메뉴 건너뛰기




Volumn 81, Issue 1-2, 1999, Pages 27-38

Transcription factor IIH: A key player in the cellular response to DNA damage

Author keywords

Apoptosis; Cell cycle; DNA repair; TFIIH; Transcription

Indexed keywords

TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR IIH; UNCLASSIFIED DRUG;

EID: 0032693601     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(99)80035-2     Document Type: Article
Times cited : (55)

References (154)
  • 1
    • 0029846871 scopus 로고    scopus 로고
    • The general transcription factors of RNA polymerase II
    • Orphanides G., Lagrange T., Reinberg D. The general transcription factors of RNA polymerase II. Genes Dev. 10:1996;2657-2683.
    • (1996) Genes Dev , vol.10 , pp. 2657-2683
    • Orphanides, G.1    Lagrange, T.2    Reinberg, D.3
  • 2
    • 0000402041 scopus 로고
    • An RNA polymerase II transcription factor has an associated DNA-dependent ATPase (dATPase) activity strongly stimulated by the TATA region of promoters
    • Conaway R.C., Conaway J.W. An RNA polymerase II transcription factor has an associated DNA-dependent ATPase (dATPase) activity strongly stimulated by the TATA region of promoters. Proc. Natl. Acad. Sci. USA. 86:1989;7356-7360.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7356-7360
    • Conaway, R.C.1    Conaway, J.W.2
  • 3
    • 0026052701 scopus 로고
    • Purification and characterization of yeast RNA polymerase II transcription factor b
    • Feaver W.J., Gileadi O., Kornberg R.D. Purification and characterization of yeast RNA polymerase II transcription factor b. J. Biol. Chem. 266:1991;19000-19005.
    • (1991) J. Biol. Chem , vol.266 , pp. 19000-19005
    • Feaver, W.J.1    Gileadi, O.2    Kornberg, R.D.3
  • 4
    • 0025787782 scopus 로고
    • Purification and interaction properties of the human RNA polymerase B (II) general transcription factor BTF2
    • Gérard M., Fischer L., Moncollin V., Chipoulet J.M., Chambon P., Egly J.-M. Purification and interaction properties of the human RNA polymerase B (II) general transcription factor BTF2. J. Biol. Chem. 266:1991;20940-20945.
    • (1991) J. Biol. Chem , vol.266 , pp. 20940-20945
    • Gérard, M.1    Fischer, L.2    Moncollin, V.3    Chipoulet, J.M.4    Chambon, P.5    Egly, J.-M.6
  • 5
    • 0026802039 scopus 로고
    • Factors involved in specific transcription by mammalian RNA polymerase II. Identification and characterization of factor IIH
    • Flores O., Lu H., Reinberg D. Factors involved in specific transcription by mammalian RNA polymerase II. Identification and characterization of factor IIH. J. Biol. Chem. 267:1992;2786-2793.
    • (1992) J. Biol. Chem , vol.267 , pp. 2786-2793
    • Flores, O.1    Lu, H.2    Reinberg, D.3
  • 6
    • 0029987031 scopus 로고    scopus 로고
    • Cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH
    • Adamczewski J.P., Rossignol M., Tassan J.P., Nigg E.A., Moncollin V., Egly J.-M., Mat1. Cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH. EMBO J. 15:1996;1877-1884.
    • (1996) EMBO J , vol.15 , pp. 1877-1884
    • Adamczewski, J.P.1    Rossignol, M.2    Tassan, J.P.3    Nigg, E.A.4    Moncollin, V.5    Egly, J.-M.6    Mat I7
  • 7
  • 8
    • 0029982779 scopus 로고    scopus 로고
    • Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH
    • Reardon J.T., Ge H., Gibbs E., Sancar A., Hurwitz J., Pan Z.Q. Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH. Proc. Natl. Acad. Sci. USA. 93:1996;6482-6487.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6482-6487
    • Reardon, J.T.1    Ge, H.2    Gibbs, E.3    Sancar, A.4    Hurwitz, J.5    Pan, Z.Q.6
  • 9
    • 0030998712 scopus 로고    scopus 로고
    • Substrate specificity of the Cdk-activating kinase (CAK) is altered upon association with TFIIH
    • Rossignol M., Kolb-Cheynel I., Egly J.-M. Substrate specificity of the Cdk-activating kinase (CAK) is altered upon association with TFIIH. EMBO J. 16:1997;1628-1637.
    • (1997) EMBO J , vol.16 , pp. 1628-1637
    • Rossignol, M.1    Kolb-Cheynel, I.2    Egly, J.-M.3
  • 10
    • 0030749609 scopus 로고    scopus 로고
    • Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair factor IIH. Homology to human cyclin-dependent kinase activating kinase and IIH subunits
    • Feaver W.J., Henry N.L., Wang Z., Wu X., Svejstrup J.Q., Bushnell D.A., Friedberg E.C., Kornberg R.D. Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair factor IIH. Homology to human cyclin-dependent kinase activating kinase and IIH subunits. J. Biol. Chem. 272:1997;19319-19327.
    • (1997) J. Biol. Chem , vol.272 , pp. 19319-19327
    • Feaver, W.J.1    Henry, N.L.2    Wang, Z.3    Wu, X.4    Svejstrup, J.Q.5    Bushnell, D.A.6    Friedberg, E.C.7    Kornberg, R.D.8
  • 11
    • 0028590113 scopus 로고
    • Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK
    • Feaver W.J., Svejstrup J.Q., Henry N.L., Kornberg R.D. Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. Cell. 79:1994;1103-1109.
    • (1994) Cell , vol.79 , pp. 1103-1109
    • Feaver, W.J.1    Svejstrup, J.Q.2    Henry, N.L.3    Kornberg, R.D.4
  • 12
    • 0028030069 scopus 로고
    • RNA polymerase transcription factor IIH holoenzyme from yeast
    • Svejstrup J.Q., Feaver W.J., Lapointe J., Kornberg R.D. RNA polymerase transcription factor IIH holoenzyme from yeast. J. Biol. Chem. 269:1994;28044-28048.
    • (1994) J. Biol. Chem , vol.269 , pp. 28044-28048
    • Svejstrup, J.Q.1    Feaver, W.J.2    Lapointe, J.3    Kornberg, R.D.4
  • 14
    • 0025158110 scopus 로고
    • A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders xeroderma pigmentosum and Cockayne's syndrome
    • Weeda G., van Ham R.C., Vermeulen W., Bootsma D., van der Eb A.J., Hoeijmakers J.H. A presumed DNA helicase encoded by ERCC-3 is involved in the human repair disorders xeroderma pigmentosum and Cockayne's syndrome. Cell. 62:1990;777-791.
    • (1990) Cell , vol.62 , pp. 777-791
    • Weeda, G.1    Van Ham, R.C.2    Vermeulen, W.3    Bootsma, D.4    Van Der Eb, A.J.5    Hoeijmakers, J.H.6
  • 17
    • 0025250069 scopus 로고
    • ERCC2: CDNA cloning and molecular characterization of a human nucleotide excision repair gene with high homology to yeast RAD3
    • Weber C.A., Salazar E.P., Stewart S.A., Thompson L.H. ERCC2: cDNA cloning and molecular characterization of a human nucleotide excision repair gene with high homology to yeast RAD3. EMBO J. 9:1990;1437-1447.
    • (1990) EMBO J , vol.9 , pp. 1437-1447
    • Weber, C.A.1    Salazar, E.P.2    Stewart, S.A.3    Thompson, L.H.4
  • 20
    • 0027994603 scopus 로고
    • A novel cyclin associates with MO15/Cdk7 to form the Cdk-activating kinase
    • Fisher R.P., Morgan D.O. A novel cyclin associates with MO15/Cdk7 to form the Cdk-activating kinase. Cell. 78:1994;713-724.
    • (1994) Cell , vol.78 , pp. 713-724
    • Fisher, R.P.1    Morgan, D.O.2
  • 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
  • 28
    • 0028123692 scopus 로고
    • Transcription initiation by RNA polymerase II does not require hydrolysis of the beta-gamma phosphoanhydride bond of ATP
    • Timmers H.T. Transcription initiation by RNA polymerase II does not require hydrolysis of the beta-gamma phosphoanhydride bond of ATP. EMBO J. 13:1994;391-399.
    • (1994) EMBO J , vol.13 , pp. 391-399
    • Timmers, H.T.1
  • 29
    • 0028964168 scopus 로고
    • The requirement for the basal transcription factor IIE is determined by the helical stability of promoter DNA
    • Holstege F.C., Tantin D., Carey M., Van DerVliet P.C., Timmers H.T. The requirement for the basal transcription factor IIE is determined by the helical stability of promoter DNA. EMBO J. 14:1995;810-819.
    • (1995) EMBO J , vol.14 , pp. 810-819
    • Holstege, F.C.1    Tantin, D.2    Carey, M.3    Van Dervliet, P.C.4    Timmers, H.T.5
  • 30
    • 0028104678 scopus 로고
    • Initiation of transcription by RNA polymerase II is limited by melting of the promoter DNA in the region immediately upstream of the initiation site
    • Pan G., Greenblatt J. Initiation of transcription by RNA polymerase II is limited by melting of the promoter DNA in the region immediately upstream of the initiation site. J. Biol. Chem. 269:1994;30101-30104.
    • (1994) J. Biol. Chem , vol.269 , pp. 30101-30104
    • Pan, G.1    Greenblatt, J.2
  • 31
    • 0028340172 scopus 로고
    • A heteroduplex template circumvents the energetic requirement for ATP during activated transcription by RNA polymerase II
    • Tantin D., Carey M. A heteroduplex template circumvents the energetic requirement for ATP during activated transcription by RNA polymerase II. J. Biol. Chem. 269:1994;17397-17400.
    • (1994) J. Biol. Chem , vol.269 , pp. 17397-17400
    • Tantin, D.1    Carey, M.2
  • 32
    • 0030007387 scopus 로고    scopus 로고
    • Opening of an RNA polymerase II promoter occurs in two distinct steps and requires the basal transcription factors IIE and IIH
    • Holstege F.C., van der Vliet P.C., Timmers H.T. Opening of an RNA polymerase II promoter occurs in two distinct steps and requires the basal transcription factors IIE and IIH. EMBO J. 15:1996;1666-1677.
    • (1996) EMBO J , vol.15 , pp. 1666-1677
    • Holstege, F.C.1    Van Der Vliet, P.C.2    Timmers, H.T.3
  • 33
    • 0031463993 scopus 로고    scopus 로고
    • Three transitions in the RNA polymerase II transcription complex during initiation
    • Holstege F.C., Fiedler U., Timmers H.T. Three transitions in the RNA polymerase II transcription complex during initiation. EMBO J. 16:1997;7468-7480.
    • (1997) EMBO J , vol.16 , pp. 7468-7480
    • Holstege, F.C.1    Fiedler, U.2    Timmers, H.T.3
  • 34
    • 0031434959 scopus 로고    scopus 로고
    • Multiple ATP-dependent steps in RNA polymerase II promoter melting and initiation
    • Yan M., Gralla J.D. Multiple ATP-dependent steps in RNA polymerase II promoter melting and initiation. EMBO J. 16:1997;7457-7467.
    • (1997) EMBO J , vol.16 , pp. 7457-7467
    • Yan, M.1    Gralla, J.D.2
  • 35
    • 0028352861 scopus 로고
    • Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II
    • Goodrich J.A., Tjian R. Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II. Cell. 77:1994;145-156.
    • (1994) Cell , vol.77 , pp. 145-156
    • Goodrich, J.A.1    Tjian, R.2
  • 36
    • 0029812863 scopus 로고    scopus 로고
    • Promoter escape by RNA polymerase II. A role for an ATP cofactor in suppression of arrest by polymerase at promoter-proximal sites
    • Dvir A., Conaway R.C., Conaway J.W. Promoter escape by RNA polymerase II. A role for an ATP cofactor in suppression of arrest by polymerase at promoter-proximal sites. J. Biol. Chem. 271:1996;23352-23356.
    • (1996) J. Biol. Chem , vol.271 , pp. 23352-23356
    • Dvir, A.1    Conaway, R.C.2    Conaway, J.W.3
  • 37
    • 0030740233 scopus 로고    scopus 로고
    • A role for TFIIH in controlling the activity of early RNA polymerase II elongation complexes
    • Dvir A., Conaway R.C., Conaway J.W. A role for TFIIH in controlling the activity of early RNA polymerase II elongation complexes. Proc. Natl. Acad. Sci. USA. 94:1997;9006-9010.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9006-9010
    • Dvir, A.1    Conaway, R.C.2    Conaway, J.W.3
  • 39
    • 0028232284 scopus 로고
    • RAD25 is a DNA helicase required for DNA repair and RNA polymerase II transcription
    • Guzder S.N., Sung P., Bailly V., Prakash L., Prakash S. RAD25 is a DNA helicase required for DNA repair and RNA polymerase II transcription. Nature. 369:1994;578-581.
    • (1994) Nature , vol.369 , pp. 578-581
    • Guzder, S.N.1    Sung, P.2    Bailly, V.3    Prakash, L.4    Prakash, S.5
  • 41
    • 0029095126 scopus 로고
    • Requirement for TFIIH kinase activity in transcription by RNA polymerase II
    • Akoulitchev S., Mäkelä T.P., Weinberg R.A., Reinberg D. Requirement for TFIIH kinase activity in transcription by RNA polymerase II. Nature. 377:1995;557-560.
    • (1995) Nature , vol.377 , pp. 557-560
    • Akoulitchev, S.1    Mäkelä, T.P.2    Weinberg, R.A.3    Reinberg, D.4
  • 42
    • 0029008667 scopus 로고
    • The KIN28 gene is required both for RNA polymerase II mediated transcription and phosphorylation of the Rpb1p CTD
    • Valay J.G., Simon M., Dubois M.F., Bensaude O., Facca C., Faye G. The KIN28 gene is required both for RNA polymerase II mediated transcription and phosphorylation of the Rpb1p CTD. J. Mol. Biol. 249:1995;535-544.
    • (1995) J. Mol. Biol , vol.249 , pp. 535-544
    • Valay, J.G.1    Simon, M.2    Dubois, M.F.3    Bensaude, O.4    Facca, C.5    Faye, G.6
  • 43
    • 0029865796 scopus 로고    scopus 로고
    • A three-step pathway of transcription initiation leading to promoter clearance at an activation RNA polymerase II promoter
    • Jiang Y., Yan M., Gralla J.D. A three-step pathway of transcription initiation leading to promoter clearance at an activation RNA polymerase II promoter. Mol. Cell. Biol. 16:1996;1614-1621.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 1614-1621
    • Jiang, Y.1    Yan, M.2    Gralla, J.D.3
  • 44
    • 0028924422 scopus 로고
    • Phosphorylation of the C-terminal domain of RNA polymerase II
    • Dahmus M.E. Phosphorylation of the C-terminal domain of RNA polymerase II. Biochim. Biophys. Acta. 1261:1995;171-182.
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 171-182
    • Dahmus, M.E.1
  • 45
    • 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
  • 46
    • 0028900584 scopus 로고
    • Transcription-dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains
    • Bregman D.B., Du L., van der Zee S., Warren S.L. Transcription-dependent redistribution of the large subunit of RNA polymerase II to discrete nuclear domains. J. Cell Biol. 129:1995;287-298.
    • (1995) J. Cell Biol , vol.129 , pp. 287-298
    • Bregman, D.B.1    Du, L.2    Van Der Zee, S.3    Warren, S.L.4
  • 48
    • 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
  • 49
    • 0032540231 scopus 로고    scopus 로고
    • The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Ho C.K., Sriskanda V., McCracken S., Bentley D., Schwer B., Shuman S. The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 273:1998;9577-9585.
    • (1998) J. Biol. Chem , vol.273 , pp. 9577-9585
    • Ho, C.K.1    Sriskanda, V.2    McCracken, S.3    Bentley, D.4    Schwer, B.5    Shuman, S.6
  • 50
    • 0029959435 scopus 로고    scopus 로고
    • The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins
    • Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M., Corden J.L. The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins. Proc. Natl. Acad. Sci. USA. 93:1996;6975-6980.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6975-6980
    • Yuryev, A.1    Patturajan, M.2    Litingtung, Y.3    Joshi, R.V.4    Gentile, C.5    Gebara, M.6    Corden, J.L.7
  • 51
    • 0031032049 scopus 로고    scopus 로고
    • A functional interaction between the carboxy-terminal domain of RNA polymerase II and pre-mRNA splicing
    • Du L., Warren S.L. A functional interaction between the carboxy-terminal domain of RNA polymerase II and pre-mRNA splicing. J. Cell Biol. 136:1997;5-18.
    • (1997) J. Cell Biol , vol.136 , pp. 5-18
    • Du, L.1    Warren, S.L.2
  • 52
    • 0031022189 scopus 로고    scopus 로고
    • Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-mRNA
    • Kim E., Du L., Bregman D.B., Warren S.L. Splicing factors associate with hyperphosphorylated RNA polymerase II in the absence of pre-mRNA. J. Cell Biol. 136:1997;19-28.
    • (1997) J. Cell Biol , vol.136 , pp. 19-28
    • Kim, E.1    Du, L.2    Bregman, D.B.3    Warren, S.L.4
  • 55
    • 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
  • 56
    • 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
  • 57
    • 0029942906 scopus 로고    scopus 로고
    • TFIIH functions in regulating transcriptional elongation by RNA polymerase II in Xenopusoocytes
    • Yankulov K.Y., Pandes M., McCracken S., Bouchard D., Bentley D.L. TFIIH functions in regulating transcriptional elongation by RNA polymerase II in Xenopusoocytes. 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
  • 58
    • 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
  • 60
    • 0030768038 scopus 로고    scopus 로고
    • Nucleotide excision repair in mammalian cells
    • Wood R.D. Nucleotide excision repair in mammalian cells. J. Biol. Chem. 272:1997;23465-23468.
    • (1997) J. Biol. Chem , vol.272 , pp. 23465-23468
    • Wood, R.D.1
  • 63
    • 0028896837 scopus 로고
    • Reconstitution of human DNA repair excision nuclease in a highly defined system
    • Mu D., Park C.H., Matsunaga T., Hsu D.S., Reardon J.T., Sancar A. Reconstitution of human DNA repair excision nuclease in a highly defined system. J. Biol. Chem. 270:1995;2415-2418.
    • (1995) J. Biol. Chem , vol.270 , pp. 2415-2418
    • Mu, D.1    Park, C.H.2    Matsunaga, T.3    Hsu, D.S.4    Reardon, J.T.5    Sancar, A.6
  • 64
    • 0029019788 scopus 로고
    • Reconstitution of yeast nucleotide excision repair with purified Rad proteins, replication protein A, and transcription factor TFIIH
    • Guzder S.N., Habraken Y., Sung P., Prakash L., Prakash S. Reconstitution of yeast nucleotide excision repair with purified Rad proteins, replication protein A, and transcription factor TFIIH. J. Biol. Chem. 270:1995;12973-12976.
    • (1995) J. Biol. Chem , vol.270 , pp. 12973-12976
    • Guzder, S.N.1    Habraken, Y.2    Sung, P.3    Prakash, L.4    Prakash, S.5
  • 66
    • 0028349469 scopus 로고
    • Transcription factor b (TFIIH) is required during nucleotide-excision repair in yeast
    • Wang Z., Svejstrup J.Q., Feaver W.J., Wu X., Kornberg R.D., Friedberg E.C. Transcription factor b (TFIIH) is required during nucleotide-excision repair in yeast. Nature. 368:1994;74-76.
    • (1994) Nature , vol.368 , pp. 74-76
    • Wang, Z.1    Svejstrup, J.Q.2    Feaver, W.J.3    Wu, X.4    Kornberg, R.D.5    Friedberg, E.C.6
  • 67
    • 0028925910 scopus 로고
    • An interaction between the Tfb1 and Ssl1 subunits of yeast TFIIH correlates with DNA repair activity
    • Matsui P., Depaulo J., Buratowski S. An interaction between the Tfb1 and Ssl1 subunits of yeast TFIIH correlates with DNA repair activity. Nucleic Acids Res. 23:1995;767-772.
    • (1995) Nucleic Acids Res , vol.23 , pp. 767-772
    • Matsui, P.1    Depaulo, J.2    Buratowski, S.3
  • 68
    • 0028912931 scopus 로고
    • The yeast TFB1 and SSL1 genes, which encode subunits of transcription factor IIH, are required for nucleotide excision repair and RNA polymerase II transcription
    • Wang Z., Buratowski S., Svejstrup J.Q., Feaver W.J., Wu X., Kornberg R.D., Donahue T.F., Friedberg E.C. The yeast TFB1 and SSL1 genes, which encode subunits of transcription factor IIH, are required for nucleotide excision repair and RNA polymerase II transcription. Mol. Cell. Biol. 15:1995;2288-2293.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 2288-2293
    • Wang, Z.1    Buratowski, S.2    Svejstrup, J.Q.3    Feaver, W.J.4    Wu, X.5    Kornberg, R.D.6    Donahue, T.F.7    Friedberg, E.C.8
  • 69
    • 0027080295 scopus 로고
    • SSL1, a suppressor of a HIS4 5'-UTR stem-loop mutation, is essential for translation initiation and affects UV resistance in yeast
    • Yoon H., Miller S.P., Pabich E.K., Donahue T.F. SSL1, a suppressor of a HIS4 5'-UTR stem-loop mutation, is essential for translation initiation and affects UV resistance in yeast. Genes Dev. 6:1992;2463-2477.
    • (1992) Genes Dev , vol.6 , pp. 2463-2477
    • Yoon, H.1    Miller, S.P.2    Pabich, E.K.3    Donahue, T.F.4
  • 70
    • 0028180697 scopus 로고
    • P44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair
    • Humbert S., van Vuuren H., Lutz Y., Hoeijmakers J.H., Egly J.-M., Moncollin V. p44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair. EMBO J. 13:1994;2393-2398.
    • (1994) EMBO J , vol.13 , pp. 2393-2398
    • Humbert, S.1    Van Vuuren, H.2    Lutz, Y.3    Hoeijmakers, J.H.4    Egly, J.-M.5    Moncollin, V.6
  • 72
    • 0029870677 scopus 로고    scopus 로고
    • Reaction mechanism of human DNA repair excision nuclease
    • Mu D., Hsu D.S., Sancar A. Reaction mechanism of human DNA repair excision nuclease. J. Biol. Chem. 271:1996;8285-8294.
    • (1996) J. Biol. Chem , vol.271 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 73
    • 15844390308 scopus 로고    scopus 로고
    • Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair
    • Sung P., Guzder S.N., Prakash L., Prakash S. Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3 and Rad25, in the incision step of nucleotide excision repair. J. Biol. Chem. 271:1996;10821-10826.
    • (1996) J. Biol. Chem , vol.271 , pp. 10821-10826
    • Sung, P.1    Guzder, S.N.2    Prakash, L.3    Prakash, S.4
  • 74
    • 0030827256 scopus 로고    scopus 로고
    • Rig2, a RING finger protein that interacts with the Kin28/Ccl1 CTD kinase in yeast
    • Faye G., Simon M., Valay J.G., Fesquet D., Facca C. Rig2, a RING finger protein that interacts with the Kin28/Ccl1 CTD kinase in yeast. Mol. Gen. Genet. 255:1997;460-466.
    • (1997) Mol. Gen. Genet , vol.255 , pp. 460-466
    • Faye, G.1    Simon, M.2    Valay, J.G.3    Fesquet, D.4    Facca, C.5
  • 75
    • 0030010184 scopus 로고    scopus 로고
    • DNA repair deficiencies associated with mutations in genes encoding subunits of transcription initiation factor TFIIH in yeast
    • Sweder K.S., Chun R., Mori T., Hanawalt P.C. DNA repair deficiencies associated with mutations in genes encoding subunits of transcription initiation factor TFIIH in yeast. Nucleic Acids Res. 24:1996;1540-1546.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1540-1546
    • Sweder, K.S.1    Chun, R.2    Mori, T.3    Hanawalt, P.C.4
  • 76
    • 0031666241 scopus 로고    scopus 로고
    • Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH
    • Coin F., Marinoni J.C., Rodolfo C., Fribourg S., Pedrini A.M., Egly J.-M. Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH. Nat. Genet. 20:1998;184-188.
    • (1998) Nat. Genet , vol.20 , pp. 184-188
    • Coin, F.1    Marinoni, J.C.2    Rodolfo, C.3    Fribourg, S.4    Pedrini, A.M.5    Egly, J.-M.6
  • 77
    • 0030570316 scopus 로고    scopus 로고
    • A 3' -> 5' XPB helicase defect in repair/transcription factor TFIIH of xeroderma pigmentosum group B affects both DNA repair and transcription
    • Hwang J.R., Moncollin V., Vermeulen W., Seroz T., van Vuuren H., Hoeijmakers J.H.J., Egly J.-M. A 3' -> 5' XPB helicase defect in repair/transcription factor TFIIH of xeroderma pigmentosum group B affects both DNA repair and transcription. J. Biol. Chem. 271:1996;15898-15904.
    • (1996) J. Biol. Chem , vol.271 , pp. 15898-15904
    • Hwang, J.R.1    Moncollin, V.2    Vermeulen, W.3    Seroz, T.4    Van Vuuren, H.5    Hoeijmakers, J.H.J.6    Egly, J.-M.7
  • 78
    • 0029079792 scopus 로고
    • Lethality in yeast of trichothiodystrophy (TTD) mutations in the human xeroderma pigmentosum group D gene. Implications for transcriptional defect in TTD
    • Guzder S.N., Sung P., Prakash S., Prakash L. Lethality in yeast of trichothiodystrophy (TTD) mutations in the human xeroderma pigmentosum group D gene. Implications for transcriptional defect in TTD. J. Biol. Chem. 270:1995;17660-17663.
    • (1995) J. Biol. Chem , vol.270 , pp. 17660-17663
    • Guzder, S.N.1    Sung, P.2    Prakash, S.3    Prakash, L.4
  • 79
    • 0031013308 scopus 로고    scopus 로고
    • Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein
    • Evans E., Fellows J., Coffer A., Wood R.D. Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein. EMBO J. 16:1997;625-638.
    • (1997) EMBO J , vol.16 , pp. 625-638
    • Evans, E.1    Fellows, J.2    Coffer, A.3    Wood, R.D.4
  • 80
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • Evans E., Moggs J.G., Hwang J.R., Egly J.-M., Wood R.D. Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J. 16:1997;6559-6573.
    • (1997) EMBO J , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.R.3    Egly, J.-M.4    Wood, R.D.5
  • 81
    • 0027391296 scopus 로고
    • Inhibition of Rad3 DNA helicase activity by DNA adducts and abasic sites: Implications for the role of a DNA helicase in damage-specific incision of DNA
    • Naegeli H., Bardwell L., Friedberg E.C. Inhibition of Rad3 DNA helicase activity by DNA adducts and abasic sites: implications for the role of a DNA helicase in damage-specific incision of DNA. Biochemistry. 32:1993;613-621.
    • (1993) Biochemistry , vol.32 , pp. 613-621
    • Naegeli, H.1    Bardwell, L.2    Friedberg, E.C.3
  • 82
    • 0028310828 scopus 로고
    • Negative superhelicity promotes ATP-dependent binding of yeast RAD3 protein to ultraviolet-damaged DNA
    • Sung P., Watkins J.F., Prakash L., Prakash S. Negative superhelicity promotes ATP-dependent binding of yeast RAD3 protein to ultraviolet-damaged DNA. J. Biol. Chem. 269:1994;8303-8308.
    • (1994) J. Biol. Chem , vol.269 , pp. 8303-8308
    • Sung, P.1    Watkins, J.F.2    Prakash, L.3    Prakash, S.4
  • 83
    • 0029974576 scopus 로고    scopus 로고
    • Nucleotide excision repair in yeast is mediated by sequential assembly of repair factors and not by a pre-assembled repairosome
    • Guzder S.N., Sung P., Prakash L., Prakash S. Nucleotide excision repair in yeast is mediated by sequential assembly of repair factors and not by a pre-assembled repairosome. J. Biol. Chem. 271:1996;8903-8910.
    • (1996) J. Biol. Chem , vol.271 , pp. 8903-8910
    • Guzder, S.N.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 84
    • 0028932889 scopus 로고
    • The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor
    • Park C.H., Mu D., Reardon J.T., Sancar A. The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor. J. Biol. Chem. 270:1995;4896-4902.
    • (1995) J. Biol. Chem , vol.270 , pp. 4896-4902
    • Park, C.H.1    Mu, D.2    Reardon, J.T.3    Sancar, A.4
  • 85
    • 0030817140 scopus 로고    scopus 로고
    • DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H
    • Nocentini S., Coin F., Saijo M., Tanaka K., Egly J.-M. DNA damage recognition by XPA protein promotes efficient recruitment of transcription factor II H. J. Biol. Chem. 272:1997;22991-22994.
    • (1997) J. Biol. Chem , vol.272 , pp. 22991-22994
    • Nocentini, S.1    Coin, F.2    Saijo, M.3    Tanaka, K.4    Egly, J.-M.5
  • 86
    • 0028356906 scopus 로고
    • Yeast nucleotide excision repair proteins Rad2 and Rad4 interact with RNA polymerase II basal transcription factor b (TFIIH)
    • Bardwell A.J., Bardwell L., Iyer N., Svejstrup J.Q., Feaver W.J., Kornberg R.D., Friedberg E.C. Yeast nucleotide excision repair proteins Rad2 and Rad4 interact with RNA polymerase II basal transcription factor b (TFIIH). Mol. Cell. Biol. 14:1994;3569-3576.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 3569-3576
    • Bardwell, A.J.1    Bardwell, L.2    Iyer, N.3    Svejstrup, J.Q.4    Feaver, W.J.5    Kornberg, R.D.6    Friedberg, E.C.7
  • 88
    • 0030944206 scopus 로고    scopus 로고
    • Model for XPC-independent transcription-coupled repair of pyrimidine dimers in humans
    • Mu D., Sancar A. Model for XPC-independent transcription-coupled repair of pyrimidine dimers in humans. J. Biol. Chem. 272:1997;7570-7573.
    • (1997) J. Biol. Chem , vol.272 , pp. 7570-7573
    • Mu, D.1    Sancar, A.2
  • 89
    • 0030716255 scopus 로고    scopus 로고
    • Characterization of reaction intermediates of human excision repair nuclease
    • Mu D., Wakasugi M., Hsu D.S., Sancar A. Characterization of reaction intermediates of human excision repair nuclease. J. Biol. Chem. 272:1997;28971-28979.
    • (1997) J. Biol. Chem , vol.272 , pp. 28971-28979
    • Mu, D.1    Wakasugi, M.2    Hsu, D.S.3    Sancar, A.4
  • 90
    • 0030025947 scopus 로고    scopus 로고
    • Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein
    • Iyer N., Reagan M.S., Wu K.J., Canagarajah B., Friedberg E.C. Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. Biochemistry. 35:1996;2157-2167.
    • (1996) Biochemistry , vol.35 , pp. 2157-2167
    • Iyer, N.1    Reagan, M.S.2    Wu, K.J.3    Canagarajah, B.4    Friedberg, E.C.5
  • 91
    • 0029784467 scopus 로고    scopus 로고
    • Transcription factor TFIIH and DNA endonuclease Rad2 constitute yeast nucleotide excision repair factor 3: Implications for nucleotide excision repair and Cockayne syndrome
    • Habraken Y., Sung P., Prakash S., Prakash L. Transcription factor TFIIH and DNA endonuclease Rad2 constitute yeast nucleotide excision repair factor 3: implications for nucleotide excision repair and Cockayne syndrome. Proc. Natl. Acad. Sci. USA. 93:1996;10718-10722.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10718-10722
    • Habraken, Y.1    Sung, P.2    Prakash, S.3    Prakash, L.4
  • 92
    • 0021905437 scopus 로고
    • DNA repair in an active gene: Removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall
    • Bohr V.A., Smith C.A., Okumoto D.S., Hanawalt P.C. DNA repair in an active gene: removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall. Cell. 40:1985;359-369.
    • (1985) Cell , vol.40 , pp. 359-369
    • Bohr, V.A.1    Smith, C.A.2    Okumoto, D.S.3    Hanawalt, P.C.4
  • 93
    • 0030013201 scopus 로고    scopus 로고
    • Relationships between DNA repair and transcription
    • Friedberg E.C. Relationships between DNA repair and transcription. Annu. Rev. Biochem. 65:1996;15-42.
    • (1996) Annu. Rev. Biochem , vol.65 , pp. 15-42
    • Friedberg, E.C.1
  • 94
    • 0023663101 scopus 로고
    • Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene
    • Mellon I., Spivak G., Hanawalt P.C. Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene. Cell. 51:1987;241-249.
    • (1987) Cell , vol.51 , pp. 241-249
    • Mellon, I.1    Spivak, G.2    Hanawalt, P.C.3
  • 95
    • 0026354699 scopus 로고
    • Escherichia coli mfdmutant deficient in 'mutation frequency decline' lacks strand-specific repair: In vitro complementation with purified coupling factor
    • Selby C.P., Witkin E.M., Sancar A. Escherichia coli mfdmutant deficient in 'mutation frequency decline' lacks strand-specific repair: in vitro complementation with purified coupling factor. Proc. Natl. Acad. Sci. USA. 88:1991;11574-11578.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11574-11578
    • Selby, C.P.1    Witkin, E.M.2    Sancar, A.3
  • 96
    • 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
  • 97
    • 0025341294 scopus 로고
    • The genetic defect in Cockayne syndrome is associated with a defect in repair of UV-induced DNA damage in transcriptionally active DNA
    • Venema J., Mullenders L.H., Natarajan A.T., van Zeeland A.A., Mayne L.V. The genetic defect in Cockayne syndrome is associated with a defect in repair of UV-induced DNA damage in transcriptionally active DNA. Proc. Natl. Acad. Sci. USA. 87:1990;4707-4711.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4707-4711
    • Venema, J.1    Mullenders, L.H.2    Natarajan, A.T.3    Van Zeeland, A.A.4    Mayne, L.V.5
  • 99
    • 0030902253 scopus 로고    scopus 로고
    • Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells
    • Balajee A.S., May A., Dianov G.L., Friedberg E.C., Bohr V.A. Reduced RNA polymerase II transcription in intact and permeabilized Cockayne syndrome group B cells. Proc. Natl. Acad. Sci. USA. 94:1997;4306-4311.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4306-4311
    • Balajee, A.S.1    May, A.2    Dianov, G.L.3    Friedberg, E.C.4    Bohr, V.A.5
  • 100
    • 0030862095 scopus 로고    scopus 로고
    • Reduced RNA polymerase II transcription in extracts of Cockayne syndrome and xeroderma pigmentosum/Cockayne syndrome cells
    • Dianov G.L., Houle J.F., Iyer N., Bohr V.A., Friedberg E.C. Reduced RNA polymerase II transcription in extracts of Cockayne syndrome and xeroderma pigmentosum/Cockayne syndrome cells. Nucleic Acids Res. 25:1997;3636-3642.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3636-3642
    • Dianov, G.L.1    Houle, J.F.2    Iyer, N.3    Bohr, V.A.4    Friedberg, E.C.5
  • 101
    • 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. 17:1997;6803-6814.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 6803-6814
    • Tantin, D.1    Kansal, A.2    Carey, M.3
  • 103
    • 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. USA. 94:1997;11205-11209.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11205-11209
    • Selby, C.P.1    Sancar, A.2
  • 105
    • 0029744847 scopus 로고    scopus 로고
    • RAD26, the yeast homolog of human Cockayne's syndrome group B gene, encodes a DNA-dependent ATPase
    • Guzder S.N., Habraken Y., Sung P., Prakash L., Prakash S. RAD26, the yeast homolog of human Cockayne's syndrome group B gene, encodes a DNA-dependent ATPase. J. Biol. Chem. 271:1996;18314-18317.
    • (1996) J. Biol. Chem , vol.271 , pp. 18314-18317
    • Guzder, S.N.1    Habraken, Y.2    Sung, P.3    Prakash, L.4    Prakash, S.5
  • 106
    • 0028969976 scopus 로고
    • Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties
    • Selby C.P., Sancar A. Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties. J. Biol. Chem. 270:1995;4882-4889.
    • (1995) J. Biol. Chem , vol.270 , pp. 4882-4889
    • Selby, C.P.1    Sancar, A.2
  • 107
    • 0031020871 scopus 로고    scopus 로고
    • Human transcription-repair coupling factor CSB/ERCC6 is a DNA- stimulated ATPase but is not a helicase and does not disrupt the ternary transcription complex of stalled RNA polymerase II
    • Selby C.P., Sancar A. Human transcription-repair coupling factor CSB/ERCC6 is a DNA- stimulated ATPase but is not a helicase and does not disrupt the ternary transcription complex of stalled RNA polymerase II. J. Biol. Chem. 272:1997;1885-1890.
    • (1997) J. Biol. Chem , vol.272 , pp. 1885-1890
    • Selby, C.P.1    Sancar, A.2
  • 109
    • 0026465665 scopus 로고
    • ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes
    • Troelstra C., van Gool A., Vermeulen W., Bootsma D., Hoeijmakers J.H. ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes. Cell. 71:1992;939-953.
    • (1992) Cell , vol.71 , pp. 939-953
    • Troelstra, C.1    Van Gool, A.2    Vermeulen, W.3    Bootsma, D.4    Hoeijmakers, J.H.5
  • 110
    • 0032561475 scopus 로고    scopus 로고
    • RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62
    • Tantin D. RNA polymerase II elongation complexes containing the Cockayne syndrome group B protein interact with a molecular complex containing the transcription factor IIH components xeroderma pigmentosum B and p62. J. Biol. Chem. 273:1998;27794-27799.
    • (1998) J. Biol. Chem , vol.273 , pp. 27794-27799
    • Tantin, D.1
  • 111
    • 0030838622 scopus 로고    scopus 로고
    • Transitions in the coupling of transcription and nucleotide excision repair within RNA polymerase II-transcribed genes of Saccharomyces cerevisiae
    • Tijsterman M., Verhage R.A., van de Putte P., Tasseron N., de Jong J.G., Brouwer J. Transitions in the coupling of transcription and nucleotide excision repair within RNA polymerase II-transcribed genes of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 94:1997;8027-8032.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8027-8032
    • Tijsterman, M.1    Verhage, R.A.2    Van De Putte, P.3    Tasseron, N.4    De Jong, J.G.5    Brouwer, J.6
  • 112
    • 0030873551 scopus 로고    scopus 로고
    • Sequence-specific and domain-specific DNA repair in xeroderma pigmentosum and Cockayne syndrome cells
    • Tu Y., Bates S., Pfeifer G.P. Sequence-specific and domain-specific DNA repair in xeroderma pigmentosum and Cockayne syndrome cells. J. Biol. Chem. 272:1997;20747-20755.
    • (1997) J. Biol. Chem , vol.272 , pp. 20747-20755
    • Tu, Y.1    Bates, S.2    Pfeifer, G.P.3
  • 113
    • 0032565540 scopus 로고    scopus 로고
    • The transcription-repair coupling factor CSA is required for efficient repair only during the elongation stages of RNA polymerase II transcription
    • Tu Y., Bates S., Pfeifer G.P. The transcription-repair coupling factor CSA is required for efficient repair only during the elongation stages of RNA polymerase II transcription. Mutat. Res. 400:1998;143-151.
    • (1998) Mutat. Res , vol.400 , pp. 143-151
    • Tu, Y.1    Bates, S.2    Pfeifer, G.P.3
  • 114
    • 0025190985 scopus 로고
    • The residual repair capacity of xeroderma pigmentosum complementation group C fibroblasts is highly specific for transcriptionally active DNA
    • Venema J., van Hoffen A., Natarajan A.T., van Zeeland A.A., Mullenders L.H. The residual repair capacity of xeroderma pigmentosum complementation group C fibroblasts is highly specific for transcriptionally active DNA. Nucleic Acids Res. 18:1990;443-448.
    • (1990) Nucleic Acids Res , vol.18 , pp. 443-448
    • Venema, J.1    Van Hoffen, A.2    Natarajan, A.T.3    Van Zeeland, A.A.4    Mullenders, L.H.5
  • 115
    • 0028106162 scopus 로고
    • Transcript cleavage by RNA polymerase II arrested by a cyclobutane pyrimidine dimer in the DNA template
    • Donahue B.A., Yin S., Taylor J.S., Reines D., Hanawalt P.C. Transcript cleavage by RNA polymerase II arrested by a cyclobutane pyrimidine dimer in the DNA template. Proc. Natl. Acad. Sci. USA. 91:1994;8502-8506.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8502-8506
    • Donahue, B.A.1    Yin, S.2    Taylor, J.S.3    Reines, D.4    Hanawalt, P.C.5
  • 116
    • 0025610725 scopus 로고
    • Transcription preferentially inhibits nucleotide excision repair of the template DNA strand in vitro
    • Selby C.P., Sancar A. Transcription preferentially inhibits nucleotide excision repair of the template DNA strand in vitro. J. Biol. Chem. 265:1990;21330-21336.
    • (1990) J. Biol. Chem , vol.265 , pp. 21330-21336
    • Selby, C.P.1    Sancar, A.2
  • 117
    • 0030804783 scopus 로고    scopus 로고
    • RNA polymerase II stalled at a thymine dimer: Footprint and effect on excision repair
    • Selby C.P., Drapkin R., Reinberg D., Sancar A. RNA polymerase II stalled at a thymine dimer: footprint and effect on excision repair. Nucleic Acids Res. 25:1997;787-793.
    • (1997) Nucleic Acids Res , vol.25 , pp. 787-793
    • Selby, C.P.1    Drapkin, R.2    Reinberg, D.3    Sancar, A.4
  • 118
    • 0029859295 scopus 로고    scopus 로고
    • UV-induced ubiquitination of RNA polymerase II: A novel modification deficient in Cockayne syndrome cells
    • Bregman D.B., Halaban R., Henning K.A., Friedberg E.C., Warren S.L. UV-induced ubiquitination of RNA polymerase II: a novel modification deficient in Cockayne syndrome cells. Proc. Natl. Acad. Sci. USA. 93:1996;11586-11590.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11586-11590
    • Bregman, D.B.1    Halaban, R.2    Henning, K.A.3    Friedberg, E.C.4    Warren, S.L.5
  • 119
    • 0032570562 scopus 로고    scopus 로고
    • Ultraviolet radiation-induced ubiquitination and proteasomal degradation of the large subunit of RNA polymerase II. Implications for transcription-coupled DNA repair
    • Ratner J.N., Balasubramanian B., Corden J., Warren S.L., Bregman D.B. Ultraviolet radiation-induced ubiquitination and proteasomal degradation of the large subunit of RNA polymerase II. Implications for transcription-coupled DNA repair. J. Biol. Chem. 273:1998;5184-5189.
    • (1998) J. Biol. Chem , vol.273 , pp. 5184-5189
    • Ratner, J.N.1    Balasubramanian, B.2    Corden, J.3    Warren, S.L.4    Bregman, D.B.5
  • 120
    • 0030739911 scopus 로고    scopus 로고
    • The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factor
    • Weeda G., Rossignol M., Fraser R.A., Winkler G.S., Vermeulen W., van't Veer L.J., Ma L., Hoeijmakers J.H., Egly J.-M. The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factor. Nucleic Acids Res. 25:1997;2274-2283.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2274-2283
    • Weeda, G.1    Rossignol, M.2    Fraser, R.A.3    Winkler, G.S.4    Vermeulen, W.5    Van't Veer, L.J.6    Ma, L.7    Hoeijmakers, J.H.8    Egly, J.-M.9
  • 122
    • 0029910712 scopus 로고    scopus 로고
    • Dual requirement for the yeast MMS19 gene in DNA repair and RNA polymerase II transcription
    • Lauder S., Bankmann M., Guzder S.N., Sung P., Prakash L., Prakash S. Dual requirement for the yeast MMS19 gene in DNA repair and RNA polymerase II transcription. Mol. Cell. Biol. 16:1996;6783-6793.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 6783-6793
    • Lauder, S.1    Bankmann, M.2    Guzder, S.N.3    Sung, P.4    Prakash, L.5    Prakash, S.6
  • 123
    • 0030858644 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae mms19mutants are deficient in transcription- coupled and global nucleotide excision repair
    • Lombaerts M., Tijsterman M., Verhage R.A., Brouwer J. Saccharomyces cerevisiae mms19mutants are deficient in transcription- coupled and global nucleotide excision repair. Nucleic Acids Res. 25:1997;3974-3979.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3974-3979
    • Lombaerts, M.1    Tijsterman, M.2    Verhage, R.A.3    Brouwer, J.4
  • 125
    • 0031026977 scopus 로고    scopus 로고
    • The gene encoding p44, a subunit of the transcription factor TFIIH, is involved in large-scale deletions associated with Werdnig-Hoffmann disease
    • Burglen L., Seroz T., Miniou P., Lefebvre S., Burlet P., Munnich A., Pequignot E.V., Egly J.-M., Melki J. The gene encoding p44, a subunit of the transcription factor TFIIH, is involved in large-scale deletions associated with Werdnig-Hoffmann disease. Am. J. Hum. Genet. 60:1997;72-79.
    • (1997) Am. J. Hum. Genet , vol.60 , pp. 72-79
    • Burglen, L.1    Seroz, T.2    Miniou, P.3    Lefebvre, S.4    Burlet, P.5    Munnich, A.6    Pequignot, E.V.7    Egly, J.-M.8    Melki, J.9
  • 127
    • 0029814685 scopus 로고    scopus 로고
    • TFIIH-mediated nucleotide excision repair and initiation of mRNA transcription in an optimized cell-free DNA repair and RNA transcription assay
    • Satoh M.S., Hanawalt P.C. TFIIH-mediated nucleotide excision repair and initiation of mRNA transcription in an optimized cell-free DNA repair and RNA transcription assay. Nucleic Acids Res. 24:1996;3576-3582.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3576-3582
    • Satoh, M.S.1    Hanawalt, P.C.2
  • 129
    • 0031834926 scopus 로고    scopus 로고
    • TATA binding protein discriminates between different lesions on DNA, resulting in a transcription decrease
    • Coin F., Frit P., Viollet B., Salles B., Egly J.-M. TATA binding protein discriminates between different lesions on DNA, resulting in a transcription decrease. Mol. Cell. Biol. 18:1998;3907-3914.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 3907-3914
    • Coin, F.1    Frit, P.2    Viollet, B.3    Salles, B.4    Egly, J.-M.5
  • 130
    • 0031943276 scopus 로고    scopus 로고
    • Yeast RNA polymerase II transcription in vitro is inhibited in the presence of nucleotide excision repair: Complementation of inhibition by Holo-TFIIH and requirement for RAD26
    • You Z., Feaver W.J., Friedberg E.C. Yeast RNA polymerase II transcription in vitro is inhibited in the presence of nucleotide excision repair: complementation of inhibition by Holo-TFIIH and requirement for RAD26. Mol. Cell. Biol. 18:1998;2668-2676.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 2668-2676
    • You, Z.1    Feaver, W.J.2    Friedberg, E.C.3
  • 131
    • 0029941444 scopus 로고    scopus 로고
    • The sensitivity of Cockayne's syndrome cells to DNA-damaging agents is not due to defective transcription-coupled repair of active genes
    • van Oosterwijk M.F., Versteeg A., Filon R., van Zeeland A.A., Mullenders L.H. The sensitivity of Cockayne's syndrome cells to DNA-damaging agents is not due to defective transcription-coupled repair of active genes. Mol. Cell. Biol. 16:1996;4436-4444.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 4436-4444
    • Van Oosterwijk, M.F.1    Versteeg, A.2    Filon, R.3    Van Zeeland, A.A.4    Mullenders, L.H.5
  • 132
    • 0032577452 scopus 로고    scopus 로고
    • Lack of transcription-coupled repair of acetylaminofluorene DNA adducts in human fibroblasts contrasts their efficient inhibition of transcription
    • van Oosterwijk M.F., Filon R., de Groot A.J.L., van Zeeland A.A., Mullenders L.H.F. Lack of transcription-coupled repair of acetylaminofluorene DNA adducts in human fibroblasts contrasts their efficient inhibition of transcription. J. Biol. Chem. 273:1998;13599-13604.
    • (1998) J. Biol. Chem , vol.273 , pp. 13599-13604
    • Van Oosterwijk, M.F.1    Filon, R.2    De Groot, A.J.L.3    Van Zeeland, A.A.4    Mullenders, L.H.F.5
  • 133
    • 0030998797 scopus 로고    scopus 로고
    • Regulation of cdk/cyclin complexes during the cell cycle
    • Arellano M., Moreno S. Regulation of cdk/cyclin complexes during the cell cycle. Int. J. Biochem. Cell. Biol. 29:1997;559-573.
    • (1997) Int. J. Biochem. Cell. Biol , vol.29 , pp. 559-573
    • Arellano, M.1    Moreno, S.2
  • 134
    • 0028856425 scopus 로고
    • MAT1 ('ménage-à-trois') a new RING finger protein subunit stabilizing cyclin H-Cdk7 complexes in starfish and Xenopus CAK
    • Devault A., Martinez A.M., Fesquet D., Labbe J.C., Morin N., Tassan J.P., Nigg E.A., Cavadore J.C., Dorée M. MAT1 ('ménage-à-trois') a new RING finger protein subunit stabilizing cyclin H-Cdk7 complexes in starfish and Xenopus CAK. EMBO J. 14:1995;5027-5036.
    • (1995) EMBO J , vol.14 , pp. 5027-5036
    • Devault, A.1    Martinez, A.M.2    Fesquet, D.3    Labbe, J.C.4    Morin, N.5    Tassan, J.P.6    Nigg, E.A.7    Cavadore, J.C.8    Dorée, M.9
  • 135
    • 0028807103 scopus 로고
    • Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase
    • Fisher R.P., Jin P., Chamberlin H.M., Morgan D.O. Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase. Cell. 83:1995;47-57.
    • (1995) Cell , vol.83 , pp. 47-57
    • Fisher, R.P.1    Jin, P.2    Chamberlin, H.M.3    Morgan, D.O.4
  • 136
    • 0028882228 scopus 로고
    • In vitro assembly of a functional human Cdk7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein
    • Tassan J.P., Jaquenoud M., Fry A.M., Frutiger S., Hughes G.J., Nigg E.A. In vitro assembly of a functional human Cdk7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein. EMBO J. 14:1995;5608-5617.
    • (1995) EMBO J , vol.14 , pp. 5608-5617
    • Tassan, J.P.1    Jaquenoud, M.2    Fry, A.M.3    Frutiger, S.4    Hughes, G.J.5    Nigg, E.A.6
  • 137
    • 0030976052 scopus 로고    scopus 로고
    • Regulation of Cdk7 substrate specificity by MAT1 and TFIIH
    • Yankulov K.Y., Bentley D.L. Regulation of Cdk7 substrate specificity by MAT1 and TFIIH. EMBO J. 16:1997;1638-1646.
    • (1997) EMBO J , vol.16 , pp. 1638-1646
    • Yankulov, K.Y.1    Bentley, D.L.2
  • 138
    • 0029066929 scopus 로고
    • KIN28 encodes a C-terminal domain kinase that controls mRNA transcription in Saccharomyces cerevisiaebut lacks cyclin-dependent kinase-activating kinase (CAK) activity
    • Cismowski M.J., Laff G.M., Solomon M.J., Reed S.I. KIN28 encodes a C-terminal domain kinase that controls mRNA transcription in Saccharomyces cerevisiaebut lacks cyclin-dependent kinase-activating kinase (CAK) activity. Mol. Cell. Biol. 15:1995;2983-2992.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 2983-2992
    • Cismowski, M.J.1    Laff, G.M.2    Solomon, M.J.3    Reed, S.I.4
  • 139
    • 0030598908 scopus 로고    scopus 로고
    • Civ1 (CAK in vivo), a novel Cdk-activating kinase
    • Thuret J.Y., Valay J.G., Faye G., Mann C. Civ1 (CAK in vivo), a novel Cdk-activating kinase. Cell. 86:1996;565-576.
    • (1996) Cell , vol.86 , pp. 565-576
    • Thuret, J.Y.1    Valay, J.G.2    Faye, G.3    Mann, C.4
  • 140
    • 0030598865 scopus 로고    scopus 로고
    • The Cdk-activating kinase (CAK) from budding yeast
    • Kaldis P., Sutton A., Solomon M.J. The Cdk-activating kinase (CAK) from budding yeast. Cell. 86:1996;553-564.
    • (1996) Cell , vol.86 , pp. 553-564
    • Kaldis, P.1    Sutton, A.2    Solomon, M.J.3
  • 141
    • 0029835809 scopus 로고    scopus 로고
    • A cyclin-dependent kinase-activating kinase (CAK) in budding yeast unrelated to vertebrate CAK
    • Espinoza F.H., Farrell A., Erdjument-Bromage H., Tempst P., Morgan D.O. A cyclin-dependent kinase-activating kinase (CAK) in budding yeast unrelated to vertebrate CAK. Science. 273:1996;1714-1717.
    • (1996) Science , vol.273 , pp. 1714-1717
    • Espinoza, F.H.1    Farrell, A.2    Erdjument-Bromage, H.3    Tempst, P.4    Morgan, D.O.5
  • 142
    • 0028089946 scopus 로고
    • Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase)
    • Tassan J.P., Schultz S.J., Bartek J., Nigg E.A. Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase). J. Cell Biol. 127:1994;467-478.
    • (1994) J. Cell Biol , vol.127 , pp. 467-478
    • Tassan, J.P.1    Schultz, S.J.2    Bartek, J.3    Nigg, E.A.4
  • 143
    • 0031937443 scopus 로고    scopus 로고
    • Repression of TFIIH transcriptional activity and TFIIH-associated cdk7 kinase activity at mitosis
    • Long J.J., Leresche A., Kriwacki R.W., Gottesfeld J.M. Repression of TFIIH transcriptional activity and TFIIH-associated cdk7 kinase activity at mitosis. Mol. Cell. Biol. 18:1998;1467-1476.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 1467-1476
    • Long, J.J.1    Leresche, A.2    Kriwacki, R.W.3    Gottesfeld, J.M.4
  • 144
    • 0029559249 scopus 로고
    • Identification of a Cdk-activating kinase in fission yeast
    • Buck V., Russell P., Millar J.B. Identification of a Cdk-activating kinase in fission yeast. EMBO J. 14:1995;6173-6183.
    • (1995) EMBO J , vol.14 , pp. 6173-6183
    • Buck, V.1    Russell, P.2    Millar, J.B.3
  • 145
    • 0029558989 scopus 로고
    • Schizosaccharomyces pombeMop1-Mcs2 is related to mammalian CAK
    • Damagnez V., Makela T.P., Cottarel G. Schizosaccharomyces pombeMop1-Mcs2 is related to mammalian CAK. EMBO J. 14:1995;6164-6172.
    • (1995) EMBO J , vol.14 , pp. 6164-6172
    • Damagnez, V.1    Makela, T.P.2    Cottarel, G.3
  • 146
    • 0030963966 scopus 로고    scopus 로고
    • Is Cdk7/cyclin H/MAT1 the genuine Cdk activating kinase in cycling Xenopusegg extracts?
    • Fesquet D., Morin N., Dorée M., Devault A. Is Cdk7/cyclin H/MAT1 the genuine Cdk activating kinase in cycling Xenopusegg extracts? Oncogene. 15:1997;1303-1307.
    • (1997) Oncogene , vol.15 , pp. 1303-1307
    • Fesquet, D.1    Morin, N.2    Dorée, M.3    Devault, A.4
  • 147
    • 0032005801 scopus 로고    scopus 로고
    • Cdk7 is essential for mitosis and for in vivo Cdk-activating kinase activity
    • Larochelle S., Pandur J., Fisher R.P., Salz H.K., Suter B. Cdk7 is essential for mitosis and for in vivo Cdk-activating kinase activity. Genes Dev. 12:1998;370-381.
    • (1998) Genes Dev , vol.12 , pp. 370-381
    • Larochelle, S.1    Pandur, J.2    Fisher, R.P.3    Salz, H.K.4    Suter, B.5
  • 150
    • 0029880959 scopus 로고    scopus 로고
    • Functional interactions between p53 and the TFIIH complex are affected by tumour-associated mutations
    • Léveillard T., Andera L., Bissonnette N., Schaeffer L., Bracco L., Egly J.-M., Wasylyk B. Functional interactions between p53 and the TFIIH complex are affected by tumour-associated mutations. EMBO J. 15:1996;1615-1624.
    • (1996) EMBO J , vol.15 , pp. 1615-1624
    • Léveillard, T.1    Andera, L.2    Bissonnette, N.3    Schaeffer, L.4    Bracco, L.5    Egly, J.-M.6    Wasylyk, B.7
  • 153
    • 0030610565 scopus 로고    scopus 로고
    • The Cdk7-cycH-p36 complex of transcription factor IIH phosphorylates p53, enhancing its sequence-specific DNA binding activity in vitro
    • Lu H., Fisher R.P., Bailey P., Levine A.J. The Cdk7-cycH-p36 complex of transcription factor IIH phosphorylates p53, enhancing its sequence-specific DNA binding activity in vitro. Mol. Cell. Biol. 17:1997;5923-5934.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 5923-5934
    • Lu, H.1    Fisher, R.P.2    Bailey, P.3    Levine, A.J.4
  • 154
    • 0032489377 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitor p16INK4A inhibits phosphorylation of RNA polymerase II by general transcription factor TFIIH
    • Serizawa H. Cyclin-dependent kinase inhibitor p16INK4A inhibits phosphorylation of RNA polymerase II by general transcription factor TFIIH. J. Biol. Chem. 273:1998;5427-5430.
    • (1998) J. Biol. Chem , vol.273 , pp. 5427-5430
    • Serizawa, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.