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Volumn 123, Issue 3, 2005, Pages 423-436

The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators

Author keywords

[No Author keywords available]

Indexed keywords

19S PROTEASOME REGULATORY PARTICLE; ADENOSINE TRIPHOSPHATASE; DNA BINDING PROTEIN; FUNGAL DNA; FUNGAL PROTEIN; HISTONE H3; PROTEASOME; REGULATOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR SAGA; UNCLASSIFIED DRUG;

EID: 27544486193     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2005.08.015     Document Type: Article
Times cited : (156)

References (54)
  • 2
    • 0033769733 scopus 로고    scopus 로고
    • PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone
    • N. Benaroudj, and A.L. Goldberg PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone Nat. Cell Biol. 2 2000 833 839
    • (2000) Nat. Cell Biol. , vol.2 , pp. 833-839
    • Benaroudj, N.1    Goldberg, A.L.2
  • 4
    • 0035423749 scopus 로고    scopus 로고
    • SAGA is an essential in vivo target of the yeast acidic activator Gal4p
    • S.R. Bhaumik, and M.R. Green SAGA is an essential in vivo target of the yeast acidic activator Gal4p Genes Dev. 15 2001 1935 1945
    • (2001) Genes Dev. , vol.15 , pp. 1935-1945
    • Bhaumik, S.R.1    Green, M.R.2
  • 5
    • 10944235448 scopus 로고    scopus 로고
    • ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication
    • J.L. Bowers, J.C. Randell, S. Chen, and S.P. Bell ATP hydrolysis by ORC catalyzes reiterative Mcm2-7 assembly at a defined origin of replication Mol. Cell 16 2004 967 978
    • (2004) Mol. Cell , vol.16 , pp. 967-978
    • Bowers, J.L.1    Randell, J.C.2    Chen, S.3    Bell, S.P.4
  • 6
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • G.D. Bowman, M. O'Donnell, and J. Kuriyan Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex Nature 429 2004 724 730
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 8
    • 0035933521 scopus 로고    scopus 로고
    • Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit
    • C.E. Brown, L. Howe, K. Sousa, S.C. Alley, M.J. Carrozza, S. Tan, and J.L. Workman Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit Science 292 2001 2333 2337
    • (2001) Science , vol.292 , pp. 2333-2337
    • Brown, C.E.1    Howe, L.2    Sousa, K.3    Alley, S.C.4    Carrozza, M.J.5    Tan, S.6    Workman, J.L.7
  • 11
    • 0035076210 scopus 로고    scopus 로고
    • Histone acetylation at promoters is differentially affected by specific activators and repressors
    • J. Deckert, and K. Struhl Histone acetylation at promoters is differentially affected by specific activators and repressors Mol. Cell. Biol. 21 2001 2726 2735
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2726-2735
    • Deckert, J.1    Struhl, K.2
  • 12
    • 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
  • 13
    • 0031710891 scopus 로고    scopus 로고
    • Identification and analysis of yeast nucleosomal histone acetyltransferase complexes
    • A. Eberharter, S. John, P.A. Grant, R.T. Utley, and J.L. Workman Identification and analysis of yeast nucleosomal histone acetyltransferase complexes Methods 15 1998 315 321
    • (1998) Methods , vol.15 , pp. 315-321
    • Eberharter, A.1    John, S.2    Grant, P.A.3    Utley, R.T.4    Workman, J.L.5
  • 14
    • 1242271997 scopus 로고    scopus 로고
    • Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3
    • E. Ezhkova, and W.P. Tansey Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3 Mol. Cell 13 2004 435 442
    • (2004) Mol. Cell , vol.13 , pp. 435-442
    • Ezhkova, E.1    Tansey, W.P.2
  • 15
    • 0035947238 scopus 로고    scopus 로고
    • The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II
    • A. Ferdous, F. Gonzalez, L. Sun, T. Kodadek, and S.A. Johnston The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II Mol. Cell 7 2001 981 991
    • (2001) Mol. Cell , vol.7 , pp. 981-991
    • Ferdous, A.1    Gonzalez, F.2    Sun, L.3    Kodadek, T.4    Johnston, S.A.5
  • 16
    • 18944364218 scopus 로고    scopus 로고
    • Function of a eukaryotic transcription activator during the transcription cycle
    • J. Fishburn, N. Mohibullah, and S. Hahn Function of a eukaryotic transcription activator during the transcription cycle Mol. Cell 18 2005 369 378
    • (2005) Mol. Cell , vol.18 , pp. 369-378
    • Fishburn, J.1    Mohibullah, N.2    Hahn, S.3
  • 17
    • 13544259975 scopus 로고    scopus 로고
    • Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability
    • M. Funakoshi, X. Li, I. Velichutina, M. Hochstrasser, and H. Kobayashi Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability J. Cell Sci. 117 2004 6447 6454
    • (2004) J. Cell Sci. , vol.117 , pp. 6447-6454
    • Funakoshi, M.1    Li, X.2    Velichutina, I.3    Hochstrasser, M.4    Kobayashi, H.5
  • 18
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • M.H. Glickman, D.M. Rubin, O. Coux, I. Wefes, G. Pfeifer, Z. Cjeka, W. Baumeister, V.A. Fried, and D. Finley A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3 Cell 94 1998 615 623
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 19
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • F. Gonzalez, A. Delahodde, T. Kodadek, and S.A. Johnston Recruitment of a 19S proteasome subcomplex to an activated promoter Science 296 2002 548 550
    • (2002) Science , vol.296 , pp. 548-550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 21
    • 0035937419 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes stabilize swi/snf binding to promoter nucleosomes
    • A.H. Hassan, K.E. Neely, and J.L. Workman Histone acetyltransferase complexes stabilize swi/snf binding to promoter nucleosomes Cell 104 2001 817 827
    • (2001) Cell , vol.104 , pp. 817-827
    • Hassan, A.H.1    Neely, K.E.2    Workman, J.L.3
  • 23
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • L. Howe, D. Auston, P. Grant, S. John, R.G. Cook, J.L. Workman, and L. Pillus Histone H3 specific acetyltransferases are essential for cell cycle progression Genes Dev. 15 2001 3144 3154
    • (2001) Genes Dev. , vol.15 , pp. 3144-3154
    • Howe, L.1    Auston, D.2    Grant, P.3    John, S.4    Cook, R.G.5    Workman, J.L.6    Pillus, L.7
  • 24
    • 1542285166 scopus 로고    scopus 로고
    • A genome-wide housekeeping role for TFIID and a highly regulated stress-related role for SAGA in Saccharomyces cerevisiae
    • K.L. Huisinga, and B.F. Pugh A genome-wide housekeeping role for TFIID and a highly regulated stress-related role for SAGA in Saccharomyces cerevisiae Mol. Cell 13 2004 573 585
    • (2004) Mol. Cell , vol.13 , pp. 573-585
    • Huisinga, K.L.1    Pugh, B.F.2
  • 25
    • 0031022333 scopus 로고    scopus 로고
    • H1-mediated repression of transcription factor binding to a stably positioned nucleosome
    • L.J. Juan, R.T. Utley, M. Vignali, L. Bohm, and J.L. Workman H1-mediated repression of transcription factor binding to a stably positioned nucleosome J. Biol. Chem. 272 1997 3635 3640
    • (1997) J. Biol. Chem. , vol.272 , pp. 3635-3640
    • Juan, L.J.1    Utley, R.T.2    Vignali, M.3    Bohm, L.4    Workman, J.L.5
  • 26
    • 0942290540 scopus 로고    scopus 로고
    • Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B
    • C.F. Kao, C. Hillyer, T. Tsukuda, K. Henry, S. Berger, and M.A. Osley Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B Genes Dev. 18 2004 184 195
    • (2004) Genes Dev. , vol.18 , pp. 184-195
    • Kao, C.F.1    Hillyer, C.2    Tsukuda, T.3    Henry, K.4    Berger, S.5    Osley, M.A.6
  • 27
    • 0035425099 scopus 로고    scopus 로고
    • The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4
    • E. Larschan, and F. Winston The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4 Genes Dev. 15 2001 1946 1956
    • (2001) Genes Dev. , vol.15 , pp. 1946-1956
    • Larschan, E.1    Winston, F.2
  • 30
    • 0033213632 scopus 로고    scopus 로고
    • Transcriptional activation by Gcn4p involves independent interactions with the SWI/SNF complex and the SRB/mediator
    • K. Natarajan, B.M. Jackson, H. Zhou, F. Winston, and A.G. Hinnebusch Transcriptional activation by Gcn4p involves independent interactions with the SWI/SNF complex and the SRB/mediator Mol. Cell 4 1999 657 664
    • (1999) Mol. Cell , vol.4 , pp. 657-664
    • Natarajan, K.1    Jackson, B.M.2    Zhou, H.3    Winston, F.4    Hinnebusch, A.G.5
  • 31
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • A. Navon, and A.L. Goldberg Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome Mol. Cell 8 2001 1339 1349
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 32
    • 0033213277 scopus 로고    scopus 로고
    • Activation domain-mediated targeting of the SWI/SNF complex to promoters stimulates transcription from nucleosome arrays
    • K.E. Neely, A.H. Hassan, A.E. Wallberg, D.J. Steger, B.R. Cairns, A.P. Wright, and J.L. Workman Activation domain-mediated targeting of the SWI/SNF complex to promoters stimulates transcription from nucleosome arrays Mol. Cell 4 1999 649 655
    • (1999) Mol. Cell , vol.4 , pp. 649-655
    • Neely, K.E.1    Hassan, A.H.2    Wallberg, A.E.3    Steger, D.J.4    Cairns, B.R.5    Wright, A.P.6    Workman, J.L.7
  • 33
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • A.F. Neuwald, L. Aravind, J.L. Spouge, and E.V. Koonin AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes Genome Res. 9 1999 27 43
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 34
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • H.H. Ng, F. Robert, R.A. Young, and K. Struhl Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity Mol. Cell 11 2003 709 719
    • (2003) Mol. Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 36
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
    • M.G. Pray-Grant, J.A. Daniel, D. Schieltz, J.R. Yates 3rd, and P.A. Grant Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation Nature 433 2005 434 438
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schieltz, D.3    Yates III, J.R.4    Grant, P.A.5
  • 40
    • 3042799223 scopus 로고    scopus 로고
    • Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae
    • T. Sone, Y. Saeki, A. Toh-e, and H. Yokosawa Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae J. Biol. Chem. 279 2004 28807 28816
    • (2004) J. Biol. Chem. , vol.279 , pp. 28807-28816
    • Sone, T.1    Saeki, Y.2    Toh-E, A.3    Yokosawa, H.4
  • 41
    • 0141891451 scopus 로고    scopus 로고
    • Initiation of DNA replication: Lessons from viral initiator proteins
    • A. Stenlund Initiation of DNA replication: lessons from viral initiator proteins Nat. Rev. Mol. Cell Biol. 4 2003 777 785
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 777-785
    • Stenlund, A.1
  • 42
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • D.E. Sterner, and S.L. Berger Acetylation of histones and transcription-related factors Microbiol. Mol. Biol. Rev. 64 2000 435 459
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 43
    • 0037015044 scopus 로고    scopus 로고
    • SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription
    • D.E. Sterner, R. Belotserkovskaya, and S.L. Berger SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription Proc. Natl. Acad. Sci. USA 99 2002 11622 11627
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11622-11627
    • Sterner, D.E.1    Belotserkovskaya, R.2    Berger, S.L.3
  • 44
    • 0034090632 scopus 로고    scopus 로고
    • Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome
    • E. Strickland, K. Hakala, P.J. Thomas, and G.N. DeMartino Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome J. Biol. Chem. 275 2000 5565 5572
    • (2000) J. Biol. Chem. , vol.275 , pp. 5565-5572
    • Strickland, E.1    Hakala, K.2    Thomas, P.J.3    Demartino, G.N.4
  • 45
    • 0036384370 scopus 로고    scopus 로고
    • Physical association of the APIS complex and general transcription factors
    • L. Sun, S.A. Johnston, and T. Kodadek Physical association of the APIS complex and general transcription factors Biochem. Biophys. Res. Commun. 296 2002 991 999
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 991-999
    • Sun, L.1    Johnston, S.A.2    Kodadek, T.3
  • 46
    • 0028890360 scopus 로고
    • A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein
    • J.C. Swaffield, K. Melcher, and S.A. Johnston A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein Nature 374 1995 88 91
    • (1995) Nature , vol.374 , pp. 88-91
    • Swaffield, J.C.1    Melcher, K.2    Johnston, S.A.3
  • 48
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • R. Verma, S. Chen, R. Feldman, D. Schieltz, J. Yates, J. Dohmen, and R.J. Deshaies Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes Mol. Biol. Cell 11 2000 3425 3439
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 49
    • 0032031606 scopus 로고    scopus 로고
    • Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo
    • L. Wang, L. Liu, and S.L. Berger Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo Genes Dev. 12 1998 640 653
    • (1998) Genes Dev. , vol.12 , pp. 640-653
    • Wang, L.1    Liu, L.2    Berger, S.L.3
  • 50
    • 2442630488 scopus 로고    scopus 로고
    • Positive and negative functions of the SAGA complex mediated through interaction of Spt8 with TBP and the N-terminal domain of TFIIA
    • L. Warfield, J.A. Ranish, and S. Hahn Positive and negative functions of the SAGA complex mediated through interaction of Spt8 with TBP and the N-terminal domain of TFIIA Genes Dev. 18 2004 1022 1034
    • (2004) Genes Dev. , vol.18 , pp. 1022-1034
    • Warfield, L.1    Ranish, J.A.2    Hahn, S.3
  • 51
    • 0036311179 scopus 로고    scopus 로고
    • Analysis of Spt7 function in the Saccharomyces cerevisiae SAGA coactivator complex
    • P.Y. Wu, and F. Winston Analysis of Spt7 function in the Saccharomyces cerevisiae SAGA coactivator complex Mol. Cell. Biol. 22 2002 5367 5379
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5367-5379
    • Wu, P.Y.1    Winston, F.2
  • 52
    • 0028856102 scopus 로고
    • Sug1 modulates yeast transcription activation by Cdc68
    • Q. Xu, R.A. Singer, and G.C. Johnston Sug1 modulates yeast transcription activation by Cdc68 Mol. Cell. Biol. 15 1995 6025 6035
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6025-6035
    • Xu, Q.1    Singer, R.A.2    Johnston, G.C.3
  • 53
    • 11344274449 scopus 로고    scopus 로고
    • A kinase-independent function of Cks1 and Cdk1 in regulation of transcription
    • V.P. Yu, C. Baskerville, B. Grunenfelder, and S.I. Reed A kinase-independent function of Cks1 and Cdk1 in regulation of transcription Mol. Cell 17 2005 145 151
    • (2005) Mol. Cell , vol.17 , pp. 145-151
    • Yu, V.P.1    Baskerville, C.2    Grunenfelder, B.3    Reed, S.I.4
  • 54
    • 0032101179 scopus 로고    scopus 로고
    • Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase
    • W. Zhang, J.R. Bone, D.G. Edmondson, B.M. Turner, and S.Y. Roth Essential and redundant functions of histone acetylation revealed by mutation of target lysines and loss of the Gcn5p acetyltransferase EMBO J. 17 1998 3155 3167
    • (1998) EMBO J. , vol.17 , pp. 3155-3167
    • Zhang, W.1    Bone, J.R.2    Edmondson, D.G.3    Turner, B.M.4    Roth, S.Y.5


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