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Volumn 109, Issue 44, 2012, Pages 17931-17935

Structure of the Mediator Head module bound to the carboxy-terminal domain of RNA polymerase II

Author keywords

Cross linking; Transcriptional initiation; X ray crystallography; Yeast

Indexed keywords

HEAD MODULE PROTEIN; MEDIATOR COMPLEX; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 84868094446     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1215241109     Document Type: Article
Times cited : (101)

References (37)
  • 1
    • 79953162883 scopus 로고    scopus 로고
    • Function and regulation of the Mediator complex
    • Conaway RC, Conaway JW (2011) Function and regulation of the Mediator complex. Curr Opin Genet Dev 21:225-230.
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 225-230
    • Conaway, R.C.1    Conaway, J.W.2
  • 2
    • 18844451820 scopus 로고    scopus 로고
    • Mediator and the mechanism of transcriptional activation
    • Kornberg RD (2005) Mediator and the mechanism of transcriptional activation. Trends Biochem Sci 30:235-239.
    • (2005) Trends Biochem Sci , vol.30 , pp. 235-239
    • Kornberg, R.D.1
  • 3
    • 79952803747 scopus 로고    scopus 로고
    • Direct interaction of RNA polymerase II and mediator required for transcription in vivo
    • Soutourina J, Wydau S, Ambroise Y, Boschiero C, Werner M (2011) Direct interaction of RNA polymerase II and mediator required for transcription in vivo. Science 331: 1451-1454.
    • (2011) Science , vol.331 , pp. 1451-1454
    • Soutourina, J.1    Wydau, S.2    Ambroise, Y.3    Boschiero, C.4    Werner, M.5
  • 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
    • 0024507111 scopus 로고
    • Mutations in RNA polymerase II enhance or suppress mutations in GAL4
    • Allison LA, Ingles CJ (1989) Mutations in RNA polymerase II enhance or suppress mutations in GAL4. Proc Natl Acad Sci USA 86:2794-2798.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2794-2798
    • Allison, L.A.1    Ingles, C.J.2
  • 6
    • 0025027915 scopus 로고
    • RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals
    • Scafe C, et al. (1990) RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals. Nature 347:491-494.
    • (1990) Nature , vol.347 , pp. 491-494
    • Scafe, C.1
  • 7
    • 0026300116 scopus 로고
    • RNA polymerase II carboxy-terminal domain contributes to the response to multiple acidic activators in vitro
    • Liao SM, Taylor IC, Kingston RE, Young RA (1991) RNA polymerase II carboxy-terminal domain contributes to the response to multiple acidic activators in vitro. Genes Dev 5(12B):2431-2440.
    • (1991) Genes Dev , vol.5 , Issue.B12 , pp. 2431-2440
    • Liao, S.M.1    Taylor, I.C.2    Kingston, R.E.3    Young, R.A.4
  • 8
    • 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 123:715-724.
    • (1989) Genetics , vol.123 , pp. 715-724
    • Nonet, M.L.1    Young, R.A.2
  • 9
    • 0028282551 scopus 로고
    • A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II
    • Kim YJ, Björklund S, Li Y, Sayre MH, Kornberg RD (1994) A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II. Cell 77:599-608.
    • (1994) Cell , vol.77 , pp. 599-608
    • Kim, Y.J.1    Björklund, S.2    Li, Y.3    Sayre, M.H.4    Kornberg, R.D.5
  • 10
    • 0025347307 scopus 로고
    • Phosphorylation of RNA polymerase IIA occurs subsequent to interaction with the promoter and before the initiation of transcription
    • Laybourn PJ, Dahmus ME (1990) Phosphorylation of RNA polymerase IIA occurs subsequent to interaction with the promoter and before the initiation of transcription. J Biol Chem 265:13165-13173.
    • (1990) J Biol Chem , vol.265 , pp. 13165-13173
    • Laybourn, P.J.1    Dahmus, M.E.2
  • 11
    • 0034307008 scopus 로고    scopus 로고
    • Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription
    • Komarnitsky P, Cho EJ, Buratowski S (2000) Different phosphorylated forms of RNA polymerase II and associated mRNA processing factors during transcription. Genes Dev 14:2452-2460.
    • (2000) Genes Dev , vol.14 , pp. 2452-2460
    • Komarnitsky, P.1    Cho, E.J.2    Buratowski, S.3
  • 12
    • 0026348276 scopus 로고
    • CTD kinase associated with yeast RNA polymerase II initiation factor b
    • Feaver WJ, Gileadi O, Li Y, Kornberg RD (1991) CTD kinase associated with yeast RNA polymerase II initiation factor b. Cell 67:1223-1230.
    • (1991) Cell , vol.67 , pp. 1223-1230
    • Feaver, W.J.1    Gileadi, O.2    Li, Y.3    Kornberg, R.D.4
  • 13
    • 34347273423 scopus 로고    scopus 로고
    • Hyperphosphorylation of the C-terminal repeat domain of RNA polymerase II facilitates dissociation of its complex with mediator
    • Soøgaard TM, Svejstrup JQ, 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
    • Soøgaard, T.M.1    Svejstrup, J.Q.2    Svejstrup, J.Q.3
  • 14
    • 0030947346 scopus 로고    scopus 로고
    • Evidence for a mediator cycle at the initiation of transcription
    • Svejstrup JQ, et al. (1997) Evidence for a mediator cycle at the initiation of transcription. Proc Natl Acad Sci USA 94:6075-6078.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6075-6078
    • Svejstrup, J.Q.1
  • 15
    • 79960442655 scopus 로고    scopus 로고
    • Structural insights to how mammalian capping enzyme reads the CTD code
    • Ghosh A, Shuman S, Lima CD (2011) Structural insights to how mammalian capping enzyme reads the CTD code. Mol Cell 43:299-310.
    • (2011) Mol Cell , vol.43 , pp. 299-310
    • Ghosh, A.1    Shuman, S.2    Lima, C.D.3
  • 16
    • 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 JD (1996) A three-step pathway of transcription initiation leading to promoter clearance at an activation RNA polymerase II promoter. Mol Cell Biol 16:1614-1621.
    • (1996) Mol Cell Biol , vol.16 , pp. 1614-1621
    • Jiang, Y.1    Yan, M.2    Gralla, J.D.3
  • 17
    • 0842347413 scopus 로고    scopus 로고
    • Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex
    • Liu Y, et al. (2004) Two cyclin-dependent kinases promote RNA polymerase II transcription and formation of the scaffold complex. Mol Cell Biol 24:1721-1735.
    • (2004) Mol Cell Biol , vol.24 , pp. 1721-1735
    • Liu, Y.1
  • 18
    • 80555125095 scopus 로고    scopus 로고
    • RNAP II CTD phosphorylated on threonine-4 is required for histone mRNA 3′ end processing
    • Hsin JP, Sheth A, Manley JL (2011) RNAP II CTD phosphorylated on threonine-4 is required for histone mRNA 3′ end processing. Science 334:683-686.
    • (2011) Science , vol.334 , pp. 683-686
    • Hsin, J.P.1    Sheth, A.2    Manley, J.L.3
  • 19
    • 84862977456 scopus 로고    scopus 로고
    • CTD tyrosine phosphorylation impairs termination factor recruitment to RNA polymerase II
    • Mayer A, 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
  • 21
    • 0031881688 scopus 로고    scopus 로고
    • The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain
    • Myers LC, et al. (1998) The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain. Genes Dev 12:45-54.
    • (1998) Genes Dev , vol.12 , pp. 45-54
    • Myers, L.C.1
  • 22
    • 0035834772 scopus 로고    scopus 로고
    • The structural and functional organization of the yeast mediator complex
    • Kang JS, et al. (2001) The structural and functional organization of the yeast mediator complex. J Biol Chem 276:42003-42010.
    • (2001) J Biol Chem , vol.276 , pp. 42003-42010
    • Kang, J.S.1
  • 23
    • 79960434142 scopus 로고    scopus 로고
    • Architecture of the Mediator head module
    • Imasaki T, et al. (2011) Architecture of the Mediator head module. Nature 475:240-243.
    • (2011) Nature , vol.475 , pp. 240-243
    • Imasaki, T.1
  • 24
    • 76649135167 scopus 로고    scopus 로고
    • Finding chimeras: A bioinformatics strategy for identification of cross-linked peptides
    • Chu F, Baker PR, Burlingame AL, Chalkley RJ (2010) Finding chimeras: A bioinformatics strategy for identification of cross-linked peptides. Mol Cell Proteomics 9:25-31.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 25-31
    • Chu, F.1    Baker, P.R.2    Burlingame, A.L.3    Chalkley, R.J.4
  • 25
    • 53049102663 scopus 로고    scopus 로고
    • Snapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the carboxyl-terminal domain of RNA polymerase II
    • Becker R, Loll B, Meinhart A (2008) Snapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the carboxyl-terminal domain of RNA polymerase II. J Biol Chem 283:22659-22669.
    • (2008) J Biol Chem , vol.283 , pp. 22659-22669
    • Becker, R.1    Loll, B.2    Meinhart, A.3
  • 26
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine- proline recognition by group IV WW domains
    • Verdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP (2000) Structural basis for phosphoserine- proline recognition by group IV WW domains. Nat Struct Biol 7:639-643.
    • (2000) Nat Struct Biol , vol.7 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 27
    • 0038094496 scopus 로고    scopus 로고
    • Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II
    • Fabrega C, Shen V, Shuman S, Lima CD (2003) Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II. Mol Cell 11:1549-1561.
    • (2003) Mol Cell , vol.11 , pp. 1549-1561
    • Fabrega, C.1    Shen, V.2    Shuman, S.3    Lima, C.D.4
  • 28
    • 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
  • 29
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, et al. (1999) A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17:1030-1032.
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1
  • 30
    • 3242728442 scopus 로고    scopus 로고
    • A triad of subunits from the Gal11/tail domain of Srb mediator is an in vivo target of transcriptional activator Gcn4p
    • Zhang F, Sumibcay L, Hinnebusch AG, Swanson MJ (2004) A triad of subunits from the Gal11/tail domain of Srb mediator is an in vivo target of transcriptional activator Gcn4p. Mol Cell Biol 24:6871-6886.
    • (2004) Mol Cell Biol , vol.24 , pp. 6871-6886
    • Zhang, F.1    Sumibcay, L.2    Hinnebusch, A.G.3    Swanson, M.J.4
  • 31
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig O, et al. (2001) The tandem affinity purification (TAP) method: A general procedure of protein complex purification. Methods 24:218-229.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1
  • 32
    • 0026581236 scopus 로고
    • Isolation of two genes that encode subunits of the yeast transcription factor IIA
    • Ranish JA, Lane WS, Hahn S (1992) Isolation of two genes that encode subunits of the yeast transcription factor IIA. Science 255:1127-1129.
    • (1992) Science , vol.255 , pp. 1127-1129
    • Ranish, J.A.1    Lane, W.S.2    Hahn, S.3
  • 33
    • 74249102477 scopus 로고    scopus 로고
    • Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism
    • Liu X, Bushnell DA, Wang D, Calero G, Kornberg RD (2010) Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism. Science 327: 206-209.
    • (2010) Science , vol.327 , pp. 206-209
    • Liu, X.1    Bushnell, D.A.2    Wang, D.3    Calero, G.4    Kornberg, R.D.5
  • 34
    • 0035157217 scopus 로고    scopus 로고
    • Selenomethionine incorporation in Saccharomyces cerevisiae RNA polymerase II
    • Bushnell DA, Cramer P, Kornberg RD (2001) Selenomethionine incorporation in Saccharomyces cerevisiae RNA polymerase II. Structure 9:R11-R14.
    • (2001) Structure , vol.9
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 35
    • 0026452218 scopus 로고
    • Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae
    • Sayre MH, Tschochner H, Kornberg RD (1992) Reconstitution of transcription with five purified initiation factors and RNA polymerase II from Saccharomyces cerevisiae. J Biol Chem 267:23376-23382.
    • (1992) J Biol Chem , vol.267 , pp. 23376-23382
    • Sayre, M.H.1    Tschochner, H.2    Kornberg, R.D.3
  • 36
    • 33644852483 scopus 로고    scopus 로고
    • Mediator as a general transcription factor
    • Takagi Y, Kornberg RD (2006) Mediator as a general transcription factor. J Biol Chem 281:80-89.
    • (2006) J Biol Chem , vol.281 , pp. 80-89
    • Takagi, Y.1    Kornberg, R.D.2
  • 37
    • 77957975473 scopus 로고    scopus 로고
    • Topographic studies of the GroEL-GroES chaperonin complex by chemical cross-linking using diformyl ethynylbenzene: The power of high resolution electron transfer dissociation for determination of both peptide sequences and their attachment sites
    • Trnka MJ, Burlingame AL (2010) Topographic studies of the GroEL-GroES chaperonin complex by chemical cross-linking using diformyl ethynylbenzene: The power of high resolution electron transfer dissociation for determination of both peptide sequences and their attachment sites. Mol Cell Proteomics 9:2306-2317.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2306-2317
    • Trnka, M.J.1    Burlingame, A.L.2


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