELL is required and sufficient for immortalization of myeloid progenitors by MLL-ELL
    • DiMartino J.F., Miller T., Ayton P.M., Landewe T., Hess J.L., Cleary M.L., Shilatifard A. A carboxy-terminal domain of ELL is required and sufficient for immortalization of myeloid progenitors by MLL-ELL. Blood. 96:2000;3887-3893.
    • (2000) Blood , vol.96 , pp. 3887-3893
    • Dimartino, J.F.1    Miller, T.2    Ayton, P.M.3    Landewe, T.4    Hess, J.L.5    Cleary, M.L.6    Shilatifard, A.7
  • 80
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.