메뉴 건너뛰기




Volumn 518, Issue 7539, 2015, Pages 376-380

Architecture of the RNA polymerase II-Mediator core initiation complex

Author keywords

[No Author keywords available]

Indexed keywords

MEDIATOR COMPLEX; RNA POLYMERASE II; TRANSCRIPTION FACTOR IIH; DNA; PROTEIN SUBUNIT; RPB4 PROTEIN, S CEREVISIAE; RPB7 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSCRIPTION FACTOR IIB;

EID: 84923358406     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14229     Document Type: Article
Times cited : (234)

References (87)
  • 1
    • 0024977414 scopus 로고
    • Five intermediate complexes in transcription initiation by RNA polymerase II
    • Buratowski, S., Hahn, S., Guarente, L. & Sharp, P. Five intermediate complexes in transcription initiation by RNA polymerase II. Cell 56, 549-561 (1989).
    • (1989) Cell , vol.56 , pp. 549-561
    • Buratowski, S.1    Hahn, S.2    Guarente, L.3    Sharp, P.4
  • 2
    • 81255210794 scopus 로고    scopus 로고
    • Transcriptional regulation in Saccharomyces cerevisiae: Transcription factor regulation and function, mechanismsof initiation, and roles of activators and coactivators
    • Hahn, S. & Young, E. T. Transcriptional regulation in Saccharomyces cerevisiae: transcription factor regulation and function, mechanismsof initiation, and roles of activators and coactivators. Genetics 189, 705-736 (2011).
    • (2011) Genetics , vol.189 , pp. 705-736
    • Hahn, S.1    Young, E.T.2
  • 3
    • 70450171352 scopus 로고    scopus 로고
    • RNA polymerase II-TFIIB structure and mechanism of transcription initiation
    • Kostrewa, D. et al. RNA polymerase II-TFIIB structure and mechanism of transcription initiation. Nature 462, 323-330 (2009).
    • (2009) Nature , vol.462 , pp. 323-330
    • Kostrewa, D.1
  • 4
    • 74249102477 scopus 로고    scopus 로고
    • Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism
    • Liu, X., Bushnell, D., Wang, D., Calero, G. & Kornberg, R. D. Structure of an RNA polymerase II-TFIIB complex and the transcription initiation mechanism. Science 327, 206-209 (2010).
    • (2010) Science , vol.327 , pp. 206-209
    • Liu, X.1    Bushnell, D.2    Wang, D.3    Calero, G.4    Kornberg, R.D.5
  • 5
    • 84864662191 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II preinitiation complex and mechanism of ATP-dependent promoter opening
    • Grünberg, S., Warfield, L. & Hahn, S. Architecture of the RNA polymerase II preinitiation complex and mechanism of ATP-dependent promoter opening. Nature Struct. Mol. Biol. 19, 788-796 (2012).
    • (2012) Nature Struct. Mol. Biol. , vol.19 , pp. 788-796
    • Grünberg, S.1    Warfield, L.2    Hahn, S.3
  • 6
    • 84872614213 scopus 로고    scopus 로고
    • Structure and function of the initially transcribing RNA polymerase II-TFIIB complex
    • Sainsbury, S., Niesser, J. & Cramer, P. Structure and function of the initially transcribing RNA polymerase II-TFIIB complex. Nature 493, 437-440 (2013).
    • (2013) Nature , vol.493 , pp. 437-440
    • Sainsbury, S.1    Niesser, J.2    Cramer, P.3
  • 7
    • 84875613843 scopus 로고    scopus 로고
    • Structural visualization of key steps in human transcription initiation
    • He, Y., Fang, J., Taatjes, D. & Nogales, E. Structural visualization of key steps in human transcription initiation. Nature 495, 481-486 (2013).
    • (2013) Nature , vol.495 , pp. 481-486
    • He, Y.1    Fang, J.2    Taatjes, D.3    Nogales, E.4
  • 8
    • 84884516365 scopus 로고    scopus 로고
    • Architecture of anRNApolymerase II transcriptionpre-initiation complex
    • Murakami, K. et al. Architecture of anRNApolymerase II transcriptionpre-initiation complex. Science 342, 1238724 (2013).
    • (2013) Science , vol.342 , pp. 1238724
    • Murakami, K.1
  • 9
    • 84904346675 scopus 로고    scopus 로고
    • Conserved architecture of the core RNA polymerase II initation complex
    • Mü hlbacher, W. et al. Conserved architecture of the core RNA polymerase II initation complex. Nature Commun. 5, 4310 (2014).
    • (2014) Nature Commun. , vol.5 , pp. 4310
    • Mü Hlbacher, W.1
  • 10
    • 80455164640 scopus 로고    scopus 로고
    • Origins and activity of the Mediator complex
    • Conaway, R. C. & Conaway, J. Origins and activity of the Mediator complex. Semin. Cell Dev. Biol. 22, 729-734 (2011).
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 729-734
    • Conaway, R.C.1    Conaway, J.2
  • 11
    • 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., Søgaard, M. & Svejstrup, J. Q. 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).
    • (2007) J. Biol. Chem. , vol.282 , pp. 14113-14120
    • Max, T.1    Søgaard, M.2    Svejstrup, J.Q.3
  • 13
    • 79960434142 scopus 로고    scopus 로고
    • Architecture of the Mediator head module
    • Imasaki, T. et al. Architecture of the Mediator head module. Nature 475, 240-243 (2011).
    • (2011) Nature , vol.475 , pp. 240-243
    • Imasaki, T.1
  • 14
    • 84871456902 scopus 로고    scopus 로고
    • Structure of the Mediator head module
    • Larivière, L. et al. Structure of the Mediator head module. Nature 492, 448-451 (2012).
    • (2012) Nature , vol.492 , pp. 448-451
    • Larivière, L.1
  • 15
    • 84868094446 scopus 로고    scopus 로고
    • Structure of the mediator head module bound to the carboxy-terminal domain of RNA polymerase II
    • Robinson, P. J., Bushnell, D., Trnka, M., Burlingame, A. & Kornberg, R. Structure of the mediator head module bound to the carboxy-terminal domain of RNA polymerase II. Proc. Natl Acad. Sci. USA 109, 17931-17935 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 17931-17935
    • Robinson, P.J.1    Bushnell, D.2    Trnka, M.3    Burlingame, A.4    Kornberg, R.5
  • 16
    • 84903816704 scopus 로고    scopus 로고
    • Redefining the modular organization of the core Mediator complex
    • Wang, X. et al. Redefining the modular organization of the core Mediator complex. Cell Res. 24, 796-808 (2014).
    • (2014) Cell Res. , vol.24 , pp. 796-808
    • Wang, X.1
  • 17
    • 84902186552 scopus 로고    scopus 로고
    • Subunit architecture and functional modular rearrangements of the transcriptional mediator complex
    • Tsai, K.-L. et al. Subunit architecture and functional modular rearrangements of the transcriptional mediator complex. Cell 157, 1430-1444 (2014).
    • (2014) Cell , vol.157 , pp. 1430-1444
    • Tsai, K.-L.1
  • 18
  • 19
    • 0036671095 scopus 로고    scopus 로고
    • Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction
    • Davis, J. A., Takagi, Y., Kornberg, R. & Asturias, F. Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction. Mol. Cell 10, 409-415 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 409-415
    • Davis, J.A.1    Takagi, Y.2    Kornberg, R.3    Asturias, F.4
  • 20
    • 33750481873 scopus 로고    scopus 로고
    • The cyclin-dependent kinase 8module sterically blocksMediator interactions with RNA polymerase II
    • Elmlund, H. et al. The cyclin-dependent kinase 8module sterically blocksMediator interactions with RNA polymerase II. Proc. Natl Acad. Sci. USA 103, 15788-15793 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 15788-15793
    • Elmlund, H.1
  • 21
    • 79953713243 scopus 로고    scopus 로고
    • Molecular architecture of the human Mediator-RNA polymerase II-TFIIF assembly
    • Bernecky, C., Grob, P., Ebmeier, C., Nogales, E. & Taatjes, D. Molecular architecture of the human Mediator-RNA polymerase II-TFIIF assembly. PLoS Biol. 9, e1000603 (2011).
    • (2011) PLoS Biol. , vol.9 , pp. e1000603
    • Bernecky, C.1    Grob, P.2    Ebmeier, C.3    Nogales, E.4    Taatjes, D.5
  • 22
    • 85027942059 scopus 로고    scopus 로고
    • A conserved Mediator-CDK8 kinase module association regulates Mediator-RNA polymerase II interaction
    • Tsai, K.-L. et al. A conserved Mediator-CDK8 kinase module association regulates Mediator-RNA polymerase II interaction. Nature Struct. Mol. Biol. 20, 611-619 (2013).
    • (2013) Nature Struct. Mol. Biol. , vol.20 , pp. 611-619
    • Tsai, K.-L.1
  • 23
    • 0035831475 scopus 로고    scopus 로고
    • Yeast nuclear extract contains twomajor forms of RNA polymerase II mediator complexes
    • Liu, Y., Ranish, J., Aebersold, R.& Hahn, S. Yeast nuclear extract contains twomajor forms of RNA polymerase II mediator complexes. J. Biol. Chem. 276, 7169-7175 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 7169-7175
    • Liu, Y.1    Ranish, J.2    Aebersold, R.3    Hahn, S.4
  • 24
    • 84923319299 scopus 로고    scopus 로고
    • Reconstitution of active humancoreMediator complex reveals a critical role of the MED14 subunit
    • Cevher, M. A. et al. Reconstitution of active humancoreMediator complex reveals a critical role of the MED14 subunit. Nature Struct. Mol. Biol. 21, 1028-1034 (2014).
    • (2014) Nature Struct. Mol. Biol. , vol.21 , pp. 1028-1034
    • Cevher, M.A.1
  • 25
    • 84890062562 scopus 로고    scopus 로고
    • Model of the Mediator middle module based on protein crosslinking
    • Larivière, L. et al. Model of the Mediator middle module based on protein crosslinking. Nucleic Acids Res. 41, 9266-9273 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. 9266-9273
    • Larivière, L.1
  • 26
    • 0001603028 scopus 로고    scopus 로고
    • An activator binding module of yeast RNA polymerase II holoenzyme
    • Lee, Y. C., Park, J., Min, S., Han, S. & Kim, Y. An activator binding module of yeast RNA polymerase II holoenzyme. Mol. Cell. Biol. 19, 2967-2976 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2967-2976
    • Lee, Y.C.1    Park, J.2    Min, S.3    Han, S.4    Kim, Y.5
  • 27
    • 47249134314 scopus 로고    scopus 로고
    • Comparative genomics supports a deep evolutionary origin for the large, four-module transcriptional mediator complex
    • Bourbon, H.-M. Comparative genomics supports a deep evolutionary origin for the large, four-module transcriptional mediator complex. Nucleic Acids Res. 36, 3993-4008 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3993-4008
    • Bourbon, H.-M.1
  • 28
    • 77149124577 scopus 로고    scopus 로고
    • Position of the general transcription factor TFIIF within the RNA polymerase II transcription preinitiation complex
    • Eichner, J., Chen, H.-T., Warfield, L. & Hahn, S. Position of the general transcription factor TFIIF within the RNA polymerase II transcription preinitiation complex. EMBO J. 29, 706-716 (2010).
    • (2010) EMBO J. , vol.29 , pp. 706-716
    • Eichner, J.1    Chen, H.-T.2    Warfield, L.3    Hahn, S.4
  • 29
    • 84869862306 scopus 로고    scopus 로고
    • Structural basis of transcription initiation
    • Zhang, Y. et al. Structural basis of transcription initiation. Science 338, 1076-1080 (2012).
    • (2012) Science , vol.338 , pp. 1076-1080
    • Zhang, Y.1
  • 30
    • 77149146167 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry
    • Chen, Z. A. et al. Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry. EMBO J. 29, 717-726 (2010).
    • (2010) EMBO J. , vol.29 , pp. 717-726
    • Chen, Z.A.1
  • 31
    • 84856781205 scopus 로고    scopus 로고
    • Architecture of the yeast RNA polymerase II open complex and regulation of activity by TFIIF
    • Fishburn, J. & Hahn, S. Architecture of the yeast RNA polymerase II open complex and regulation of activity by TFIIF. Mol. Cell. Biol. 32, 12-25 (2012).
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 12-25
    • Fishburn, J.1    Hahn, S.2
  • 32
    • 33749514827 scopus 로고    scopus 로고
    • Structure and TBP binding of the Mediator head subcomplex Med8-Med18-Med20
    • Larivière, L. et al. Structure and TBP binding of the Mediator head subcomplex Med8-Med18-Med20. Nature Struct. Mol. Biol. 13, 895-901 (2006).
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 895-901
    • Larivière, L.1
  • 33
    • 58149351376 scopus 로고    scopus 로고
    • Identification, structure, and functional requirement of the Mediator submodule Med7N/31
    • Koschubs, T. et al. Identification, structure, and functional requirement of the Mediator submodule Med7N/31. EMBO J. 28, 69-80 (2009).
    • (2009) EMBO J. , vol.28 , pp. 69-80
    • Koschubs, T.1
  • 34
    • 0025962218 scopus 로고
    • Two dissociable subunits of yeast RNApolymerase II stimulate the initiation of transcription at a promoter in vitro
    • Edwards, A. M., Kane, C. M., Young, R. A. & Kornberg, R. D.Two dissociable subunits of yeast RNApolymerase II stimulate the initiation of transcription at a promoter in vitro. J. Biol. Chem. 266, 71-75 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 71-75
    • Edwards, A.M.1    Kane, C.M.2    Young, R.A.3    Kornberg, R.D.4
  • 35
    • 33744948144 scopus 로고    scopus 로고
    • Human Mediator enhances basal transcription by facilitating recruitment of transcription factor IIB during preinitiation complex assembly
    • Baek, H. J., Kang, Y.& Roeder, R. Human Mediator enhances basal transcription by facilitating recruitment of transcription factor IIB during preinitiation complex assembly. J. Biol. Chem. 281, 15172-15181 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 15172-15181
    • Baek, H.J.1    Kang, Y.2    Roeder, R.3
  • 36
    • 0032900980 scopus 로고    scopus 로고
    • Intermediates in formationandactivity of the RNA polymerase II preinitiation complex: Holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB
    • Ranish, J. A., Yudkovsky, N. & Hahn, S. Intermediates in formationandactivity of the RNA polymerase II preinitiation complex: holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB. Genes Dev. 13, 49-63 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 49-63
    • Ranish, J.A.1    Yudkovsky, N.2    Hahn, S.3
  • 37
    • 0027253864 scopus 로고
    • A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast
    • Thompson, C. M., Koleske, A., Chao, D. & Young, R. A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast. Cell 73, 1361-1375 (1993).
    • (1993) Cell , vol.73 , pp. 1361-1375
    • Thompson, C.M.1    Koleske, A.2    Chao, D.3    Young, R.4
  • 38
    • 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. Direct interaction of RNA polymerase II and mediator required for transcription in vivo. Science 331, 1451-1454 (2011).
    • (2011) Science , vol.331 , pp. 1451-1454
    • Soutourina, J.1    Wydau, S.2    Ambroise, Y.3    Boschiero, C.4    Werner, M.5
  • 39
    • 0024354605 scopus 로고
    • Intragenic and extragenic suppressors ofmutations in the heptapeptide repeat domain of Saccharomyces cerevisiae RNA polymerase II
    • Nonet, M. L.& Young, R. Intragenic and extragenic suppressors ofmutations in the heptapeptide repeat domain of Saccharomyces cerevisiae RNA polymerase II. Genetics 123, 715-724 (1989).
    • (1989) Genetics , vol.123 , pp. 715-724
    • Nonet, M.L.1    Young, R.2
  • 40
    • 14844290215 scopus 로고    scopus 로고
    • Structures of complete RNA polymerase II and its subcomplex Rpb4/7
    • Armache, K. J., Mitterweger, S., Meinhart, A. & Cramer, P. Structures of complete RNA polymerase II and its subcomplex, Rpb4/7. J. Biol. Chem. 280, 7131-7134 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 7131-7134
    • Armache, K.J.1    Mitterweger, S.2    Meinhart, A.3    Cramer, P.4
  • 41
    • 33748753071 scopus 로고    scopus 로고
    • The classical srb4-138 mutant allele causes dissociation of yeast Mediator
    • Linder, T., Zhu, X., Baraznenok, V. & Gustafsson, C. The classical srb4-138 mutant allele causes dissociation of yeast Mediator. Biochem. Biophys. Res. Commun. 349, 948-953 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 948-953
    • Linder, T.1    Zhu, X.2    Baraznenok, V.3    Gustafsson, C.4
  • 42
    • 33644852483 scopus 로고    scopus 로고
    • Mediator as a general transcription factor
    • Takagi, Y. & Kornberg, R. D.Mediator as a general transcription factor. J. Biol. Chem. 281, 80-89 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 80-89
    • Takagi, Y.1    Kornberg, R.D.2
  • 43
    • 33746408090 scopus 로고    scopus 로고
    • Head module control of mediator interactions
    • Takagi, Y. et al. Head module control of mediator interactions. Mol. Cell 23, 355-364 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 355-364
    • Takagi, Y.1
  • 44
    • 84863540819 scopus 로고    scopus 로고
    • Comparative dynamic transcriptome analysis (cDTA) reveals mutual feedback between mRNA synthesis and degradation
    • Sun, M. et al. Comparative dynamic transcriptome analysis (cDTA) reveals mutual feedback between mRNA synthesis and degradation. Genome Res. 22, 1350-1359 (2012).
    • (2012) Genome Res. , vol.22 , pp. 1350-1359
    • Sun, M.1
  • 45
    • 84903471633 scopus 로고    scopus 로고
    • Rpb4 subunit functions mainly in mRNA synthesis by RNA polymerase II
    • Schulz, D., Pirkl, N., Lehmann, E. & Cramer, P. Rpb4 subunit functions mainly in mRNA synthesis by RNA polymerase II. J. Biol. Chem. 289, 17446-17452 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 17446-17452
    • Schulz, D.1    Pirkl, N.2    Lehmann, E.3    Cramer, P.4
  • 46
    • 84886948058 scopus 로고    scopus 로고
    • RNA polymerase i structure and transcription regulation
    • Engel, C., Sainsbury, S., Cheung, A., Kostrewa, D. & Cramer, P. RNA polymerase I structure and transcription regulation. Nature 502, 650-655 (2013).
    • (2013) Nature , vol.502 , pp. 650-655
    • Engel, C.1    Sainsbury, S.2    Cheung, A.3    Kostrewa, D.4    Cramer, P.5
  • 47
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer, P., Bushnell, D. & Kornberg, R. Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292, 1863-1876 (2001).
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.2    Kornberg, R.3
  • 48
    • 0043244876 scopus 로고    scopus 로고
    • Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage
    • Kettenberger, H., Armache, K.-J. & Cramer, P. Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage. Cell 114, 347-357 (2003).
    • (2003) Cell , vol.114 , pp. 347-357
    • Kettenberger, H.1    Armache, K.-J.2    Cramer, P.3
  • 49
    • 84871700533 scopus 로고    scopus 로고
    • Mediator-regulated transcription through the 11 nucleosome
    • Nock, A., Ascano, J., Barrero, M. & Malik, S. Mediator-regulated transcription through the 11 nucleosome. Mol. Cell 48, 837-848 (2012).
    • (2012) Mol. Cell , vol.48 , pp. 837-848
    • Nock, A.1    Ascano, J.2    Barrero, M.3    Malik, S.4
  • 50
    • 48349095490 scopus 로고    scopus 로고
    • Mediator-dependent recruitment of TFIIHmodules in preinitiation complex
    • Esnault, C. et al. Mediator-dependent recruitment of TFIIHmodules in preinitiation complex. Mol. Cell 31, 337-346 (2008).
    • (2008) Mol. Cell , vol.31 , pp. 337-346
    • Esnault, C.1
  • 51
    • 0028826925 scopus 로고
    • Yeast global transcriptional regulators Sin4 andRgr1 are components of mediator complex/RNA polymerase II holoenzyme
    • Li, Y. et al. Yeast global transcriptional regulators Sin4 andRgr1 are components of mediator complex/RNA polymerase II holoenzyme. Proc. Natl Acad. Sci. USA 92, 10864-10868 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10864-10868
    • Li, Y.1
  • 52
    • 24044470632 scopus 로고    scopus 로고
    • A conserved mediator hinge revealed in the structure of the MED7.MED21 (Med7.Srb7) heterodimer
    • Baumli, S., Hoeppner, S. & Cramer, P. A conserved mediator hinge revealed in the structure of the MED7.MED21 (Med7.Srb7) heterodimer. J. Biol. Chem. 280, 18171-18178 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 18171-18178
    • Baumli, S.1    Hoeppner, S.2    Cramer, P.3
  • 53
    • 80051729454 scopus 로고    scopus 로고
    • Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcriptioninitiationcomplex stabilization
    • Seizl, M., Larivière, L., Pfaffeneder, T., Wenzeck, L. & Cramer, P. Mediator head subcomplex Med11/22 contains a common helix bundle building block with a specific function in transcriptioninitiationcomplex stabilization.Nucleic Acids Res. 39, 6291-6304 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 6291-6304
    • Seizl, M.1    Larivière, L.2    Pfaffeneder, T.3    Wenzeck, L.4    Cramer, P.5
  • 54
    • 0842304212 scopus 로고    scopus 로고
    • RNA polymerase II (Pol II)-TFIIF and Pol II-mediator complexes: The major stable Pol II complexes and their activity in transcription initiation and reinitiation
    • Rani, P. G., Ranish, J. & Hahn, S.RNA polymerase II (Pol II)-TFIIF and Pol II-mediator complexes: the major stable Pol II complexes and their activity in transcription initiation and reinitiation. Mol. Cell. Biol. 24, 1709-1720 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1709-1720
    • Rani, P.G.1    Ranish, J.2    Hahn, S.3
  • 55
    • 67449116330 scopus 로고    scopus 로고
    • Structural basis of transcription: Mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA
    • Sydow, J. F. et al. Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA. Mol. Cell 34, 710-721 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 710-721
    • Sydow, J.F.1
  • 56
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATAbox complex
    • Kim, Y., Geiger, J. H., Hahn, S. & Sigler, P. B. Crystal structure of a yeast TBP/TATAbox complex. Nature 365, 512-520 (1993).
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 57
    • 34547683177 scopus 로고    scopus 로고
    • The positions of TFIIF and TFIIE in the RNA polymerase II transcription preinitiation complex
    • Chen, H.-T., Warfield, L. & Hahn, S. The positions of TFIIF and TFIIE in the RNA polymerase II transcription preinitiation complex. Nature Struct. Mol. Biol. 14, 696-703 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 696-703
    • Chen, H.-T.1    Warfield, L.2    Hahn, S.3
  • 58
    • 0346515712 scopus 로고    scopus 로고
    • Assays and affinity purification of biotinylated and nonbiotinylated forms of double-tagged core RNA polymerase II from Saccharomyces cerevisiae
    • Kireeva, M. L., Lubkowska, L., Komissarova, N. & Kashlev, M. Assays and affinity purification of biotinylated and nonbiotinylated forms of double-tagged core RNA polymerase II from Saccharomyces cerevisiae. Methods Enzymol. 370, 138-155 (2003).
    • (2003) Methods Enzymol. , vol.370 , pp. 138-155
    • Kireeva, M.L.1    Lubkowska, L.2    Komissarova, N.3    Kashlev, M.4
  • 59
    • 77955381399 scopus 로고    scopus 로고
    • Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics
    • Leitner, A. et al. Probing native protein structures by chemical cross-linking, mass spectrometry, and bioinformatics. Mol. Cell. Proteomics 9, 1634-1649 (2010).
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1634-1649
    • Leitner, A.1
  • 60
    • 84866095385 scopus 로고    scopus 로고
    • Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry
    • Herzog, F. et al. Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry. Science 337, 1348-1352 (2012).
    • (2012) Science , vol.337 , pp. 1348-1352
    • Herzog, F.1
  • 61
    • 84891714984 scopus 로고    scopus 로고
    • Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline
    • Leitner, A., Walzthoeni, T. & Aebersold, R. Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline. Nature Protocols 9, 120-137 (2014).
    • (2014) Nature Protocols , vol.9 , pp. 120-137
    • Leitner, A.1    Walzthoeni, T.2    Aebersold, R.3
  • 62
    • 77249179311 scopus 로고    scopus 로고
    • ICC-CLASS: Isotopically-coded cleavable crosslinking analysis software suite
    • Petrotchenko, E. V. & Borchers, C. ICC-CLASS: isotopically-coded cleavable crosslinking analysis software suite. BMC Bioinformatics 11, 64 (2010).
    • (2010) BMC Bioinformatics , vol.11 , pp. 64
    • Petrotchenko, E.V.1    Borchers, C.2
  • 63
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36-51 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 64
    • 79960898027 scopus 로고    scopus 로고
    • Computer controlled cryo-electron microscopy-TOM2 a software package for high-throughput applications
    • Korinek, A., Beck, F., Baumeister, W., Nickell, S.& Plitzko, J. M. Computer controlled cryo-electron microscopy-TOM2 a software package for high-throughput applications. J. Struct. Biol. 175, 394-405 (2011).
    • (2011) J. Struct. Biol. , vol.175 , pp. 394-405
    • Korinek, A.1    Beck, F.2    Baumeister, W.3    Nickell, S.4    Plitzko, J.M.5
  • 65
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable nearatomic-resolution single-particle cryo-EM. Nature Methods 10, 584-590 (2013).
    • (2013) Nature Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 66
    • 84868496402 scopus 로고    scopus 로고
    • Unraveling the structure ofmembrane proteins in situ by transfer function corrected cryo-electron tomography
    • Eibauer, M. et al. Unraveling the structure ofmembrane proteins in situ by transfer function corrected cryo-electron tomography. J. Struct. Biol.180, 488-496 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 488-496
    • Eibauer, M.1
  • 67
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 69
    • 84860584901 scopus 로고    scopus 로고
    • PyTom: A python-based toolbox for localization of macromolecules in cryo-electron tomograms and subtomogram analysis
    • Hrabe, T. et al. PyTom: a python-based toolbox for localization of macromolecules in cryo-electron tomograms and subtomogram analysis. J. Struct. Biol. 178, 177-188 (2012).
    • (2012) J. Struct. Biol. , vol.178 , pp. 177-188
    • Hrabe, T.1
  • 70
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 71
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh, T. R. et al. SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nature Protocols 3, 1941-1974 (2008).
    • (2008) Nature Protocols , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1
  • 72
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determinationof local defocus and specimen tilt in electron microscopy
    • Mindell, J. A. & Grigorieff, N. Accurate determinationof local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 73
    • 84887242753 scopus 로고    scopus 로고
    • One number does not fit all: Mapping local variations in resolution in cryo-EM reconstructions
    • Cardone, G., Heymann, J. B. & Steven, A. C. One number does not fit all: mapping local variations in resolution in cryo-EM reconstructions. J. Struct. Biol. 184, 226-236 (2013).
    • (2013) J. Struct. Biol. , vol.184 , pp. 226-236
    • Cardone, G.1    Heymann, J.B.2    Steven, A.C.3
  • 74
    • 33644847296 scopus 로고    scopus 로고
    • Estimation of variance in singleparticle reconstruction using the bootstrap technique
    • Penczek, P. A., Yang, C., Frank, J. & Spahn, C. M. T. Estimation of variance in singleparticle reconstruction using the bootstrap technique. J. Struct. Biol.154,168-183 (2006).
    • (2006) J. Struct. Biol. , vol.154 , pp. 168-183
    • Penczek, P.A.1    Yang, C.2    Frank, J.3    Spahn, C.M.T.4
  • 75
    • 2042540051 scopus 로고    scopus 로고
    • Gridding-based direct Fourier inversion of the three-dimensional ray transform
    • Penczek, P. A., Renka, R. & Schomberg, H. Gridding-based direct Fourier inversion of the three-dimensional ray transform. J. Opt. Soc. Am. A 21, 499-509 (2004).
    • (2004) J. Opt. Soc. Am. A , vol.21 , pp. 499-509
    • Penczek, P.A.1    Renka, R.2    Schomberg, H.3
  • 76
    • 77955358961 scopus 로고    scopus 로고
    • Using Situs for the integration ofmulti-resolution structures
    • Wriggers, W. Using Situs for the integration ofmulti-resolution structures. Biophys. Rev. 2, 21-27 (2010).
    • (2010) Biophys. Rev. , vol.2 , pp. 21-27
    • Wriggers, W.1
  • 77
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera- A visualization system for exploratory research and analysis
    • Pettersen, E. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.1
  • 78
    • 82455199223 scopus 로고    scopus 로고
    • Structural basis of initial RNA polymerase II transcription
    • Cheung, A. C. M., Sainsbury, S. & Cramer, P. Structural basis of initial RNA polymerase II transcription. EMBO J. 30, 4755-4763 (2011).
    • (2011) EMBO J. , vol.30 , pp. 4755-4763
    • Cheung, A.C.M.1    Sainsbury, S.2    Cramer, P.3
  • 79
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 80
    • 27344436659 scopus 로고    scopus 로고
    • Scalable molecular dynamics with NAMD
    • Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781-1802 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1781-1802
    • Phillips, J.C.1
  • 81
    • 84986512474 scopus 로고
    • CHARMM: A programformacromolecular energy, minimization, and dynamics calculations
    • Brooks, B. R. et al.CHARMM: a programformacromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217 (1983).
    • (1983) J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1
  • 82
    • 43749107283 scopus 로고    scopus 로고
    • Comparative protein structure modeling using Modeller
    • Eswar, N. et al. Comparative protein structure modeling using Modeller. Curr. Protocols Bioinf. 5, 5.6.1-5.6.30 (2006).
    • (2006) Curr. Protocols Bioinf. , vol.5 , pp. 561-5630
    • Eswar, N.1
  • 83
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 84
    • 84885359411 scopus 로고    scopus 로고
    • Global analysis of eukaryotic mRNA degradation reveals Xrn1-dependent buffering of transcript levels
    • Sun, M. et al. Global analysis of eukaryotic mRNA degradation reveals Xrn1-dependent buffering of transcript levels. Mol. Cell 52, 52-62 (2013).
    • (2013) Mol. Cell , vol.52 , pp. 52-62
    • Sun, M.1
  • 85
    • 64049097892 scopus 로고    scopus 로고
    • Mediator structural conservation and implications for the regulation mechanism
    • Cai, G., Imasaki, T., Takagi, Y. & Asturias, F. J. Mediator structural conservation and implications for the regulation mechanism. Structure 17, 559-567 (2009).
    • (2009) Structure , vol.17 , pp. 559-567
    • Cai, G.1    Imasaki, T.2    Takagi, Y.3    Asturias, F.J.4
  • 86
    • 84861082442 scopus 로고    scopus 로고
    • Interaction of the mediator head module with RNA polymerase II
    • Cai, G. et al. Interaction of the mediator head module with RNA polymerase II. Structure 20, 899-910 (2012).
    • (2012) Structure , vol.20 , pp. 899-910
    • Cai, G.1
  • 87
    • 77953713807 scopus 로고    scopus 로고
    • Preparation and topology of the Mediator middle module
    • Koschubs, T. et al. Preparation and topology of the Mediator middle module. Nucleic Acids Res. 38, 3186-3195 (2010).
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3186-3195
    • Koschubs, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.