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Volumn 95, Issue 4, 2013, Pages 680-691

Structural bioinformatics of the general transcription factor TFIID

Author keywords

Homology modeling; TAF; TFIID; Transcription factor

Indexed keywords

DIMER; HISTONE; M1 AMINOPEPTIDASE PROTEIN; RNA POLYMERASE II; TAF2 PROTEIN; TAF3 PROTEIN; TAF4 PROTEIN; TATA BINDING PROTEIN; TATA BINDING PROTEIN ASSOCIATED FACTOR; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR IID; UNCLASSIFIED DRUG;

EID: 84874663459     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.10.024     Document Type: Review
Times cited : (20)

References (113)
  • 1
    • 0031579666 scopus 로고    scopus 로고
    • Transcription initiation from TATA-less promoters within eukaryotic protein-coding genes
    • S.T. Smale Transcription initiation from TATA-less promoters within eukaryotic protein-coding genes Biochim. Biophys. Acta 1351 1997 73 88
    • (1997) Biochim. Biophys. Acta , vol.1351 , pp. 73-88
    • Smale, S.T.1
  • 2
    • 0027255450 scopus 로고
    • Transcription factor TFIID recognizes DNA sequences downstream of the TATA element in the Hsp70 heat shock gene
    • P.A. Emanuel, and D.S. Gilmour Transcription factor TFIID recognizes DNA sequences downstream of the TATA element in the Hsp70 heat shock gene Proc. Natl. Acad. Sci. U.S.A. 90 1993 8449 8453
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 8449-8453
    • Emanuel, P.A.1    Gilmour, D.S.2
  • 3
    • 18944366286 scopus 로고    scopus 로고
    • Functional characterization of core promoter elements: DPE-specific transcription requires the protein kinase CK2 and the PC4 coactivator
    • B.A. Lewis, R.J. Sims 3rd, W.S. Lane, and D. Reinberg Functional characterization of core promoter elements: DPE-specific transcription requires the protein kinase CK2 and the PC4 coactivator Mol. Cell 18 2005 471 481
    • (2005) Mol. Cell , vol.18 , pp. 471-481
    • Lewis, B.A.1    Sims III, R.J.2    Lane, W.S.3    Reinberg, D.4
  • 4
    • 1542328960 scopus 로고    scopus 로고
    • Identification and distinct regulation of yeast TATA box-containing genes
    • A.D. Basehoar, S.J. Zanton, and B.F. Pugh Identification and distinct regulation of yeast TATA box-containing genes Cell 116 2004 699 709
    • (2004) Cell , vol.116 , pp. 699-709
    • Basehoar, A.D.1    Zanton, S.J.2    Pugh, B.F.3
  • 5
    • 0025288866 scopus 로고
    • DNA-binding and transcriptional properties of human transcription factor TFIID after mild proteolysis
    • M.W. Van Dyke, and M. Sawadogo DNA-binding and transcriptional properties of human transcription factor TFIID after mild proteolysis Mol. Cell. Biol. 10 1990 3415 3420
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3415-3420
    • Van Dyke, M.W.1    Sawadogo, M.2
  • 6
    • 0032765083 scopus 로고    scopus 로고
    • Three-dimensional structure of the human TFIID-IIA-IIB complex
    • F. Andel 3rd, A.G. Ladurner, C. Inouye, R. Tjian, and E. Nogales Three-dimensional structure of the human TFIID-IIA-IIB complex Science 286 1999 2153 2156
    • (1999) Science , vol.286 , pp. 2153-2156
    • Andel III, F.1    Ladurner, A.G.2    Inouye, C.3    Tjian, R.4    Nogales, E.5
  • 7
    • 77954763022 scopus 로고    scopus 로고
    • Unexpected roles for core promoter recognition factors in cell-type-specific transcription and gene regulation
    • J.A. Goodrich, and R. Tjian Unexpected roles for core promoter recognition factors in cell-type-specific transcription and gene regulation Nat. Rev. Genet. 11 2010 549 558
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 549-558
    • Goodrich, J.A.1    Tjian, R.2
  • 10
    • 0023804820 scopus 로고
    • In vitro transcription of the Drosophila engrailed gene
    • W.C. Soeller, S.J. Poole, and T. Kornberg In vitro transcription of the Drosophila engrailed gene Genes Dev. 2 1988 68 81
    • (1988) Genes Dev. , vol.2 , pp. 68-81
    • Soeller, W.C.1    Poole, S.J.2    Kornberg, T.3
  • 11
    • 0031582085 scopus 로고    scopus 로고
    • Multiple downstream promoter modules regulate the transcription of the Drosophila melanogaster I, Doc and F elements
    • G. Minchiotti, C. Contursi, and P.P. Di Nocera Multiple downstream promoter modules regulate the transcription of the Drosophila melanogaster I, Doc and F elements J. Mol. Biol. 267 1997 37 46
    • (1997) J. Mol. Biol. , vol.267 , pp. 37-46
    • Minchiotti, G.1    Contursi, C.2    Di Nocera, P.P.3
  • 12
    • 79953713243 scopus 로고    scopus 로고
    • Molecular architecture of the human mediator-RNA polymerase II-TFIIF assembly
    • C. Bernecky, P. Grob, C.C. Ebmeier, E. Nogales, and D.J. Taatjes Molecular architecture of the human mediator-RNA polymerase II-TFIIF assembly PLoS Biol. 2011 e1000603
    • (2011) PLoS Biol. , pp. 1000603
    • Bernecky, C.1    Grob, P.2    Ebmeier, C.C.3    Nogales, E.4    Taatjes, D.J.5
  • 13
    • 84862666457 scopus 로고    scopus 로고
    • A movie of RNA polymerase II transcription
    • A.C. Cheung, and P. Cramer A movie of RNA polymerase II transcription Cell 149 2012 1431 1437
    • (2012) Cell , vol.149 , pp. 1431-1437
    • Cheung, A.C.1    Cramer, P.2
  • 14
    • 33644838451 scopus 로고    scopus 로고
    • Cryo-electron microscopy studies of human TFIID: Conformational breathing in the integration of gene regulatory cues
    • P. Grob, M.J. Cruse, C. Inouye, M. Peris, P.A. Penczek, R. Tjian, and E. Nogales Cryo-electron microscopy studies of human TFIID: conformational breathing in the integration of gene regulatory cues Structure 14 2006 511 520
    • (2006) Structure , vol.14 , pp. 511-520
    • Grob, P.1    Cruse, M.J.2    Inouye, C.3    Peris, M.4    Penczek, P.A.5    Tjian, R.6    Nogales, E.7
  • 15
    • 79953162966 scopus 로고    scopus 로고
    • New insights into the function of transcription factor TFIID from recent structural studies
    • G. Papai, P.A. Weil, and P. Schultz New insights into the function of transcription factor TFIID from recent structural studies Curr. Opin. Genet. Dev. 21 2011 219 224
    • (2011) Curr. Opin. Genet. Dev. , vol.21 , pp. 219-224
    • Papai, G.1    Weil, P.A.2    Schultz, P.3
  • 16
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • E.L. Sonnhammer, S.R. Eddy, and R. Durbin Pfam: a comprehensive database of protein domain families based on seed alignments Proteins 28 1997 405 420
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 18
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • A. Lupas, M. Van Dyke, and J. Stock Predicting coiled coils from protein sequences Science 252 1991 1162 1164
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 19
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • R. Linding, R.B. Russell, V. Neduva, and T.J. Gibson GlobPlot: exploring protein sequences for globularity and disorder Nucleic Acids Res. 31 2003 3701 3708
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 21
    • 0038386050 scopus 로고    scopus 로고
    • 3D-Jury: A simple approach to improve protein structure predictions
    • K. Ginalski, A. Elofsson, D. Fischer, and L. Rychlewski 3D-Jury: a simple approach to improve protein structure predictions Bioinformatics 19 2003 1015 1018
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, K.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 22
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST-A tool for discovery in protein databases
    • S.F. Altschul, and E.V. Koonin Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases Trends Biochem. Sci. 23 1998 444 447
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 24
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • L.J. McGuffin, K. Bryson, and D.T. Jones The PSIPRED protein structure prediction server Bioinformatics 16 2000 404 405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 26
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 27
    • 54949097750 scopus 로고    scopus 로고
    • MetaMQAP: A meta-server for the quality assessment of protein models
    • M. Pawlowski, M.J. Gajda, R. Matlak, and J.M. Bujnicki MetaMQAP: a meta-server for the quality assessment of protein models BMC Bioinform. 9 2008 403
    • (2008) BMC Bioinform. , vol.9 , pp. 403
    • Pawlowski, M.1    Gajda, M.J.2    Matlak, R.3    Bujnicki, J.M.4
  • 32
    • 0033969766 scopus 로고    scopus 로고
    • TAFs revisited: More data reveal new twists and confirm old ideas
    • S.R. Albright, and R. Tjian TAFs revisited: more data reveal new twists and confirm old ideas Gene 242 2000 1 13
    • (2000) Gene , vol.242 , pp. 1-13
    • Albright, S.R.1    Tjian, R.2
  • 33
    • 0036724187 scopus 로고    scopus 로고
    • Mechanism of rapid transcriptional induction of tumor necrosis factor alpha-responsive genes by NF-kappaB
    • E. Ainbinder, M. Revach, O. Wolstein, S. Moshonov, N. Diamant, and R. Dikstein Mechanism of rapid transcriptional induction of tumor necrosis factor alpha-responsive genes by NF-kappaB Mol. Cell. Biol. 22 2002 6354 6362
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6354-6362
    • Ainbinder, E.1    Revach, M.2    Wolstein, O.3    Moshonov, S.4    Diamant, N.5    Dikstein, R.6
  • 34
    • 77953711351 scopus 로고    scopus 로고
    • TFIIA and the transactivator Rap1 cooperate to commit TFIID for transcription initiation
    • G. Papai, M.K. Tripathi, C. Ruhlmann, J.H. Layer, P.A. Weil, and P. Schultz TFIIA and the transactivator Rap1 cooperate to commit TFIID for transcription initiation Nature 465 2010 956 960
    • (2010) Nature , vol.465 , pp. 956-960
    • Papai, G.1    Tripathi, M.K.2    Ruhlmann, C.3    Layer, J.H.4    Weil, P.A.5    Schultz, P.6
  • 35
    • 67649946313 scopus 로고    scopus 로고
    • Recent advances in understanding the structure and function of general transcription factor TFIID
    • E. Cler, G. Papai, P. Schultz, and I. Davidson Recent advances in understanding the structure and function of general transcription factor TFIID Cell. Mol. Life Sci. 66 2009 2123 2134
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2123-2134
    • Cler, E.1    Papai, G.2    Schultz, P.3    Davidson, I.4
  • 36
    • 34247275734 scopus 로고    scopus 로고
    • Crystal structure, biochemical and genetic characterization of yeast and E. cuniculi TAF(II)5 N-terminal domain: Implications for TFIID assembly
    • C. Romier, N. James, C. Birck, J. Cavarelli, C. Vivares, M.A. Collart, and D. Moras Crystal structure, biochemical and genetic characterization of yeast and E. cuniculi TAF(II)5 N-terminal domain: implications for TFIID assembly J. Mol. Biol. 368 2007 1292 1306
    • (2007) J. Mol. Biol. , vol.368 , pp. 1292-1306
    • Romier, C.1    James, N.2    Birck, C.3    Cavarelli, J.4    Vivares, C.5    Collart, M.A.6    Moras, D.7
  • 37
    • 33846587568 scopus 로고    scopus 로고
    • Structural analysis and dimerization potential of the human TAF5 subunit of TFIID
    • S. Bhattacharya, S. Takada, and R.H. Jacobson Structural analysis and dimerization potential of the human TAF5 subunit of TFIID Proc. Natl. Acad. Sci. U.S.A. 104 2007 1189 1194
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 1189-1194
    • Bhattacharya, S.1    Takada, S.2    Jacobson, R.H.3
  • 38
    • 2942535001 scopus 로고    scopus 로고
    • The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications
    • M.H. Kim, D.R. Cooper, A. Oleksy, Y. Devedjiev, U. Derewenda, O. Reiner, J. Otlewski, and Z.S. Derewenda The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications Structure 12 2004 987 998
    • (2004) Structure , vol.12 , pp. 987-998
    • Kim, M.H.1    Cooper, D.R.2    Oleksy, A.3    Devedjiev, Y.4    Derewenda, U.5    Reiner, O.6    Otlewski, J.7    Derewenda, Z.S.8
  • 39
    • 33344471552 scopus 로고    scopus 로고
    • The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif
    • A. Mateja, T. Cierpicki, M. Paduch, Z.S. Derewenda, and J. Otlewski The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif J. Mol. Biol. 357 2006 621 631
    • (2006) J. Mol. Biol. , vol.357 , pp. 621-631
    • Mateja, A.1    Cierpicki, T.2    Paduch, M.3    Derewenda, Z.S.4    Otlewski, J.5
  • 40
    • 58149161238 scopus 로고    scopus 로고
    • Diversity of WD-repeat proteins
    • T.F. Smith Diversity of WD-repeat proteins Subcell. Biochem. 48 2008 20 30
    • (2008) Subcell. Biochem. , vol.48 , pp. 20-30
    • Smith, T.F.1
  • 41
    • 0029982356 scopus 로고    scopus 로고
    • Distinct domains of hTAFII100 are required for functional interaction with transcription factor TFIIF beta (RAP30) and incorporation into the TFIID complex
    • V. Dubrovskaya, A.C. Lavigne, I. Davidson, J. Acker, A. Staub, and L. Tora Distinct domains of hTAFII100 are required for functional interaction with transcription factor TFIIF beta (RAP30) and incorporation into the TFIID complex EMBO J. 15 1996 3702 3712
    • (1996) EMBO J. , vol.15 , pp. 3702-3712
    • Dubrovskaya, V.1    Lavigne, A.C.2    Davidson, I.3    Acker, J.4    Staub, A.5    Tora, L.6
  • 42
    • 84874657139 scopus 로고    scopus 로고
    • The BioMolecular Engineering Research Center
    • The BioMolecular Engineering Research Center The WD Repeat Family of Proteins 25/10/2012 http://bmerc-www.bu.edu/projects/wdrepeat/
    • (2012) The WD Repeat Family of Proteins
  • 44
    • 0034791302 scopus 로고    scopus 로고
    • Analysis of TAF90 mutants displaying allele-specific and broad defects in transcription
    • R.J. Durso, A.K. Fisher, T.J. Albright-Frey, and J.C. Reese Analysis of TAF90 mutants displaying allele-specific and broad defects in transcription Mol. Cell. Biol. 21 2001 7331 7344
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7331-7344
    • Durso, R.J.1    Fisher, A.K.2    Albright-Frey, T.J.3    Reese, J.C.4
  • 46
    • 0036566794 scopus 로고    scopus 로고
    • Identification of histone H4-like TAF in Schizosaccharomyces pombe as a protein that interacts with WD repeat-containing TAF
    • H. Mitsuzawa, and A. Ishihama Identification of histone H4-like TAF in Schizosaccharomyces pombe as a protein that interacts with WD repeat-containing TAF Nucleic Acids Res. 30 2002 1952 1958
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1952-1958
    • Mitsuzawa, H.1    Ishihama, A.2
  • 47
    • 44149123117 scopus 로고    scopus 로고
    • Structural basis of histone H4 recognition by p55
    • J.J. Song, J.D. Garlick, and R.E. Kingston Structural basis of histone H4 recognition by p55 Genes Dev. 22 2008 1313 1318
    • (2008) Genes Dev. , vol.22 , pp. 1313-1318
    • Song, J.J.1    Garlick, J.D.2    Kingston, R.E.3
  • 53
    • 0034954166 scopus 로고    scopus 로고
    • The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger
    • Y.G. Gangloff, J.C. Pointud, S. Thuault, L. Carre, C. Romier, S. Muratoglu, M. Brand, L. Tora, J.L. Couderc, and I. Davidson The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger Mol. Cell. Biol. 21 2001 5109 5121
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5109-5121
    • Gangloff, Y.G.1    Pointud, J.C.2    Thuault, S.3    Carre, L.4    Romier, C.5    Muratoglu, S.6    Brand, M.7    Tora, L.8    Couderc, J.L.9    Davidson, I.10
  • 55
    • 4344669438 scopus 로고    scopus 로고
    • E protein silencing by the leukemogenic AML1-ETO fusion protein
    • J. Zhang, M. Kalkum, S. Yamamura, B.T. Chait, and R.G. Roeder E protein silencing by the leukemogenic AML1-ETO fusion protein Science 305 2004 1286 1289
    • (2004) Science , vol.305 , pp. 1286-1289
    • Zhang, J.1    Kalkum, M.2    Yamamura, S.3    Chait, B.T.4    Roeder, R.G.5
  • 56
    • 34249943644 scopus 로고    scopus 로고
    • Conserved region i of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators
    • X. Wang, D.M. Truckses, S. Takada, T. Matsumura, N. Tanese, and R.H. Jacobson Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators Proc. Natl. Acad. Sci. U.S.A. 104 2007 7839 7844
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7839-7844
    • Wang, X.1    Truckses, D.M.2    Takada, S.3    Matsumura, T.4    Tanese, N.5    Jacobson, R.H.6
  • 57
    • 0037160103 scopus 로고    scopus 로고
    • Crystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20)
    • S. Werten, A. Mitschler, C. Romier, Y.G. Gangloff, S. Thuault, I. Davidson, and D. Moras Crystal structure of a subcomplex of human transcription factor TFIID formed by TATA binding protein-associated factors hTAF4 (hTAF(II)135) and hTAF12 (hTAF(II)20) J. Biol. Chem. 277 2002 45502 45509
    • (2002) J. Biol. Chem. , vol.277 , pp. 45502-45509
    • Werten, S.1    Mitschler, A.2    Romier, C.3    Gangloff, Y.G.4    Thuault, S.5    Davidson, I.6    Moras, D.7
  • 58
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking
    • R. Bayliss, T. Littlewood, and M. Stewart Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking Cell 102 2000 99 108
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 59
    • 0036923972 scopus 로고    scopus 로고
    • Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta
    • G. Cingolani, J. Bednenko, M.T. Gillespie, and L. Gerace Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta Mol. Cell 10 2002 1345 1353
    • (2002) Mol. Cell , vol.10 , pp. 1345-1353
    • Cingolani, G.1    Bednenko, J.2    Gillespie, M.T.3    Gerace, L.4
  • 60
    • 0037184968 scopus 로고    scopus 로고
    • GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta
    • R. Bayliss, T. Littlewood, L.A. Strawn, S.R. Wente, and M. Stewart GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta J. Biol. Chem. 277 2002 50597 50606
    • (2002) J. Biol. Chem. , vol.277 , pp. 50597-50606
    • Bayliss, R.1    Littlewood, T.2    Strawn, L.A.3    Wente, S.R.4    Stewart, M.5
  • 61
    • 43149121353 scopus 로고    scopus 로고
    • Molecular basis for the recognition of snurportin 1 by importin beta
    • G. Mitrousis, A.S. Olia, N. Walker-Kopp, and G. Cingolani Molecular basis for the recognition of snurportin 1 by importin beta J. Biol. Chem. 283 2008 7877 7884
    • (2008) J. Biol. Chem. , vol.283 , pp. 7877-7884
    • Mitrousis, G.1    Olia, A.S.2    Walker-Kopp, N.3    Cingolani, G.4
  • 62
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-beta bound to the IBB domain of importin-alpha
    • G. Cingolani, C. Petosa, K. Weis, and C.W. Muller Structure of importin-beta bound to the IBB domain of importin-alpha Nature 399 1999 221 229
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 63
    • 35748985252 scopus 로고    scopus 로고
    • Structural basis for RanGTP independent entry of spliceosomal U snRNPs into the nucleus
    • D. Wohlwend, A. Strasser, A. Dickmanns, and R. Ficner Structural basis for RanGTP independent entry of spliceosomal U snRNPs into the nucleus J. Mol. Biol. 374 2007 1129 1138
    • (2007) J. Mol. Biol. , vol.374 , pp. 1129-1138
    • Wohlwend, D.1    Strasser, A.2    Dickmanns, A.3    Ficner, R.4
  • 65
    • 84864975153 scopus 로고    scopus 로고
    • TFIID TAF6/TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5
    • E. Scheer, F. Delbac, L. Tora, D. Moras, and C. Romier TFIID TAF6/TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5 J. Biol. Chem. 287 2012 27580 27592
    • (2012) J. Biol. Chem. , vol.287 , pp. 27580-27592
    • Scheer, E.1    Delbac, F.2    Tora, L.3    Moras, D.4    Romier, C.5
  • 66
    • 0031754774 scopus 로고    scopus 로고
    • The armadillo family of structural proteins
    • M. Hatzfeld The armadillo family of structural proteins Int. Rev. Cytol. 186 1999 179 224
    • (1999) Int. Rev. Cytol. , vol.186 , pp. 179-224
    • Hatzfeld, M.1
  • 67
    • 16544366708 scopus 로고    scopus 로고
    • ARIA, an Arabidopsis arm repeat protein interacting with a transcriptional regulator of abscisic acid-responsive gene expression, is a novel abscisic acid signaling component
    • S. Kim, H.I. Choi, H.J. Ryu, J.H. Park, M.D. Kim, and S.Y. Kim ARIA, an Arabidopsis arm repeat protein interacting with a transcriptional regulator of abscisic acid-responsive gene expression, is a novel abscisic acid signaling component Plant Physiol. 136 2004 3639 3648
    • (2004) Plant Physiol. , vol.136 , pp. 3639-3648
    • Kim, S.1    Choi, H.I.2    Ryu, H.J.3    Park, J.H.4    Kim, M.D.5    Kim, S.Y.6
  • 70
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 A resolution: A tripartite protein assembly and a left-handed superhelix
    • G. Arents, R.W. Burlingame, B.C. Wang, W.E. Love, and E.N. Moudrianakis The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix Proc. Natl. Acad. Sci. U.S.A. 88 1991 10148 10152
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 71
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • K. Luger, A.W. Mader, R.K. Richmond, D.F. Sargent, and T.J. Richmond Crystal structure of the nucleosome core particle at 2.8 A resolution Nature 389 1997 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 72
    • 0032563164 scopus 로고    scopus 로고
    • Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family
    • C. Birck, O. Poch, C. Romier, M. Ruff, G. Mengus, A.C. Lavigne, I. Davidson, and D. Moras Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family Cell 94 1998 239 249
    • (1998) Cell , vol.94 , pp. 239-249
    • Birck, C.1    Poch, O.2    Romier, C.3    Ruff, M.4    Mengus, G.5    Lavigne, A.C.6    Davidson, I.7    Moras, D.8
  • 77
    • 0028861418 scopus 로고
    • The PHD finger: Implications for chromatin-mediated transcriptional regulation
    • R. Aasland, T.J. Gibson, and A.F. Stewart The PHD finger: implications for chromatin-mediated transcriptional regulation Trends Biochem. Sci. 20 1995 56 59
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 56-59
    • Aasland, R.1    Gibson, T.J.2    Stewart, A.F.3
  • 78
    • 33846019277 scopus 로고    scopus 로고
    • Methylation of lysine 4 on histone H3: Intricacy of writing and reading a single epigenetic mark
    • A.J. Ruthenburg, C.D. Allis, and J. Wysocka Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark Mol. Cell 25 2007 15 30
    • (2007) Mol. Cell , vol.25 , pp. 15-30
    • Ruthenburg, A.J.1    Allis, C.D.2    Wysocka, J.3
  • 80
    • 0035135515 scopus 로고    scopus 로고
    • Histone folds mediate selective heterodimerization of yeast TAF(II)25 with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7
    • Y.G. Gangloff, S.L. Sanders, C. Romier, D. Kirschner, P.A. Weil, L. Tora, and I. Davidson Histone folds mediate selective heterodimerization of yeast TAF(II)25 with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7 Mol. Cell. Biol. 21 2001 1841 1853
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1841-1853
    • Gangloff, Y.G.1    Sanders, S.L.2    Romier, C.3    Kirschner, D.4    Weil, P.A.5    Tora, L.6    Davidson, I.7
  • 81
    • 18144399308 scopus 로고    scopus 로고
    • The nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partners
    • E. Soutoglou, M.A. Demeny, E. Scheer, G. Fienga, P. Sassone-Corsi, and L. Tora The nuclear import of TAF10 is regulated by one of its three histone fold domain-containing interaction partners Mol. Cell. Biol. 25 2005 4092 4104
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4092-4104
    • Soutoglou, E.1    Demeny, M.A.2    Scheer, E.3    Fienga, G.4    Sassone-Corsi, P.5    Tora, L.6
  • 83
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Y. Kim, J.H. Geiger, S. Hahn, and P.B. Sigler Crystal structure of a yeast TBP/TATA-box complex Nature 365 1993 512 520
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geiger, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 84
    • 0034082814 scopus 로고    scopus 로고
    • Binding mechanisms of TATA box-binding proteins: DNA kinking is stabilized by specific hydrogen bonds
    • L. Pardo, M. Campillo, D. Bosch, N. Pastor, and H. Weinstein Binding mechanisms of TATA box-binding proteins: DNA kinking is stabilized by specific hydrogen bonds Biophys. J. 78 2000 1988 1996
    • (2000) Biophys. J. , vol.78 , pp. 1988-1996
    • Pardo, L.1    Campillo, M.2    Bosch, D.3    Pastor, N.4    Weinstein, H.5
  • 85
    • 0032483558 scopus 로고    scopus 로고
    • Solution structure of a TBP-TAF(II)230 complex: Protein mimicry of the minor groove surface of the TATA box unwound by TBP
    • D. Liu, R. Ishima, K.I. Tong, S. Bagby, T. Kokubo, D.R. Muhandiram, L.E. Kay, Y. Nakatani, and M. Ikura Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP Cell 94 1998 573 583
    • (1998) Cell , vol.94 , pp. 573-583
    • Liu, D.1    Ishima, R.2    Tong, K.I.3    Bagby, S.4    Kokubo, T.5    Muhandiram, D.R.6    Kay, L.E.7    Nakatani, Y.8    Ikura, M.9
  • 86
    • 0032710459 scopus 로고    scopus 로고
    • The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo
    • A.M. Dudley, C. Rougeulle, and F. Winston The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo Genes Dev. 13 1999 2940 2945
    • (1999) Genes Dev. , vol.13 , pp. 2940-2945
    • Dudley, A.M.1    Rougeulle, C.2    Winston, F.3
  • 87
    • 0034839274 scopus 로고    scopus 로고
    • TAF(II)250: A transcription toolbox
    • D.A. Wassarman, and F. Sauer TAF(II)250: a transcription toolbox J. Cell. Sci. 114 2001 2895 2902
    • (2001) J. Cell. Sci. , vol.114 , pp. 2895-2902
    • Wassarman, D.A.1    Sauer, F.2
  • 88
    • 0032913567 scopus 로고    scopus 로고
    • Phosphorylation of TFIIA stimulates TATA binding protein-TATA interaction and contributes to maximal transcription and viability in yeast
    • S.P. Solow, L. Lezina, and P.M. Lieberman Phosphorylation of TFIIA stimulates TATA binding protein-TATA interaction and contributes to maximal transcription and viability in yeast Mol. Cell. Biol. 19 1999 2846 2852
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2846-2852
    • Solow, S.P.1    Lezina, L.2    Lieberman, P.M.3
  • 89
    • 2342506598 scopus 로고    scopus 로고
    • TAF1 activates transcription by phosphorylation of serine 33 in histone H2B
    • T. Maile, S. Kwoczynski, R.J. Katzenberger, D.A. Wassarman, and F. Sauer TAF1 activates transcription by phosphorylation of serine 33 in histone H2B Science 304 2004 1010 1014
    • (2004) Science , vol.304 , pp. 1010-1014
    • Maile, T.1    Kwoczynski, S.2    Katzenberger, R.J.3    Wassarman, D.A.4    Sauer, F.5
  • 91
    • 0034730745 scopus 로고    scopus 로고
    • Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila
    • A.D. Pham, and F. Sauer Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila Science 289 2000 2357 2360
    • (2000) Science , vol.289 , pp. 2357-2360
    • Pham, A.D.1    Sauer, F.2
  • 92
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAFII250 double bromodomain module
    • R.H. Jacobson, A.G. Ladurner, D.S. King, and R. Tjian Structure and function of a human TAFII250 double bromodomain module Science 288 2000 1422 1425
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H.1    Ladurner, A.G.2    King, D.S.3    Tjian, R.4
  • 93
    • 0035845006 scopus 로고    scopus 로고
    • Structure and function of bromodomains in chromatin-regulating complexes
    • R. Marmorstein, and S.L. Berger Structure and function of bromodomains in chromatin-regulating complexes Gene 272 2001 1 9
    • (2001) Gene , vol.272 , pp. 1-9
    • Marmorstein, R.1    Berger, S.L.2
  • 94
    • 0037007180 scopus 로고    scopus 로고
    • Ratcheting up vir gene expression in Agrobacterium tumefaciens: Coiled coils in histidine kinase signal transduction
    • Y. Wang, R. Gao, and D.G. Lynn Ratcheting up vir gene expression in Agrobacterium tumefaciens: coiled coils in histidine kinase signal transduction Chembiochem 3 2002 311 317
    • (2002) Chembiochem , vol.3 , pp. 311-317
    • Wang, Y.1    Gao, R.2    Lynn, D.G.3
  • 95
    • 0036674866 scopus 로고    scopus 로고
    • NUANCE, a giant protein connecting the nucleus and actin cytoskeleton
    • Y.Y. Zhen, T. Libotte, M. Munck, A.A. Noegel, and E. Korenbaum NUANCE, a giant protein connecting the nucleus and actin cytoskeleton J. Cell. Sci. 115 2002 3207 3222
    • (2002) J. Cell. Sci. , vol.115 , pp. 3207-3222
    • Zhen, Y.Y.1    Libotte, T.2    Munck, M.3    Noegel, A.A.4    Korenbaum, E.5
  • 100
    • 0030832267 scopus 로고    scopus 로고
    • The class II trans-activator CIITA interacts with the TBP-associated factor TAFII32
    • J.D. Fontes, B. Jiang, and B.M. Peterlin The class II trans-activator CIITA interacts with the TBP-associated factor TAFII32 Nucleic Acids Res. 25 1997 2522 2528
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2522-2528
    • Fontes, J.D.1    Jiang, B.2    Peterlin, B.M.3
  • 101
    • 0030987367 scopus 로고    scopus 로고
    • Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein
    • S.K. Mahanta, T. Scholl, F.C. Yang, and J.L. Strominger Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein Proc. Natl. Acad. Sci. U.S.A. 94 1997 6324 6329
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6324-6329
    • Mahanta, S.K.1    Scholl, T.2    Yang, F.C.3    Strominger, J.L.4
  • 103
    • 25444456367 scopus 로고    scopus 로고
    • Prediction of the general transcription factors associated with RNA polymerase II in Plasmodium falciparum: Conserved features and differences relative to other eukaryotes
    • I. Callebaut, K. Prat, E. Meurice, J.P. Mornon, and S. Tomavo Prediction of the general transcription factors associated with RNA polymerase II in Plasmodium falciparum: conserved features and differences relative to other eukaryotes BMC Genom. 6 2005 100
    • (2005) BMC Genom. , vol.6 , pp. 100
    • Callebaut, I.1    Prat, K.2    Meurice, E.3    Mornon, J.P.4    Tomavo, S.5
  • 104
    • 37349116228 scopus 로고    scopus 로고
    • Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis
    • B. Nocek, R. Mulligan, M. Bargassa, F. Collart, and A. Joachimiak Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis Proteins 70 2008 273 279
    • (2008) Proteins , vol.70 , pp. 273-279
    • Nocek, B.1    Mulligan, R.2    Bargassa, M.3    Collart, F.4    Joachimiak, A.5
  • 105
    • 79956081199 scopus 로고    scopus 로고
    • The role of multifunctional M1 metallopeptidases in cell cycle progression
    • W.A. Peer The role of multifunctional M1 metallopeptidases in cell cycle progression Ann. Bot. 107 2011 1171 1181
    • (2011) Ann. Bot. , vol.107 , pp. 1171-1181
    • Peer, W.A.1
  • 106
    • 84874655703 scopus 로고    scopus 로고
    • Structural and biochemical studies on human TAF2
    • M. Mijuskovic Structural and biochemical studies on human TAF2 ETH 2007
    • (2007) ETH
    • Mijuskovic, M.1
  • 107
    • 0029812470 scopus 로고    scopus 로고
    • HTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II
    • A. Bertolotti, Y. Lutz, D.J. Heard, P. Chambon, and L. Tora hTAF(II)68, a novel RNA/ssDNA-binding protein with homology to the pro-oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II EMBO J. 15 1996 5022 5031
    • (1996) EMBO J. , vol.15 , pp. 5022-5031
    • Bertolotti, A.1    Lutz, Y.2    Heard, D.J.3    Chambon, P.4    Tora, L.5
  • 109
    • 63049100536 scopus 로고    scopus 로고
    • PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function
    • L. Jobert, M. Argentini, and L. Tora PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function Exp. Cell. Res. 315 2009 1273 1286
    • (2009) Exp. Cell. Res. , vol.315 , pp. 1273-1286
    • Jobert, L.1    Argentini, M.2    Tora, L.3
  • 110
    • 0031935157 scopus 로고    scopus 로고
    • EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: Interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes
    • A. Bertolotti, T. Melot, J. Acker, M. Vigneron, O. Delattre, and L. Tora EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes Mol. Cell. Biol. 18 1998 1489 1497
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1489-1497
    • Bertolotti, A.1    Melot, T.2    Acker, J.3    Vigneron, M.4    Delattre, O.5    Tora, L.6
  • 111
    • 0242581682 scopus 로고    scopus 로고
    • Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition
    • D. Lu, M.A. Searles, and A. Klug Crystal structure of a zinc-finger-RNA complex reveals two modes of molecular recognition Nature 426 2003 96 100
    • (2003) Nature , vol.426 , pp. 96-100
    • Lu, D.1    Searles, M.A.2    Klug, A.3
  • 112
    • 0029082445 scopus 로고
    • The interaction of TFIIIA with specific RNA-DNA heteroduplexes
    • K.P. Nightingale, and A.P. Wolffe The interaction of TFIIIA with specific RNA-DNA heteroduplexes J. Biol. Chem. 270 1995 22665 22668
    • (1995) J. Biol. Chem. , vol.270 , pp. 22665-22668
    • Nightingale, K.P.1    Wolffe, A.P.2
  • 113
    • 0037087628 scopus 로고    scopus 로고
    • A unified nomenclature for TATA box binding protein (TBP)-associated factors (TAFs) involved in RNA polymerase II transcription
    • L. Tora A unified nomenclature for TATA box binding protein (TBP)-associated factors (TAFs) involved in RNA polymerase II transcription Genes Dev. 16 2002 673 675
    • (2002) Genes Dev. , vol.16 , pp. 673-675
    • Tora, L.1


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