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Volumn 1829, Issue 3-4, 2013, Pages 258-264

A structural perspective on RNA polymerase I and RNA polymerase III transcription machineries

Author keywords

Eukaryotic transcription; RNA polymerase I; RNA polymerase III; RRNAs; Structural biology; TRNAs

Indexed keywords

DNA DIRECTED RNA POLYMERASE; DNA DIRECTED RNA POLYMERASE III; MAF1 PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84875249328     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2012.09.009     Document Type: Review
Times cited : (21)

References (81)
  • 1
    • 0034652838 scopus 로고    scopus 로고
    • Survey and summary: transcription by RNA polymerases I and III
    • Paule M.R., White R.J. Survey and summary: transcription by RNA polymerases I and III. Nucleic Acids Res. 2000, 28:1283-1298.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1283-1298
    • Paule, M.R.1    White, R.J.2
  • 2
    • 0038506040 scopus 로고    scopus 로고
    • Life on a planet of its own: regulation of RNA polymerase I transcription in the nucleolus
    • Grummt I. Life on a planet of its own: regulation of RNA polymerase I transcription in the nucleolus. Genes Dev. 2003, 17:1691-1702.
    • (2003) Genes Dev. , vol.17 , pp. 1691-1702
    • Grummt, I.1
  • 3
    • 56649105133 scopus 로고    scopus 로고
    • RNA polymerases I and III, non-coding RNAs and cancer
    • White R.J. RNA polymerases I and III, non-coding RNAs and cancer. Trends Genet. 2008, 24:622-629.
    • (2008) Trends Genet. , vol.24 , pp. 622-629
    • White, R.J.1
  • 4
    • 42549130434 scopus 로고    scopus 로고
    • RNA metabolism and oncogenesis
    • Johnson D.L., Johnson S.A.S. RNA metabolism and oncogenesis. Science 2008, 320:461-462.
    • (2008) Science , vol.320 , pp. 461-462
    • Johnson, D.L.1    Johnson, S.A.S.2
  • 7
    • 79955035405 scopus 로고    scopus 로고
    • RNA polymerase III transcription in cancer: the BRF2 connection
    • Cabarcas S., Schramm L. RNA polymerase III transcription in cancer: the BRF2 connection. Mol. Cancer 2011, 10:47.
    • (2011) Mol. Cancer , vol.10 , pp. 47
    • Cabarcas, S.1    Schramm, L.2
  • 8
    • 77949495196 scopus 로고    scopus 로고
    • The RNA polymerase I transcription machinery: an emerging target for the treatment of cancer
    • Drygin D., Rice W.G., Grummt I. The RNA polymerase I transcription machinery: an emerging target for the treatment of cancer. Annu. Rev. Pharmacol. Toxicol. 2010, 50:131-156.
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 131-156
    • Drygin, D.1    Rice, W.G.2    Grummt, I.3
  • 9
    • 0014683539 scopus 로고
    • Multiple forms of DNA-dependent RNA polymerase in eukaryotic organisms
    • Roeder R.G., Rutter W.J. Multiple forms of DNA-dependent RNA polymerase in eukaryotic organisms. Nature 1969, 224:234-237.
    • (1969) Nature , vol.224 , pp. 234-237
    • Roeder, R.G.1    Rutter, W.J.2
  • 10
  • 11
    • 34548801789 scopus 로고    scopus 로고
    • The molecular basis of eukaryotic transcription
    • Kornberg R.D. The molecular basis of eukaryotic transcription. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:12955-12961.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 12955-12961
    • Kornberg, R.D.1
  • 13
    • 81255210794 scopus 로고    scopus 로고
    • Transcriptional regulation in Saccharomyces cerevisiae: transcription factor regulation and function, mechanisms of initiation, and roles of activators and coactivators
    • Hahn S., Young E.T. Transcriptional regulation in Saccharomyces cerevisiae: transcription factor regulation and function, mechanisms of initiation, and roles of activators and coactivators. Annu. Rev. Genet. 2011, 189:705-736.
    • (2011) Annu. Rev. Genet. , vol.189 , pp. 705-736
    • Hahn, S.1    Young, E.T.2
  • 14
    • 84862666457 scopus 로고    scopus 로고
    • A movie of RNA polymerase II transcription
    • Cheung A.C.M., Cramer P. A movie of RNA polymerase II transcription. Cell 2012, 149:1431-1437.
    • (2012) Cell , vol.149 , pp. 1431-1437
    • Cheung, A.C.M.1    Cramer, P.2
  • 15
    • 84857423235 scopus 로고    scopus 로고
    • Conservation between the RNA Polymerase I, II, and III transcription initiation machineries
    • Vannini A., Cramer P. Conservation between the RNA Polymerase I, II, and III transcription initiation machineries. Mol. Cell 2012, 45:439-446.
    • (2012) Mol. Cell , vol.45 , pp. 439-446
    • Vannini, A.1    Cramer, P.2
  • 21
    • 0027248774 scopus 로고
    • Three-dimensional model of yeast RNA polymerase I determined by electron microscopy of two-dimensional crystals
    • Schultz P., Célia H., Riva M., Sentenac A., Oudet P. Three-dimensional model of yeast RNA polymerase I determined by electron microscopy of two-dimensional crystals. EMBO J. 1993, 12:2601-2607.
    • (1993) EMBO J. , vol.12 , pp. 2601-2607
    • Schultz, P.1    Célia, H.2    Riva, M.3    Sentenac, A.4    Oudet, P.5
  • 23
    • 0037531306 scopus 로고    scopus 로고
    • Cryo-negative staining reveals conformational flexibility within yeast RNA polymerase I
    • De Carlo S., Carles C., Riva M., Schultz P. Cryo-negative staining reveals conformational flexibility within yeast RNA polymerase I. J. Mol. Biol. 2003, 329:891-902.
    • (2003) J. Mol. Biol. , vol.329 , pp. 891-902
    • De Carlo, S.1    Carles, C.2    Riva, M.3    Schultz, P.4
  • 24
    • 0036227539 scopus 로고    scopus 로고
    • Rpa12p, a conserved RNA polymerase I subunit with two functional domains
    • Van Mullem V., Landrieux E., Vandenhaute J., Thuriaux P. Rpa12p, a conserved RNA polymerase I subunit with two functional domains. Mol. Microbiol. 2002, 43:1105-1113.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1105-1113
    • Van Mullem, V.1    Landrieux, E.2    Vandenhaute, J.3    Thuriaux, P.4
  • 25
    • 79956308538 scopus 로고    scopus 로고
    • Evolution of two modes of intrinsic RNA polymerase transcript cleavage
    • Ruan W., Lehmann E., Thomm M., Kostrewa D., Cramer P. Evolution of two modes of intrinsic RNA polymerase transcript cleavage. J. Biol. Chem. 2011, 286:18701-18707.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18701-18707
    • Ruan, W.1    Lehmann, E.2    Thomm, M.3    Kostrewa, D.4    Cramer, P.5
  • 26
    • 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 2003, 114:347-357.
    • (2003) Cell , vol.114 , pp. 347-357
    • Kettenberger, H.1    Armache, K.-J.2    Cramer, P.3
  • 27
    • 0028567044 scopus 로고
    • The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II
    • Jeon C., Yoon H., Agarwal K. The transcription factor TFIIS zinc ribbon dipeptide Asp-Glu is critical for stimulation of elongation and RNA cleavage by RNA polymerase II. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:9106-9110.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9106-9110
    • Jeon, C.1    Yoon, H.2    Agarwal, K.3
  • 29
    • 0034653424 scopus 로고    scopus 로고
    • Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface
    • Okuda M., Watanabe Y., Okamura H., Hanaoka F., Ohkuma Y., Nishimura Y. Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface. EMBO J. 2000, 19:1346-1356.
    • (2000) EMBO J. , vol.19 , pp. 1346-1356
    • Okuda, M.1    Watanabe, Y.2    Okamura, H.3    Hanaoka, F.4    Ohkuma, Y.5    Nishimura, Y.6
  • 30
    • 84863194842 scopus 로고    scopus 로고
    • Crosslinking-MS analysis reveals RNA polymerase I domain architecture and basis of rRNA cleavage
    • Jennebach S., Herzog F., Aebersold R., Cramer P. Crosslinking-MS analysis reveals RNA polymerase I domain architecture and basis of rRNA cleavage. Nucleic Acids Res. 2012, 40:5591-5601.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 5591-5601
    • Jennebach, S.1    Herzog, F.2    Aebersold, R.3    Cramer, P.4
  • 31
    • 0032535546 scopus 로고    scopus 로고
    • The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination
    • Chédin S., Riva M., Schultz P., Sentenac A., Carles C. The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination. Genes Dev. 1998, 12:3857-3871.
    • (1998) Genes Dev. , vol.12 , pp. 3857-3871
    • Chédin, S.1    Riva, M.2    Schultz, P.3    Sentenac, A.4    Carles, C.5
  • 32
    • 33745499068 scopus 로고    scopus 로고
    • Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model
    • Jasiak A.J., Armache K.-J., Martens B., Jansen R.-P., Cramer P. Structural biology of RNA polymerase III: subcomplex C17/25 X-ray structure and 11 subunit enzyme model. Mol. Cell 2006, 23:71-81.
    • (2006) Mol. Cell , vol.23 , pp. 71-81
    • Jasiak, A.J.1    Armache, K.-J.2    Martens, B.3    Jansen, R.-P.4    Cramer, P.5
  • 33
    • 84860408300 scopus 로고    scopus 로고
    • Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA Polymerase III.
    • Ehara H., Sekine S.-i., Yokoyama S. Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA Polymerase III. Protein Sci. 2011, 20:1558-1565.
    • (2011) Protein Sci. , vol.20 , pp. 1558-1565
    • Ehara, H.1    Sekine, S.-I.2    Yokoyama, S.3
  • 35
    • 35148816658 scopus 로고    scopus 로고
    • Structural biology of RNA polymerase III: mass spectrometry elucidates subcomplex architecture
    • Lorenzen K., Vannini A., Cramer P., Heck A.J.R. Structural biology of RNA polymerase III: mass spectrometry elucidates subcomplex architecture. Structure 2007, 15:1237-1245.
    • (2007) Structure , vol.15 , pp. 1237-1245
    • Lorenzen, K.1    Vannini, A.2    Cramer, P.3    Heck, A.J.R.4
  • 37
    • 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. Nat. Struct. Mol. Biol. 2012, 19:788-796.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 788-796
    • Grünberg, S.1    Warfield, L.2    Hahn, S.3
  • 38
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding J., Biegert A., Lupas A.N. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 2005, 33:W244-W248.
    • (2005) Nucleic Acids Res. , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 39
    • 0037108150 scopus 로고    scopus 로고
    • Recruitment of RNA polymerase III to its target promoters
    • Schramm L., Hernandez N. Recruitment of RNA polymerase III to its target promoters. Genes Dev. 2002, 16:2593-2620.
    • (2002) Genes Dev. , vol.16 , pp. 2593-2620
    • Schramm, L.1    Hernandez, N.2
  • 40
    • 0035967858 scopus 로고    scopus 로고
    • The RNA polymerase III transcription apparatus
    • Geiduschek E.P., Kassavetis G.A. The RNA polymerase III transcription apparatus. J. Mol. Biol. 2001, 310:1-26.
    • (2001) J. Mol. Biol. , vol.310 , pp. 1-26
    • Geiduschek, E.P.1    Kassavetis, G.A.2
  • 41
    • 1942471135 scopus 로고    scopus 로고
    • At the crossroads of growth control; making ribosomal RNA
    • Moss T. At the crossroads of growth control; making ribosomal RNA. Curr. Opin. Genet. Dev. 2004, 14:210-217.
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 210-217
    • Moss, T.1
  • 42
    • 0028286488 scopus 로고
    • Short-range DNA looping by the Xenopus HMG-box transcription factor, xUBF
    • Bazett-Jones D.P., Leblanc B., Herfort M., Moss T. Short-range DNA looping by the Xenopus HMG-box transcription factor, xUBF. Science 1994, 264:1134-1137.
    • (1994) Science , vol.264 , pp. 1134-1137
    • Bazett-Jones, D.P.1    Leblanc, B.2    Herfort, M.3    Moss, T.4
  • 43
    • 0037197695 scopus 로고    scopus 로고
    • Solution structure of the first HMG box domain in human upstream binding factor
    • Xu Y., Yang W., Wu J., Shi Y. Solution structure of the first HMG box domain in human upstream binding factor. Biochemistry 2002, 41:5415-5420.
    • (2002) Biochemistry , vol.41 , pp. 5415-5420
    • Xu, Y.1    Yang, W.2    Wu, J.3    Shi, Y.4
  • 44
    • 0037465536 scopus 로고    scopus 로고
    • Solution structure and DNA binding property of the fifth HMG box domain in comparison with the first HMG box domain in human upstream binding factor
    • Yang W., Xu Y., Wu J., Zeng W., Shi Y. Solution structure and DNA binding property of the fifth HMG box domain in comparison with the first HMG box domain in human upstream binding factor. Biochemistry 2003, 42:1930-1938.
    • (2003) Biochemistry , vol.42 , pp. 1930-1938
    • Yang, W.1    Xu, Y.2    Wu, J.3    Zeng, W.4    Shi, Y.5
  • 46
    • 80052955293 scopus 로고    scopus 로고
    • Yeast Rrn7 and human TAF1B are TFIIB-related RNA polymerase I general transcription factors
    • Knutson B.A., Hahn S. Yeast Rrn7 and human TAF1B are TFIIB-related RNA polymerase I general transcription factors. Science 2011, 333:1637-1640.
    • (2011) Science , vol.333 , pp. 1637-1640
    • Knutson, B.A.1    Hahn, S.2
  • 48
    • 0028556519 scopus 로고
    • Assembly of transcriptionally active RNA polymerase I initiation factor SL1 from recombinant subunits
    • Zomerdijk J.C., Beckmann H., Comai L., Tjian R. Assembly of transcriptionally active RNA polymerase I initiation factor SL1 from recombinant subunits. Science 1994, 266:2015-2018.
    • (1994) Science , vol.266 , pp. 2015-2018
    • Zomerdijk, J.C.1    Beckmann, H.2    Comai, L.3    Tjian, R.4
  • 50
    • 80052954724 scopus 로고    scopus 로고
    • TAF1B is a TFIIB-like component of the basal transcription machinery for RNA polymerase I
    • Naidu S., Friedrich J.K., Russell J., Zomerdijk J.C.B.M. TAF1B is a TFIIB-like component of the basal transcription machinery for RNA polymerase I. Science 2011, 333:1640-1642.
    • (2011) Science , vol.333 , pp. 1640-1642
    • Naidu, S.1    Friedrich, J.K.2    Russell, J.3    Zomerdijk, J.C.B.M.4
  • 51
    • 0034712932 scopus 로고    scopus 로고
    • RNA polymerase I transcription factor Rrn3 is functionally conserved between yeast and human
    • Moorefield B., Greene E.A., Reeder R.H. RNA polymerase I transcription factor Rrn3 is functionally conserved between yeast and human. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:4724-4729.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4724-4729
    • Moorefield, B.1    Greene, E.A.2    Reeder, R.H.3
  • 52
    • 0034252226 scopus 로고    scopus 로고
    • TIF-IA, the factor mediating growth-dependent control of ribosomal RNA synthesis, is the mammalian homolog of yeast Rrn3p
    • Bodem J., Dobreva G., Hoffmann-Rohrer U., Iben S., Zentgraf H., Delius H., Vingron M., Grummt I. TIF-IA, the factor mediating growth-dependent control of ribosomal RNA synthesis, is the mammalian homolog of yeast Rrn3p. EMBO Rep. 2000, 1:171-175.
    • (2000) EMBO Rep. , vol.1 , pp. 171-175
    • Bodem, J.1    Dobreva, G.2    Hoffmann-Rohrer, U.3    Iben, S.4    Zentgraf, H.5    Delius, H.6    Vingron, M.7    Grummt, I.8
  • 53
    • 0034675857 scopus 로고    scopus 로고
    • The recruitment of RNA polymerase I on rDNA is mediated by the interaction of the A43 subunit with Rrn3
    • Peyroche G. The recruitment of RNA polymerase I on rDNA is mediated by the interaction of the A43 subunit with Rrn3. EMBO J. 2000, 19:5473-5482.
    • (2000) EMBO J. , vol.19 , pp. 5473-5482
    • Peyroche, G.1
  • 55
    • 46949087678 scopus 로고    scopus 로고
    • Mammalian Rrn3 is required for the formation of a transcription competent preinitiation complex containing RNA polymerase I
    • Cavanaugh A.H., Evans A., Rothblum L.I. Mammalian Rrn3 is required for the formation of a transcription competent preinitiation complex containing RNA polymerase I. Gene Expr. 2008, 14:131-147.
    • (2008) Gene Expr. , vol.14 , pp. 131-147
    • Cavanaugh, A.H.1    Evans, A.2    Rothblum, L.I.3
  • 56
    • 79959373574 scopus 로고    scopus 로고
    • Transcription by RNA polymerase III: more complex than we thought
    • White R.J. Transcription by RNA polymerase III: more complex than we thought. Nat. Rev. Genet. 2011, 12:459-463.
    • (2011) Nat. Rev. Genet. , vol.12 , pp. 459-463
    • White, R.J.1
  • 57
    • 79952254334 scopus 로고    scopus 로고
    • General transcription factors and subunits of RNA polymerase III: paralogs for promoter- and cell type-specific transcription in multicellular eukaryotes
    • Teichmann M., Dieci G., Pascali C., Boldina G. General transcription factors and subunits of RNA polymerase III: paralogs for promoter- and cell type-specific transcription in multicellular eukaryotes. Transcription 2010, 1:130-135.
    • (2010) Transcription , vol.1 , pp. 130-135
    • Teichmann, M.1    Dieci, G.2    Pascali, C.3    Boldina, G.4
  • 58
    • 0040215628 scopus 로고
    • Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes
    • Miller J., McLachlan A.D., Klug A. Repetitive zinc-binding domains in the protein transcription factor IIIA from Xenopus oocytes. EMBO J. 1985, 4:1609-1614.
    • (1985) EMBO J. , vol.4 , pp. 1609-1614
    • Miller, J.1    McLachlan, A.D.2    Klug, A.3
  • 59
    • 0010182724 scopus 로고
    • A specific transcription factor that can bind either the 5S RNA gene or 5S RNA
    • Pelham H.R., Brown D.D. A specific transcription factor that can bind either the 5S RNA gene or 5S RNA. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:4170-4174.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 4170-4174
    • Pelham, H.R.1    Brown, D.D.2
  • 60
    • 0032539846 scopus 로고    scopus 로고
    • Differing roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex
    • Nolte R.T., Conlin R.M., Harrison S.C., Brown R.S. Differing roles for zinc fingers in DNA recognition: structure of a six-finger transcription factor IIIA complex. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:2938-2943.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2938-2943
    • Nolte, R.T.1    Conlin, R.M.2    Harrison, S.C.3    Brown, R.S.4
  • 61
    • 0031576363 scopus 로고    scopus 로고
    • Solution structure of the first three zinc fingers of TFIIIA bound to the cognate DNA sequence: determinants of affinity and sequence specificity
    • Wuttke D.S., Foster M.P., Case D.A., Gottesfeld J.M., Wright P.E. Solution structure of the first three zinc fingers of TFIIIA bound to the cognate DNA sequence: determinants of affinity and sequence specificity. J. Mol. Biol. 1997, 273:183-206.
    • (1997) J. Mol. Biol. , vol.273 , pp. 183-206
    • Wuttke, D.S.1    Foster, M.P.2    Case, D.A.3    Gottesfeld, J.M.4    Wright, P.E.5
  • 62
    • 0242581682 scopus 로고    scopus 로고
    • Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition
    • Lu D., Alexandra Searles M., Klug A. Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition. Nat. Cell Biol. 2003, 426:96-100.
    • (2003) Nat. Cell Biol. , vol.426 , pp. 96-100
    • Lu, D.1    Alexandra Searles, M.2    Klug, A.3
  • 65
    • 84855838591 scopus 로고    scopus 로고
    • Extra-transcriptional functions of RNA Polymerase III complexes: TFIIIC as a potential global chromatin bookmark
    • Donze D. Extra-transcriptional functions of RNA Polymerase III complexes: TFIIIC as a potential global chromatin bookmark. Gene 2011, 493:169-175.
    • (2011) Gene , vol.493 , pp. 169-175
    • Donze, D.1
  • 66
    • 33750087881 scopus 로고    scopus 로고
    • Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly
    • Mylona A., Fernández-Tornero C., Legrand P., Haupt M., Sentenac A., Acker J., Müller C.W. Structure of the tau60/Delta tau91 subcomplex of yeast transcription factor IIIC: insights into preinitiation complex assembly. Mol. Cell 2006, 24:221-232.
    • (2006) Mol. Cell , vol.24 , pp. 221-232
    • Mylona, A.1    Fernández-Tornero, C.2    Legrand, P.3    Haupt, M.4    Sentenac, A.5    Acker, J.6    Müller, C.W.7
  • 67
    • 0036830540 scopus 로고    scopus 로고
    • Activator recruitment by the general transcription machinery: X-ray structural analysis of the Oct-1 POU domain/human U1 octamer/SNAP190 peptide ternary complex
    • Hovde S., Hinkley C.S., Strong K., Brooks A., Gu L., Henry R.W., Geiger J. Activator recruitment by the general transcription machinery: X-ray structural analysis of the Oct-1 POU domain/human U1 octamer/SNAP190 peptide ternary complex. Genes Dev. 2002, 16:2772-2777.
    • (2002) Genes Dev. , vol.16 , pp. 2772-2777
    • Hovde, S.1    Hinkley, C.S.2    Strong, K.3    Brooks, A.4    Gu, L.5    Henry, R.W.6    Geiger, J.7
  • 68
    • 34248675797 scopus 로고    scopus 로고
    • Transcription factor TFIIIB and transcription by RNA polymerase III
    • Kassavetis G.A., Geiduschek E.P. Transcription factor TFIIIB and transcription by RNA polymerase III. Biochem. Soc. Trans. 2006, 34:1082.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 1082
    • Kassavetis, G.A.1    Geiduschek, E.P.2
  • 69
    • 0242668442 scopus 로고    scopus 로고
    • Crystal structure of a transcription factor IIIB core interface ternary complex
    • Juo Z.S., Kassavetis G.A., Wang J., Geiduschek E.P., Sigler P.B. Crystal structure of a transcription factor IIIB core interface ternary complex. Nature 2003, 422:534-539.
    • (2003) Nature , vol.422 , pp. 534-539
    • Juo, Z.S.1    Kassavetis, G.A.2    Wang, J.3    Geiduschek, E.P.4    Sigler, P.B.5
  • 70
    • 27344446026 scopus 로고    scopus 로고
    • Reconfiguring the connectivity of a multiprotein complex: fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB
    • Kassavetis G.A., Soragni E., Driscoll R., Geiduschek E.P. Reconfiguring the connectivity of a multiprotein complex: fusions of yeast TATA-binding protein with Brf1, and the function of transcription factor IIIB. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:15406-15411.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15406-15411
    • Kassavetis, G.A.1    Soragni, E.2    Driscoll, R.3    Geiduschek, E.P.4
  • 71
    • 57649128298 scopus 로고    scopus 로고
    • Structural characterization of the interaction between TFIIIB components Bdp1 and Brf1
    • Saïda F. Structural characterization of the interaction between TFIIIB components Bdp1 and Brf1. Biochemistry 2008, 47:13197-13206.
    • (2008) Biochemistry , vol.47 , pp. 13197-13206
    • Saïda, F.1
  • 72
    • 77957005180 scopus 로고    scopus 로고
    • Cell growth- and differentiation-dependent regulation of RNA polymerase III transcription
    • Dumay-Odelot H., Durrieu-Gaillard S., Da Silva D., Roeder R.G., Teichmann M. Cell growth- and differentiation-dependent regulation of RNA polymerase III transcription. Cell Cycle 2010, 9:3687-3699.
    • (2010) Cell Cycle , vol.9 , pp. 3687-3699
    • Dumay-Odelot, H.1    Durrieu-Gaillard, S.2    Da Silva, D.3    Roeder, R.G.4    Teichmann, M.5
  • 73
    • 0031053040 scopus 로고    scopus 로고
    • Mutation in a new gene MAF1 affects tRNA suppressor efficiency in Saccharomyces cerevisiae
    • Boguta M., Czerska K., Zoladek T. Mutation in a new gene MAF1 affects tRNA suppressor efficiency in Saccharomyces cerevisiae. Gene 1997, 185:291-296.
    • (1997) Gene , vol.185 , pp. 291-296
    • Boguta, M.1    Czerska, K.2    Zoladek, T.3
  • 74
    • 77957658806 scopus 로고    scopus 로고
    • Maf1 regulation: a model of signal transduction inside the nucleus
    • (Austin, Tex.)
    • Wei Y., Zheng X.S. Maf1 regulation: a model of signal transduction inside the nucleus. Nucleus 2010, 1:162-165. (Austin, Tex.).
    • (2010) Nucleus , vol.1 , pp. 162-165
    • Wei, Y.1    Zheng, X.S.2
  • 75
    • 33744512096 scopus 로고    scopus 로고
    • General repression of RNA polymerase III transcription is triggered by protein phosphatase type 2A-mediated dephosphorylation of Maf1
    • Oficjalska-Pham D., Harismendy O., Smagowicz W.J., Gonzalez de Peredo A., Boguta M., Sentenac A., Lefebvre O. General repression of RNA polymerase III transcription is triggered by protein phosphatase type 2A-mediated dephosphorylation of Maf1. Mol. Cell 2006, 22:623-632.
    • (2006) Mol. Cell , vol.22 , pp. 623-632
    • Oficjalska-Pham, D.1    Harismendy, O.2    Smagowicz, W.J.3    Gonzalez de Peredo, A.4    Boguta, M.5    Sentenac, A.6    Lefebvre, O.7
  • 76
    • 33744515555 scopus 로고    scopus 로고
    • Dephosphorylation and genome-wide association of Maf1 with Pol III-transcribed genes during repression
    • Roberts D.N., Wilson B., Huff J.T., Stewart A.J., Cairns B.R. Dephosphorylation and genome-wide association of Maf1 with Pol III-transcribed genes during repression. Mol. Cell 2006, 22:633-644.
    • (2006) Mol. Cell , vol.22 , pp. 633-644
    • Roberts, D.N.1    Wilson, B.2    Huff, J.T.3    Stewart, A.J.4    Cairns, B.R.5
  • 77
    • 0742270606 scopus 로고    scopus 로고
    • Tor pathway regulates Rrn3p-dependent recruitment of yeast RNA polymerase I to the promoter but does not participate in alteration of the number of active genes
    • Claypool J.A., French S.L., Johzuka K., Eliason K., Vu L., Dodd J.A., Beyer A.L., Nomura M. Tor pathway regulates Rrn3p-dependent recruitment of yeast RNA polymerase I to the promoter but does not participate in alteration of the number of active genes. Mol. Biol. Cell 2004, 15:946-956.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 946-956
    • Claypool, J.A.1    French, S.L.2    Johzuka, K.3    Eliason, K.4    Vu, L.5    Dodd, J.A.6    Beyer, A.L.7    Nomura, M.8
  • 78
    • 1542343973 scopus 로고    scopus 로고
    • MTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability
    • Mayer C. mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability. Genes Dev. 2004, 18:423-434.
    • (2004) Genes Dev. , vol.18 , pp. 423-434
    • Mayer, C.1
  • 79
    • 84856405632 scopus 로고    scopus 로고
    • Drosophila RNA polymerase III repressor Maf1 controls body size and developmental timing by modulating tRNAiMet synthesis and systemic insulin signaling
    • Rideout E.J., Marshall L., Grewal S.S. Drosophila RNA polymerase III repressor Maf1 controls body size and developmental timing by modulating tRNAiMet synthesis and systemic insulin signaling. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:1139-1144.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 1139-1144
    • Rideout, E.J.1    Marshall, L.2    Grewal, S.S.3
  • 80
    • 84859900304 scopus 로고    scopus 로고
    • Nutrient/TOR-dependent regulation of RNA polymerase III controls tissue and organismal growth in Drosophila
    • Marshall L., Rideout E.J., Grewal S.S. Nutrient/TOR-dependent regulation of RNA polymerase III controls tissue and organismal growth in Drosophila. EMBO J. 2012, 31:1916-1930.
    • (2012) EMBO J. , vol.31 , pp. 1916-1930
    • Marshall, L.1    Rideout, E.J.2    Grewal, S.S.3
  • 81
    • 78149231296 scopus 로고    scopus 로고
    • Full repression of RNA polymerase III transcription requires interaction between two domains of its negative regulator Maf1
    • Gajda A., Towpik J., Steuerwald U., Müller C.W., Lefebvre O., Boguta M. Full repression of RNA polymerase III transcription requires interaction between two domains of its negative regulator Maf1. J. Biol. Chem. 2010, 285:35719-35727.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35719-35727
    • Gajda, A.1    Towpik, J.2    Steuerwald, U.3    Müller, C.W.4    Lefebvre, O.5    Boguta, M.6


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