메뉴 건너뛰기




Volumn 9, Issue 8, 2013, Pages

High-Throughput Genetic and Gene Expression Analysis of the RNAPII-CTD Reveals Unexpected Connections to SRB10/CDK8

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE 8; MESSENGER RNA; RNA POLYMERASE II; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR ELF 1; TRANSCRIPTION FACTOR II B; TRANSCRIPTION FACTOR RPN4; UNCLASSIFIED DRUG;

EID: 84884651887     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1003758     Document Type: Article
Times cited : (20)

References (70)
  • 1
    • 0022132080 scopus 로고
    • Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases
    • Allison LA, Moyle M, Shales M, Ingles CJ, (1985) Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases. Cell 42: 599-610.
    • (1985) Cell , vol.42 , pp. 599-610
    • Allison, L.A.1    Moyle, M.2    Shales, M.3    Ingles, C.J.4
  • 2
    • 0009370184 scopus 로고
    • A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II
    • Corden JL, Cadena DL, Ahearn JM Jr, Dahmus ME, (1985) A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II. Proc Natl Acad Sci U S A 82: 7934-7938.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 7934-7938
    • Corden, J.L.1    Cadena, D.L.2    Ahearn Jr., J.M.3    Dahmus, M.E.4
  • 3
    • 84872405841 scopus 로고    scopus 로고
    • Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription
    • Heidemann M, Hintermair C, Voss K, Eick D, (2012) Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription. Biochim Biophys Acta 1829: 55-62.
    • (2012) Biochim Biophys Acta , vol.1829 , pp. 55-62
    • Heidemann, M.1    Hintermair, C.2    Voss, K.3    Eick, D.4
  • 4
    • 0023651270 scopus 로고
    • Functional redundancy and structural polymorphism in the large subunit of RNA polymerase II
    • Nonet M, Sweetser D, Young RA, (1987) Functional redundancy and structural polymorphism in the large subunit of RNA polymerase II. Cell 50: 909-915.
    • (1987) Cell , vol.50 , pp. 909-915
    • Nonet, M.1    Sweetser, D.2    Young, R.A.3
  • 5
    • 0023807922 scopus 로고
    • The C-terminal domain of the largest subunit of RNA polymerase II of saccharomyces cerevisiae, drosophila melanogaster, and mammals: A conserved structure with an essential function
    • Allison LA, Wong JK, Fitzpatrick VD, Moyle M, Ingles CJ, (1988) The C-terminal domain of the largest subunit of RNA polymerase II of saccharomyces cerevisiae, drosophila melanogaster, and mammals: A conserved structure with an essential function. Mol Cell Biol 8: 321-329.
    • (1988) Mol Cell Biol , vol.8 , pp. 321-329
    • Allison, L.A.1    Wong, J.K.2    Fitzpatrick, V.D.3    Moyle, M.4    Ingles, C.J.5
  • 6
    • 0024022636 scopus 로고
    • The C-terminal repeat domain of RNA polymerase II largest subunit is essential in vivo but is not required for accurate transcription initiation in vitro
    • Zehring WA, Lee JM, Weeks JR, Jokerst RS, Greenleaf AL, (1988) The C-terminal repeat domain of RNA polymerase II largest subunit is essential in vivo but is not required for accurate transcription initiation in vitro. Proc Natl Acad Sci U S A 85: 3698-3702.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 3698-3702
    • Zehring, W.A.1    Lee, J.M.2    Weeks, J.R.3    Jokerst, R.S.4    Greenleaf, A.L.5
  • 7
    • 0025027915 scopus 로고
    • RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals
    • Scafe C, Chao D, Lopes J, Hirsch JP, Henry S, et al. (1990) RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals. Nature 347: 491-4.
    • (1990) Nature , vol.347 , pp. 491-494
    • Scafe, C.1    Chao, D.2    Lopes, J.3    Hirsch, J.P.4    Henry, S.5
  • 8
    • 0025790439 scopus 로고
    • The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex
    • Lu H, Flores O, Weinmann R, Reinberg D, (1991) The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex. Proc Natl Acad Sci U S A 88: 10004-10008.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10004-10008
    • Lu, H.1    Flores, O.2    Weinmann, R.3    Reinberg, D.4
  • 9
    • 0037073061 scopus 로고    scopus 로고
    • Regulation of transcription elongation by phosphorylation
    • Kobor MS, Greenblatt J, (2002) Regulation of transcription elongation by phosphorylation. Biochim Biophys Acta 1577: 261-275.
    • (2002) Biochim Biophys Acta , vol.1577 , pp. 261-275
    • Kobor, M.S.1    Greenblatt, J.2
  • 10
    • 34347273423 scopus 로고    scopus 로고
    • Hyperphosphorylation of the C-terminal repeat domain of RNA polymerase II facilitates dissociation of its complex with mediator
    • Max T, Sogaard M, Svejstrup JQ, (2007) Hyperphosphorylation of the C-terminal repeat domain of RNA polymerase II facilitates dissociation of its complex with mediator. J Biol Chem 282: 14113-14120.
    • (2007) J Biol Chem , vol.282 , pp. 14113-14120
    • Max, T.1    Sogaard, M.2    Svejstrup, J.Q.3
  • 11
    • 15644372864 scopus 로고    scopus 로고
    • 5′-capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II
    • McCracken S, Fong N, Rosonina E, Yankulov K, Brothers G, et al. (1997) 5′-capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II. Genes Dev 11: 3306-3318.
    • (1997) Genes Dev , vol.11 , pp. 3306-3318
    • McCracken, S.1    Fong, N.2    Rosonina, E.3    Yankulov, K.4    Brothers, G.5
  • 12
    • 70350389837 scopus 로고    scopus 로고
    • Phosphorylation of the yeast Rpb1 C-terminal domain at serines 2, 5, and 7
    • Kim M, Suh H, Cho EJ, Buratowski S, (2009) Phosphorylation of the yeast Rpb1 C-terminal domain at serines 2, 5, and 7. J Biol Chem 284: 26421-26426.
    • (2009) J Biol Chem , vol.284 , pp. 26421-26426
    • Kim, M.1    Suh, H.2    Cho, E.J.3    Buratowski, S.4
  • 13
    • 65549156025 scopus 로고    scopus 로고
    • TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II
    • Akhtar MS, Heidemann M, Tietjen JR, Zhang DW, Chapman RD, et al. (2009) TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II. Mol Cell 34: 387-393.
    • (2009) Mol Cell , vol.34 , pp. 387-393
    • Akhtar, M.S.1    Heidemann, M.2    Tietjen, J.R.3    Zhang, D.W.4    Chapman, R.D.5
  • 14
    • 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 EJ, Kobor MS, Kim M, Greenblatt J, Buratowski S, (2001) Opposing effects of Ctk1 kinase and Fcp1 phosphatase at ser 2 of the RNA polymerase II C-terminal domain. Genes Dev 15: 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
  • 15
    • 84862977456 scopus 로고    scopus 로고
    • CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II
    • Mayer A, Heidemann M, Lidschreiber M, Schreieck A, Sun M, et al. (2012) CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II. Science 336: 1723-1725.
    • (2012) Science , vol.336 , pp. 1723-1725
    • Mayer, A.1    Heidemann, M.2    Lidschreiber, M.3    Schreieck, A.4    Sun, M.5
  • 16
    • 0033165865 scopus 로고    scopus 로고
    • An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae
    • Kobor MS, Archambault J, Lester W, Holstege FC, Gileadi O, et al. (1999) An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae. Mol Cell 4: 55-62.
    • (1999) Mol Cell , vol.4 , pp. 55-62
    • Kobor, M.S.1    Archambault, J.2    Lester, W.3    Holstege, F.C.4    Gileadi, O.5
  • 17
    • 0033564705 scopus 로고    scopus 로고
    • A protein phosphatase functions to recycle RNA polymerase II
    • Cho H, Kim TK, Mancebo H, Lane WS, Flores O, et al. (1999) A protein phosphatase functions to recycle RNA polymerase II. Genes Dev 13: 1540-1552.
    • (1999) Genes Dev , vol.13 , pp. 1540-1552
    • Cho, H.1    Kim, T.K.2    Mancebo, H.3    Lane, W.S.4    Flores, O.5
  • 18
    • 84863229897 scopus 로고    scopus 로고
    • Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination
    • Zhang DW, Mosley AL, Ramisetty SR, Rodriguez-Molina JB, Washburn MP, et al. (2012) Ssu72 phosphatase-dependent erasure of phospho-Ser7 marks on the RNA polymerase II C-terminal domain is essential for viability and transcription termination. J Biol Chem 287: 8541-8551.
    • (2012) J Biol Chem , vol.287 , pp. 8541-8551
    • Zhang, D.W.1    Mosley, A.L.2    Ramisetty, S.R.3    Rodriguez-Molina, J.B.4    Washburn, M.P.5
  • 19
    • 0024354605 scopus 로고
    • Intragenic and extragenic suppressors of mutations in the heptapeptide repeat domain of saccharomyces cerevisiae RNA polymerase II
    • Nonet ML, Young RA, (1989) Intragenic and extragenic suppressors of mutations in the heptapeptide repeat domain of saccharomyces cerevisiae RNA polymerase II. Genetics 123: 715-24.
    • (1989) Genetics , vol.123 , pp. 715-724
    • Nonet, M.L.1    Young, R.A.2
  • 20
    • 0027253864 scopus 로고
    • A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast
    • Thompson CM, Koleske AJ, Chao DM, Young RA, (1993) A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast. Cell 73: 1361-1375.
    • (1993) Cell , vol.73 , pp. 1361-1375
    • Thompson, C.M.1    Koleske, A.J.2    Chao, D.M.3    Young, R.A.4
  • 22
    • 33646023157 scopus 로고    scopus 로고
    • Genome-wide location of the coactivator mediator: Binding without activation and transient Cdk8 interaction on DNA
    • Andrau JC, van de Pasch L, Lijnzaad P, Bijma T, Koerkamp MG, et al. (2006) Genome-wide location of the coactivator mediator: Binding without activation and transient Cdk8 interaction on DNA. Mol Cell 22: 179-192.
    • (2006) Mol Cell , vol.22 , pp. 179-192
    • Andrau, J.C.1    van de Pasch, L.2    Lijnzaad, P.3    Bijma, T.4    Koerkamp, M.G.5
  • 23
    • 33646075157 scopus 로고    scopus 로고
    • Genome-wide occupancy profile of mediator and the Srb8-11 module reveals interactions with coding regions
    • Zhu X, Wiren M, Sinha I, Rasmussen NN, Linder T, et al. (2006) Genome-wide occupancy profile of mediator and the Srb8-11 module reveals interactions with coding regions. Mol Cell 22: 169-178.
    • (2006) Mol Cell , vol.22 , pp. 169-178
    • Zhu, X.1    Wiren, M.2    Sinha, I.3    Rasmussen, N.N.4    Linder, T.5
  • 25
    • 0035883746 scopus 로고    scopus 로고
    • The Swi5 activator recruits the mediator complex to the HO promoter without RNA polymerase II
    • Bhoite LT, Yu Y, Stillman DJ, (2001) The Swi5 activator recruits the mediator complex to the HO promoter without RNA polymerase II. Genes Dev 15: 2457-2469.
    • (2001) Genes Dev , vol.15 , pp. 2457-2469
    • Bhoite, L.T.1    Yu, Y.2    Stillman, D.J.3
  • 26
    • 0013592684 scopus 로고    scopus 로고
    • Activator-specific requirement of yeast mediator proteins for RNA polymerase II transcriptional activation
    • Han SJ, Lee YC, Gim BS, Ryu GH, Park SJ, et al. (1999) Activator-specific requirement of yeast mediator proteins for RNA polymerase II transcriptional activation. Mol Cell Biol 19: 979-988.
    • (1999) Mol Cell Biol , vol.19 , pp. 979-988
    • Han, S.J.1    Lee, Y.C.2    Gim, B.S.3    Ryu, G.H.4    Park, S.J.5
  • 28
    • 85027942059 scopus 로고    scopus 로고
    • A conserved mediator-CDK8 kinase module association regulates mediator-RNA polymerase II interaction
    • Tsai KL, Sato S, Tomomori-Sato C, Conaway RC, Conaway JW, et al. (2013) A conserved mediator-CDK8 kinase module association regulates mediator-RNA polymerase II interaction. Nat Struct Mol Biol 20: 611-619.
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 611-619
    • Tsai, K.L.1    Sato, S.2    Tomomori-Sato, C.3    Conaway, R.C.4    Conaway, J.W.5
  • 29
    • 0032110627 scopus 로고    scopus 로고
    • Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-dependent kinases
    • Hengartner CJ, Myer VE, Liao SM, Wilson CJ, Koh SS, et al. (1998) Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-dependent kinases. Mol Cell 2: 43-53.
    • (1998) Mol Cell , vol.2 , pp. 43-53
    • Hengartner, C.J.1    Myer, V.E.2    Liao, S.M.3    Wilson, C.J.4    Koh, S.S.5
  • 30
    • 0842347413 scopus 로고    scopus 로고
    • Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex
    • Liu Y, Kung C, Fishburn J, Ansari AZ, Shokat KM, et al. (2004) Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex. Mol Cell Biol 24: 1721-35.
    • (2004) Mol Cell Biol , vol.24 , pp. 1721-1735
    • Liu, Y.1    Kung, C.2    Fishburn, J.3    Ansari, A.Z.4    Shokat, K.M.5
  • 31
    • 0033000483 scopus 로고    scopus 로고
    • GAL4 is regulated by the RNA polymerase II holoenzyme-associated cyclin-dependent protein kinase SRB10/CDK8
    • Hirst M, Kobor MS, Kuriakose N, Greenblatt J, Sadowski I, (1999) GAL4 is regulated by the RNA polymerase II holoenzyme-associated cyclin-dependent protein kinase SRB10/CDK8. Mol Cell 3: 673-8.
    • (1999) Mol Cell , vol.3 , pp. 673-678
    • Hirst, M.1    Kobor, M.S.2    Kuriakose, N.3    Greenblatt, J.4    Sadowski, I.5
  • 32
    • 77956046092 scopus 로고    scopus 로고
    • Quantitative genetic interaction mapping using the E-MAP approach
    • Collins SR, Roguev A, Krogan NJ, (2010) Quantitative genetic interaction mapping using the E-MAP approach. Methods Enzymol 470: 205-231.
    • (2010) Methods Enzymol , vol.470 , pp. 205-231
    • Collins, S.R.1    Roguev, A.2    Krogan, N.J.3
  • 33
    • 0029037999 scopus 로고
    • Construction and analysis of yeast RNA polymerase II CTD deletion and substitution mutations
    • West ML, Corden JL, (1995) Construction and analysis of yeast RNA polymerase II CTD deletion and substitution mutations. Genetics 140: 1223-1233.
    • (1995) Genetics , vol.140 , pp. 1223-1233
    • West, M.L.1    Corden, J.L.2
  • 35
    • 77957766550 scopus 로고    scopus 로고
    • Uniform transitions of the general RNA polymerase II transcription complex
    • Mayer A, Lidschreiber M, Siebert M, Leike K, Soding J, et al. (2010) Uniform transitions of the general RNA polymerase II transcription complex. Nat Struct Mol Biol 17: 1272-1278.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1272-1278
    • Mayer, A.1    Lidschreiber, M.2    Siebert, M.3    Leike, K.4    Soding, J.5
  • 36
    • 80455140227 scopus 로고    scopus 로고
    • Splitting the task: Ubp8 and Ubp10 deubiquitinate different cellular pools of H2BK123
    • Schulze JM, Hentrich T, Nakanishi S, Gupta A, Emberly E, et al. (2011) Splitting the task: Ubp8 and Ubp10 deubiquitinate different cellular pools of H2BK123. Genes Dev 25: 2242-2247.
    • (2011) Genes Dev , vol.25 , pp. 2242-2247
    • Schulze, J.M.1    Hentrich, T.2    Nakanishi, S.3    Gupta, A.4    Emberly, E.5
  • 38
    • 77957786100 scopus 로고    scopus 로고
    • Gene-specific RNA polymerase II phosphorylation and the CTD code
    • Kim H, Erickson B, Luo W, Seward D, Graber JH, et al. (2010) Gene-specific RNA polymerase II phosphorylation and the CTD code. Nat Struct Mol Biol 17: 1279-1286.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1279-1286
    • Kim, H.1    Erickson, B.2    Luo, W.3    Seward, D.4    Graber, J.H.5
  • 39
    • 84856273602 scopus 로고    scopus 로고
    • A universal RNA polymerase II CTD cycle is orchestrated by complex interplays between kinase, phosphatase, and isomerase enzymes along genes
    • Bataille AR, Jeronimo C, Jacques PE, Laramee L, Fortin ME, et al. (2012) A universal RNA polymerase II CTD cycle is orchestrated by complex interplays between kinase, phosphatase, and isomerase enzymes along genes. Mol Cell 45: 158-170.
    • (2012) Mol Cell , vol.45 , pp. 158-170
    • Bataille, A.R.1    Jeronimo, C.2    Jacques, P.E.3    Laramee, L.4    Fortin, M.E.5
  • 40
    • 23944462969 scopus 로고    scopus 로고
    • Genome-wide map of nucleosome acetylation and methylation in yeast
    • Pokholok DK, Harbison CT, Levine S, Cole M, Hannett NM, et al. (2005) Genome-wide map of nucleosome acetylation and methylation in yeast. Cell 122: 517-527.
    • (2005) Cell , vol.122 , pp. 517-527
    • Pokholok, D.K.1    Harbison, C.T.2    Levine, S.3    Cole, M.4    Hannett, N.M.5
  • 41
    • 0037336041 scopus 로고    scopus 로고
    • Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast
    • Xiao T, Hall H, Kizer KO, Shibata Y, Hall MC, et al. (2003) Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeast. Genes Dev 17: 654-663.
    • (2003) Genes Dev , vol.17 , pp. 654-663
    • Xiao, T.1    Hall, H.2    Kizer, K.O.3    Shibata, Y.4    Hall, M.C.5
  • 42
    • 77958608570 scopus 로고    scopus 로고
    • A dual interface determines the recognition of RNA polymerase II by RNA capping enzyme
    • Suh MH, Meyer PA, Gu M, Ye P, Zhang M, et al. (2010) A dual interface determines the recognition of RNA polymerase II by RNA capping enzyme. J Biol Chem 285: 34027-34038.
    • (2010) J Biol Chem , vol.285 , pp. 34027-34038
    • Suh, M.H.1    Meyer, P.A.2    Gu, M.3    Ye, P.4    Zhang, M.5
  • 43
    • 37249015899 scopus 로고    scopus 로고
    • Transcribing RNA polymerase II is phosphorylated at CTD residue serine-7
    • Chapman RD, Heidemann M, Albert TK, Mailhammer R, Flatley A, et al. (2007) Transcribing RNA polymerase II is phosphorylated at CTD residue serine-7. Science 318: 1780-2.
    • (2007) Science , vol.318 , pp. 1780-1782
    • Chapman, R.D.1    Heidemann, M.2    Albert, T.K.3    Mailhammer, R.4    Flatley, A.5
  • 44
    • 84856285875 scopus 로고    scopus 로고
    • RNA polymerase II carboxy-terminal domain phosphorylation regulates protein stability of the Set2 methyltransferase and histone H3 di- and trimethylation at lysine 36
    • Fuchs SM, Kizer KO, Braberg H, Krogan NJ, Strahl BD, (2011) RNA polymerase II carboxy-terminal domain phosphorylation regulates protein stability of the Set2 methyltransferase and histone H3 di- and trimethylation at lysine 36. J Biol Chem 287: 3249-3256.
    • (2011) J Biol Chem , vol.287 , pp. 3249-3256
    • Fuchs, S.M.1    Kizer, K.O.2    Braberg, H.3    Krogan, N.J.4    Strahl, B.D.5
  • 45
    • 34247341747 scopus 로고    scopus 로고
    • H2A.Z-mediated localization of genes at the nuclear periphery confers epigenetic memory of previous transcriptional state
    • Brickner D, Cajigas I, Fondufe-Mittendorf Y, Ahmed S, Lee P, et al. (2007) H2A.Z-mediated localization of genes at the nuclear periphery confers epigenetic memory of previous transcriptional state. PLoS Biol 5: e81.
    • (2007) PLoS Biol , vol.5
    • Brickner, D.1    Cajigas, I.2    Fondufe-Mittendorf, Y.3    Ahmed, S.4    Lee, P.5
  • 46
    • 64549091902 scopus 로고    scopus 로고
    • Where does mediator bind in vivo?
    • Fan X, Struhl K, (2009) Where does mediator bind in vivo? PLoS One 4: e5029.
    • (2009) PLoS One , vol.4
    • Fan, X.1    Struhl, K.2
  • 47
    • 23744490065 scopus 로고    scopus 로고
    • Mediator expression profiling epistasis reveals a signal transduction pathway with antagonistic submodules and highly specific downstream targets
    • van de Peppel J, Kettelarij N, van Bakel H, Kockelkorn TT, van Leenen D, et al. (2005) Mediator expression profiling epistasis reveals a signal transduction pathway with antagonistic submodules and highly specific downstream targets. Mol Cell 19: 511-522.
    • (2005) Mol Cell , vol.19 , pp. 511-522
    • van de Peppel, J.1    Kettelarij, N.2    van Bakel, H.3    Kockelkorn, T.T.4    van Leenen, D.5
  • 48
    • 35548985701 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of Rpn4 is controlled by a phosphorylation-dependent ubiquitylation signal
    • Ju D, Xu H, Wang X, Xie Y, (2007) Ubiquitin-mediated degradation of Rpn4 is controlled by a phosphorylation-dependent ubiquitylation signal. Biochim Biophys Acta 1773: 1672-1680.
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 1672-1680
    • Ju, D.1    Xu, H.2    Wang, X.3    Xie, Y.4
  • 49
    • 0035089793 scopus 로고    scopus 로고
    • A compromised yeast RNA polymerase II enhances UV sensitivity in the absence of global genome nucleotide excision repair
    • Wong JMS, Ingles CJ, (2001) A compromised yeast RNA polymerase II enhances UV sensitivity in the absence of global genome nucleotide excision repair. Molecular and General Genetics 264: 842-851.
    • (2001) Molecular and General Genetics , vol.264 , pp. 842-851
    • Wong, J.M.S.1    Ingles, C.J.2
  • 50
    • 80053445278 scopus 로고    scopus 로고
    • Elevated proteasome capacity extends replicative lifespan in saccharomyces cerevisiae
    • Kruegel U, Robison B, Dange T, Kahlert G, Delaney JR, et al. (2011) Elevated proteasome capacity extends replicative lifespan in saccharomyces cerevisiae. PLoS Genet 7: e1002253.
    • (2011) PLoS Genet , vol.7
    • Kruegel, U.1    Robison, B.2    Dange, T.3    Kahlert, G.4    Delaney, J.R.5
  • 51
    • 77749274424 scopus 로고    scopus 로고
    • Proteasomal degradation of Rpn4 in saccharomyces cerevisiae is critical for cell viability under stressed conditions
    • Wang X, Xu H, Ha SW, Ju D, Xie Y, (2010) Proteasomal degradation of Rpn4 in saccharomyces cerevisiae is critical for cell viability under stressed conditions. Genetics 184: 335-342.
    • (2010) Genetics , vol.184 , pp. 335-342
    • Wang, X.1    Xu, H.2    Ha, S.W.3    Ju, D.4    Xie, Y.5
  • 52
    • 0036226237 scopus 로고    scopus 로고
    • Control of 26S proteasome expression by transcription factors regulating multidrug resistance in saccharomyces cerevisiae
    • Owsianik G, Balzi lL, Ghislain M, (2002) Control of 26S proteasome expression by transcription factors regulating multidrug resistance in saccharomyces cerevisiae. Mol Microbiol 43: 1295-1308.
    • (2002) Mol Microbiol , vol.43 , pp. 1295-1308
    • Owsianik, G.1    Balzi, L.2    Ghislain, M.3
  • 53
    • 0037426868 scopus 로고    scopus 로고
    • Srb10/Cdk8 regulates yeast filamentous growth by phosphorylating the transcription factor Ste12
    • Nelson C, Goto S, Lund K, Hung W, Sadowski I, (2003) Srb10/Cdk8 regulates yeast filamentous growth by phosphorylating the transcription factor Ste12. Nature 421: 187-190.
    • (2003) Nature , vol.421 , pp. 187-190
    • Nelson, C.1    Goto, S.2    Lund, K.3    Hung, W.4    Sadowski, I.5
  • 54
    • 84856786805 scopus 로고    scopus 로고
    • Cdk8 regulates stability of the transcription factor Phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae
    • Raithatha S, Su TC, Lourenco P, Goto S, Sadowski I, (2012) Cdk8 regulates stability of the transcription factor Phd1 to control pseudohyphal differentiation of saccharomyces cerevisiae. Mol Cell Biol 32: 664-674.
    • (2012) Mol Cell Biol , vol.32 , pp. 664-674
    • Raithatha, S.1    Su, T.C.2    Lourenco, P.3    Goto, S.4    Sadowski, I.5
  • 55
    • 33644843117 scopus 로고    scopus 로고
    • A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor
    • Hahn JS, Neef DW, Thiele DJ, (2006) A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor. Mol Microbiol 60: 240-251.
    • (2006) Mol Microbiol , vol.60 , pp. 240-251
    • Hahn, J.S.1    Neef, D.W.2    Thiele, D.J.3
  • 56
    • 84857176030 scopus 로고    scopus 로고
    • Sumoylation of transcription factor Gcn4 facilitates its Srb10-mediated clearance from promoters in yeast
    • Rosonina E, Duncan SM, Manley JL, (2012) Sumoylation of transcription factor Gcn4 facilitates its Srb10-mediated clearance from promoters in yeast. Genes Dev 26: 350-355.
    • (2012) Genes Dev , vol.26 , pp. 350-355
    • Rosonina, E.1    Duncan, S.M.2    Manley, J.L.3
  • 57
    • 0035339092 scopus 로고    scopus 로고
    • Negative regulation of Gcn4 and Msn2 transcription factors by Srb10 cyclin-dependent kinase
    • Chi Y, Huddleston MJ, Zhang X, Young RA, Annan RS, et al. (2001) Negative regulation of Gcn4 and Msn2 transcription factors by Srb10 cyclin-dependent kinase. Genes Dev 15: 1078-1092.
    • (2001) Genes Dev , vol.15 , pp. 1078-1092
    • Chi, Y.1    Huddleston, M.J.2    Zhang, X.3    Young, R.A.4    Annan, R.S.5
  • 58
    • 27744495040 scopus 로고    scopus 로고
    • A putative stimulatory role for activator turnover in gene expression
    • Lipford JR, Smith GT, Chi Y, Deshaies RJ, (2005) A putative stimulatory role for activator turnover in gene expression. Nature 438: 113-116.
    • (2005) Nature , vol.438 , pp. 113-116
    • Lipford, J.R.1    Smith, G.T.2    Chi, Y.3    Deshaies, R.J.4
  • 59
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in saccharomyces cerevisiae
    • Longtine MS, McKenzie A 3rd, Demarini DJ, Shah NG, Wach A, et al. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in saccharomyces cerevisiae. Yeast 14: 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie 3rd, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5
  • 60
    • 0009355836 scopus 로고
    • Fusion of escherichia coli lacZ to the cytochrome c gene of saccharomyces cerevisiae
    • Guarente L, Ptashne M, (1981) Fusion of escherichia coli lacZ to the cytochrome c gene of saccharomyces cerevisiae. Proc Natl Acad Sci U S A 78: 2199-2203.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 2199-2203
    • Guarente, L.1    Ptashne, M.2
  • 61
    • 78649938122 scopus 로고    scopus 로고
    • Functional overlap and regulatory links shape genetic interactions between signaling pathways
    • van Wageningen S, Kemmeren P, Lijnzaad P, Margaritis T, Benschop JJ, et al. (2010) Functional overlap and regulatory links shape genetic interactions between signaling pathways. Cell 143: 991-1004.
    • (2010) Cell , vol.143 , pp. 991-1004
    • van Wageningen, S.1    Kemmeren, P.2    Lijnzaad, P.3    Margaritis, T.4    Benschop, J.J.5
  • 62
    • 79955949044 scopus 로고    scopus 로고
    • The specificity and topology of chromatin interaction pathways in yeast
    • Lenstra TL, Benschop JJ, Kim T, Schulze JM, Brabers NA, et al. (2011) The specificity and topology of chromatin interaction pathways in yeast. Mol Cell 42: 536-549.
    • (2011) Mol Cell , vol.42 , pp. 536-549
    • Lenstra, T.L.1    Benschop, J.J.2    Kim, T.3    Schulze, J.M.4    Brabers, N.A.5
  • 63
    • 78651307692 scopus 로고    scopus 로고
    • YPA: An integrated repository of promoter features in saccharomyces cerevisiae
    • Chang DT, Huang CY, Wu CY, Wu WS, (2011) YPA: An integrated repository of promoter features in saccharomyces cerevisiae. Nucleic Acids Res 39: D647-52.
    • (2011) Nucleic Acids Res , vol.39
    • Chang, D.T.1    Huang, C.Y.2    Wu, C.Y.3    Wu, W.S.4
  • 65
    • 33846689706 scopus 로고    scopus 로고
    • Using GOstats to test gene lists for GO term association
    • Falcon S, Gentleman R, (2007) Using GOstats to test gene lists for GO term association. Bioinformatics 23: 257-258.
    • (2007) Bioinformatics , vol.23 , pp. 257-258
    • Falcon, S.1    Gentleman, R.2
  • 66
    • 69749117490 scopus 로고    scopus 로고
    • Linking cell cycle to histone modifications: SBF and H2B monoubiquitination machinery and cell-cycle regulation of H3K79 dimethylation
    • Schulze JM, Jackson J, Nakanishi S, Gardner JM, Hentrich T, et al. (2009) Linking cell cycle to histone modifications: SBF and H2B monoubiquitination machinery and cell-cycle regulation of H3K79 dimethylation. Mol Cell 35: 626-641.
    • (2009) Mol Cell , vol.35 , pp. 626-641
    • Schulze, J.M.1    Jackson, J.2    Nakanishi, S.3    Gardner, J.M.4    Hentrich, T.5
  • 67
    • 2142658771 scopus 로고    scopus 로고
    • Using chromatin immunoprecipitation to map cotranscriptional mRNA processing in saccharomyces cerevisiae
    • Keogh MC, Buratowski S, (2004) Using chromatin immunoprecipitation to map cotranscriptional mRNA processing in saccharomyces cerevisiae. Methods Mol Biol 257: 1-16.
    • (2004) Methods Mol Biol , vol.257 , pp. 1-16
    • Keogh, M.C.1    Buratowski, S.2
  • 68
    • 77949576511 scopus 로고    scopus 로고
    • rMAT-an R/Bioconductor package for analyzing ChIP-chip experiments
    • Droit A, Cheung C, Gottardo R, (2010) rMAT-an R/Bioconductor package for analyzing ChIP-chip experiments. Bioinformatics 26: 678-679.
    • (2010) Bioinformatics , vol.26 , pp. 678-679
    • Droit, A.1    Cheung, C.2    Gottardo, R.3
  • 69
    • 84857890387 scopus 로고    scopus 로고
    • CHROMATRA: A galaxy tool for visualizing genome-wide chromatin signatures
    • Hentrich T, Schulze JM, Emberly E, Kobor MS, (2012) CHROMATRA: A galaxy tool for visualizing genome-wide chromatin signatures. Bioinformatics 28: 717-718.
    • (2012) Bioinformatics , vol.28 , pp. 717-718
    • Hentrich, T.1    Schulze, J.M.2    Emberly, E.3    Kobor, M.S.4
  • 70
    • 0020645052 scopus 로고
    • Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast
    • Guarente L, (1983) Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol 101: 181-191.
    • (1983) Methods Enzymol , vol.101 , pp. 181-191
    • Guarente, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.