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Volumn 427, Issue 8, 2015, Pages 1765-1778

Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity

Author keywords

Deubiquitinating enzyme; SAGA; Sgf73; Transcription activation; Ubp8

Indexed keywords

SGF73 PROTEIN; TRANSCRIPTION FACTOR SAGA; UBIQUITIN; UNCLASSIFIED DRUG; HISTONE ACETYLTRANSFERASE; PROTEIN BINDING; PROTEINASE; SACCHAROMYCES CEREVISIAE PROTEIN; SAGA COMPLEX, S CEREVISIAE; SGF73 PROTEIN, S CEREVISIAE; TRANSACTIVATOR PROTEIN; UBP8 PROTEIN, S CEREVISIAE;

EID: 84933039719     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.12.004     Document Type: Article
Times cited : (14)

References (47)
  • 1
    • 77952569347 scopus 로고    scopus 로고
    • Inducible gene expression: Diverse regulatory mechanisms
    • Weake VM, Workman JL. Inducible gene expression: diverse regulatory mechanisms. Nat Rev Genet 2010;11:426-37.
    • (2010) Nat Rev Genet , vol.11 , pp. 426-437
    • Weake, V.M.1    Workman, J.L.2
  • 3
    • 68249129270 scopus 로고    scopus 로고
    • Insights into SAGA function during gene expression
    • Rodriguez-Navarro S. Insights into SAGA function during gene expression. EMBO Rep 2009;10:843-50.
    • (2009) EMBO Rep , vol.10 , pp. 843-850
    • Rodriguez-Navarro, S.1
  • 4
    • 79960080101 scopus 로고    scopus 로고
    • Combinatorial depletion analysis to assemble the network architecture of the SAGA and ADA chromatin remodeling complexes
    • Lee KK, Sardiu ME, Swanson SK, Gilmore JM, Torok M, Grant PA, et al. Combinatorial depletion analysis to assemble the network architecture of the SAGA and ADA chromatin remodeling complexes. Mol Syst Biol 2011;7:503.
    • (2011) Mol Syst Biol , vol.7 , pp. 503
    • Lee, K.K.1    Sardiu, M.E.2    Swanson, S.K.3    Gilmore, J.M.4    Torok, M.5    Grant, P.A.6
  • 5
    • 34147111657 scopus 로고    scopus 로고
    • Multi-tasking on chromatin with the SAGA coactivator complexes
    • Daniel JA, Grant PA. Multi-tasking on chromatin with the SAGA coactivator complexes. Mutat Res 2007;618:135-48.
    • (2007) Mutat Res , vol.618 , pp. 135-148
    • Daniel, J.A.1    Grant, P.A.2
  • 6
    • 0242361623 scopus 로고    scopus 로고
    • Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGAassociatedUbp8
    • Henry KW, Wyce A, Lo WS, Duggan LJ, Emre NC, Kao CF, et al. Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGAassociatedUbp8. Genes Dev 2003;17:2648-63.
    • (2003) Genes Dev , vol.17 , pp. 2648-2663
    • Henry, K.W.1    Wyce, A.2    Lo, W.S.3    Duggan, L.J.4    Emre, N.C.5    Kao, C.F.6
  • 7
    • 33749487778 scopus 로고    scopus 로고
    • The mRNA export factor Sus1 is involved in Spt/ Ada/ Gcn5 acetyltransferase-mediated H2B deubiquitinylationthrough its interaction with Ubp8 and Sgf11
    • Kohler A, Garcia PP, Llopis A, Zapater M, Posas F, Hurt E,et al. The mRNA export factor Sus1 is involved in Spt/Ada/ Gcn5 acetyltransferase-mediated H2B deubiquitinylationthrough its interaction with Ubp8 and Sgf11. Mol Biol Cell 2006;17:4228-36.
    • (2006) Mol Biol Cell , vol.17 , pp. 4228-4236
    • Kohler, A.1    Garcia, P.P.2    Llopis, A.3    Zapater, M.4    Posas, F.5    Hurt, E.6
  • 8
    • 44649179312 scopus 로고    scopus 로고
    • Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export
    • Kohler A, Schneider M, Cabal GG, Nehrbass U, Hurt E. Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export. Nat Cell Biol 2008;10:707-15.
    • (2008) Nat Cell Biol , vol.10 , pp. 707-715
    • Kohler, A.1    Schneider, M.2    Cabal, G.G.3    Nehrbass, U.4    Hurt, E.5
  • 10
    • 2942744859 scopus 로고    scopus 로고
    • H2B ubiquitylation and deubiquitylation in gene activation
    • Wyce A, Henry KW, Berger SL. H2B ubiquitylation and deubiquitylation in gene activation. Novartis Found Symp 2004; 259:63-73.
    • (2004) Novartis Found Symp , vol.259 , pp. 63-73
    • Wyce, A.1    Henry, K.W.2    Berger, S.L.3
  • 11
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk K, Recht J, Osley MA. Rad6-dependent ubiquitination of histone H2B in yeast. Science 2000;287:501-4.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 13
    • 36849046285 scopus 로고    scopus 로고
    • Histone crosstalk between H2B monoubiquitination and H3 methylation mediated by COMPASS
    • Lee JS, Shukla A, Schneider J, Swanson SK, Washburn MP, Florens L, et al. Histone crosstalk between H2B monoubiquitination and H3 methylation mediated by COMPASS. Cell 2007;131:1084-96.
    • (2007) Cell , vol.131 , pp. 1084-1096
    • Lee, J.S.1    Shukla, A.2    Schneider, J.3    Swanson, S.K.4    Washburn, M.P.5    Florens, L.6
  • 14
    • 24944520025 scopus 로고    scopus 로고
    • Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression
    • Schneider J, Wood A, Lee JS, Schuster R, Dueker J, Maguire C, et al. Molecular regulation of histone H3 trimethylation by COMPASS and the regulation of gene expression. Mol Cell2005;19:849-56.
    • (2005) Mol Cell , vol.19 , pp. 849-856
    • Schneider, J.1    Wood, A.2    Lee, J.S.3    Schuster, R.4    Dueker, J.5    Maguire, C.6
  • 15
    • 0345826106 scopus 로고    scopus 로고
    • Deubiquitination of histone H2B by a yeast acetyltransferase complex regulates transcription
    • Daniel JA, Torok MS, Sun ZW, Schieltz D, Allis CD, Yates JR, et al. Deubiquitination of histone H2B by a yeast acetyltransferase complex regulates transcription. J Biol Chem 2004; 279:1867-71.
    • (2004) J Biol Chem , vol.279 , pp. 1867-1871
    • Daniel, J.A.1    Torok, M.S.2    Sun, Z.W.3    Schieltz, D.4    Allis, C.D.5    Yates, J.R.6
  • 16
    • 72949102636 scopus 로고    scopus 로고
    • Dissection of USP catalytic domains reveals five common insertion points
    • Ye Y, Scheel H, Hofmann K, Komander D. Dissection of USP catalytic domains reveals five common insertion points. Mol Biosyst 2009;5:1797-808.
    • (2009) Mol Biosyst , vol.5 , pp. 1797-1808
    • Ye, Y.1    Scheel, H.2    Hofmann, K.3    Komander, D.4
  • 17
    • 12844277462 scopus 로고    scopus 로고
    • The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex
    • Lee KK, Florens L, Swanson SK, Washburn MP, Workman JL. The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex. Mol Cell Biol 2005;25:1173-82.
    • (2005) Mol Cell Biol , vol.25 , pp. 1173-1182
    • Lee, K.K.1    Florens, L.2    Swanson, S.K.3    Washburn, M.P.4    Workman, J.L.5
  • 18
    • 77952519938 scopus 로고    scopus 로고
    • Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module
    • Kohler A, Zimmerman E, Schneider M, Hurt E, Zheng N. Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module. Cell 2010;141:606-17.
    • (2010) Cell , vol.141 , pp. 606-617
    • Kohler, A.1    Zimmerman, E.2    Schneider, M.3    Hurt, E.4    Zheng, N.5
  • 19
    • 77953060092 scopus 로고    scopus 로고
    • Structural insights into the assembly and functionof the SAGA deubiquitinating module
    • Samara NL, Datta AB, Berndsen CE, Zhang X, Yao T, Cohen RE, et al. Structural insights into the assembly and functionof the SAGA deubiquitinating module. Science 2010;328: 1025-9.
    • (2010) Science , vol.328 , pp. 1025-1029
    • Samara, N.L.1    Datta, A.B.2    Berndsen, C.E.3    Zhang, X.4    Yao, T.5    Cohen, R.E.6
  • 20
    • 84864848052 scopus 로고    scopus 로고
    • A role for intersubunit interactions in maintaining SAGA deubiquitinating module structure and activity
    • Samara NL, Ringel AE, Wolberger C. A role for intersubunit interactions in maintaining SAGA deubiquitinating module structure and activity. Structure 2012;20:1414-24.
    • (2012) Structure , vol.20 , pp. 1414-1424
    • Samara, N.L.1    Ringel, A.E.2    Wolberger, C.3
  • 21
    • 33846021632 scopus 로고    scopus 로고
    • Amino-terminal dimerization, NRDP1- rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)
    • Avvakumov GV, Walker JR, Xue S, Finerty PJ, Mackenzie F, Newman EM, et al. Amino-terminal dimerization, NRDP1- rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J BiolChem 2006;281:38061-70.
    • (2006) J BiolChem , vol.281 , pp. 38061-38070
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3    Finerty, P.J.4    Mackenzie, F.5    Newman, E.M.6
  • 22
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu M, Li P, Li M, Li W, Yao T, WU JW, et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 2002;111:1041-54.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Jw, W.U.6
  • 23
    • 80053594090 scopus 로고    scopus 로고
    • Mechanism of USP7/HAUSP activation by its Cterminalubiquitin-like domain and allosteric regulation byGMPsynthetase
    • Faesen AC, Dirac AM, Shanmugham A, Ovaa H, Perrakis A, Sixma TK. Mechanism of USP7/HAUSP activation by its Cterminalubiquitin-like domain and allosteric regulation byGMPsynthetase. Mol Cell 2011;44:147-59.]
    • (2011) Mol Cell , vol.44 , pp. 147-159
    • Faesen, A.C.1    Dirac, A.M.2    Shanmugham, A.3    Ovaa, H.4    Perrakis, A.5    Sixma, T.K.6
  • 24
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanisticstudies on the hydrolysis of ubiquitin C-terminal 7-amido-4- methylcoumarin by deubiquitinating enzymes
    • Dang LC, Melandri FD, Stein RL. Kinetic and mechanisticstudies on the hydrolysis of ubiquitin C-terminal 7-amido-4- methylcoumarin by deubiquitinating enzymes. Biochemistry1998;37:1868-79.
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 25
    • 84857657088 scopus 로고    scopus 로고
    • The combined use of the Thermofluor assay and ThermoQ analytical software for the determination ofprotein stability and buffer optimization as an aid in protein crystallization
    • Phillips K, de la Pena AH. The combined use of the Thermofluor assay and ThermoQ analytical software for the determination ofprotein stability and buffer optimization as an aid in protein crystallization. Curr Protoc Mol Biol 2011. http://dx.doi.org/10. 1002/0471142727.mb1028s94.
    • (2011) Curr Protoc Mol Biol
    • Phillips, K.1    De La Pena, A.H.2
  • 26
    • 50949126350 scopus 로고    scopus 로고
    • Protein partners of deubiquitinating enzymes
    • Ventii KH, Wilkinson KD. Protein partners of deubiquitinating enzymes. Biochem J 2008;414:161-75.
    • (2008) Biochem J , vol.414 , pp. 161-175
    • Ventii, K.H.1    Wilkinson, K.D.2
  • 27
    • 84900397992 scopus 로고    scopus 로고
    • Mechanisms for regulating deubiquitinating enzymes
    • Wolberger C. Mechanisms for regulating deubiquitinating enzymes. Protein Sci 2014;23:344-53.
    • (2014) Protein Sci , vol.23 , pp. 344-353
    • Wolberger, C.1
  • 28
    • 65249186662 scopus 로고    scopus 로고
    • Polyubiquitin binding and disassembly by deubiquitinating enzymes
    • Reyes-Turcu FE, Wilkinson KD. Polyubiquitin binding and disassembly by deubiquitinating enzymes. Chem Rev 2009; 109:1495-508.
    • (2009) Chem Rev , vol.109 , pp. 1495-1508
    • Reyes-Turcu, F.E.1    Wilkinson, K.D.2
  • 30
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma R, Aravind L, Oania R, Mcdonald WH, et al. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 2002;298:611-5.
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4
  • 31
    • 33748188085 scopus 로고    scopus 로고
    • Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1
    • Yao T, Song L, Xu W, Demartino GN, Florens L, Swanson SK, et al. Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nat Cell Biol 2006;8:994-1002.
    • (2006) Nat Cell Biol , vol.8 , pp. 994-1002
    • Yao, T.1    Song, L.2    Xu, W.3    Demartino, G.N.4    Florens, L.5    Swanson, S.K.6
  • 32
    • 77951247308 scopus 로고    scopus 로고
    • WDR20 regulates activity of the USP12 × UAF1 deubiquitinating enzyme complex
    • Kee Y, Yang K, Cohn MA, Haas W, Gygi SP, D'Andrea AD. WDR20 regulates activity of the USP12 × UAF1 deubiquitinating enzyme complex. J Biol Chem 2010;285:11252-7.
    • (2010) J Biol Chem , vol.285 , pp. 11252-11257
    • Kee, Y.1    Yang, K.2    Cohn, M.A.3    Haas, W.4    Gygi, S.P.5    D'Andrea, A.D.6
  • 33
    • 64149129169 scopus 로고    scopus 로고
    • UAF1 is a subunit of multiple deubiquitinating enzyme complexes
    • Cohn MA, Kee Y, Haas W, Gygi SP, D'Andrea AD. UAF1 is a subunit of multiple deubiquitinating enzyme complexes. J Biol Chem 2009;284:5343-51.
    • (2009) J Biol Chem , vol.284 , pp. 5343-5351
    • Cohn, M.A.1    Kee, Y.2    Haas, W.3    Gygi, S.P.4    D'Andrea, A.D.5
  • 34
    • 36749082959 scopus 로고    scopus 로고
    • A UAF1-containing multisubunit protein complexregulates the Fanconi anemia pathway
    • Cohn MA, Kowal P, Yang K, Haas W, Huang TT, Gygi SP, et al. A UAF1-containing multisubunit protein complexregulates the Fanconi anemia pathway. Mol Cell 2007;28: 786-97.
    • (2007) Mol Cell , vol.28 , pp. 786-797
    • Cohn, M.A.1    Kowal, P.2    Yang, K.3    Haas, W.4    Huang, T.T.5    Gygi, S.P.6
  • 36
    • 38149068875 scopus 로고    scopus 로고
    • A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing
    • Zhao Y, Lang G, Ito S, Bonnet J, Metzger E, Sawatsubashi S, et al. A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing. Mol Cell 2008;29:92-101.
    • (2008) Mol Cell , vol.29 , pp. 92-101
    • Zhao, Y.1    Lang, G.2    Ito, S.3    Bonnet, J.4    Metzger, E.5    Sawatsubashi, S.6
  • 37
    • 38149078715 scopus 로고    scopus 로고
    • The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression
    • Zhang XY, Varthi M, Skyes SM, Phillips C, Warzecha C, Zhu W, et al. The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression. Mol Cell 2008;29: 102-11.
    • (2008) Mol Cell , vol.29 , pp. 102-111
    • Zhang, X.Y.1    Varthi, M.2    Skyes, S.M.3    Phillips, C.4    Warzecha, C.5    Zhu, W.6
  • 38
    • 80052597874 scopus 로고    scopus 로고
    • The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements
    • Lang G, Bonnet J, Umlauf D, Karmodiya K, Koffler J, Stierle M, et al. The tightly controlled deubiquitination activity of the human SAGA complex differentially modifies distinct gene regulatory elements. Mol Cell Biol 2011;31:3734-44.
    • (2011) Mol Cell Biol , vol.31 , pp. 3734-3744
    • Lang, G.1    Bonnet, J.2    Umlauf, D.3    Karmodiya, K.4    Koffler, J.5    Stierle, M.6
  • 39
    • 45849133054 scopus 로고    scopus 로고
    • USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A
    • Zhang XY, Pfeiffer HK, Thorne AW, McMahon SB. USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A. Cell Cycle 2008;7:1522-4.
    • (2008) Cell Cycle , vol.7 , pp. 1522-1524
    • Zhang, X.Y.1    Pfeiffer, H.K.2    Thorne, A.W.3    McMahon, S.B.4
  • 40
    • 79952030196 scopus 로고    scopus 로고
    • Aberrant expression of USP22 is associated with liver metastasis and poor prognosis of colorectal cancer
    • Liu YL, Yang YM, Xu, H, Dong XS. Aberrant expression of USP22 is associated with liver metastasis and poor prognosis of colorectal cancer. J Surg Oncol 2011;103: 283-9.
    • (2011) J Surg Oncol , vol.103 , pp. 283-289
    • Liu, Y.L.1    Yang, Y.M.2    Xu, H.3    Dong, X.S.4
  • 41
    • 84899089765 scopus 로고    scopus 로고
    • Ubiquitinspecific protease 22: A novel molecular biomarker in cervical cancer prognosis and therapeutics
    • Yang M, Liu YD, Wang YY, Liu TB, Ge TT, Lou G. Ubiquitinspecific protease 22: a novel molecular biomarker in cervical cancer prognosis and therapeutics. Tumour Biol 2014;35: 929-34.
    • (2014) Tumour Biol , vol.35 , pp. 929-934
    • Yang, M.1    Liu, Y.D.2    Wang, Y.Y.3    Liu, T.B.4    Ge, T.T.5    Lou, G.6
  • 42
    • 80052248649 scopus 로고    scopus 로고
    • Estrogen-dependent gene transcription in human breast cancer cells relies upon proteasome-dependentmonoubiquitination of histone H2B
    • Prenzel T, Prenzel-Nahrmann YB, Kramer F, Hennion M, Hsu C, Gorsler T, et al. Estrogen-dependent gene transcription in human breast cancer cells relies upon proteasome-dependentmonoubiquitination of histone H2B. Cancer Res 2011;71: 5739-53.
    • (2011) Cancer Res , vol.71 , pp. 5739-5753
    • Prenzel, T.1    Prenzel-Nahrmann, Y.B.2    Kramer, F.3    Hennion, M.4    Hsu, C.5    Gorsler, T.6
  • 43
    • 84856107676 scopus 로고    scopus 로고
    • The tumor suppressor CDC73 interacts with the ring finger proteins RNF20 andRNF40 and is required for themaintenance of histone 2B monoubiquitination
    • Hahn MA, Dickson KA, Jackson S, Clarkson A, Gill AJ, Marsh DJ. The tumor suppressor CDC73 interacts with the ring finger proteins RNF20 andRNF40 and is required for themaintenance of histone 2B monoubiquitination. Hum MolGenet 2012;21:559-68.
    • (2012) Hum MolGenet , vol.21 , pp. 559-568
    • Hahn, M.A.1    Dickson, K.A.2    Jackson, S.3    Clarkson, A.4    Gill, A.J.5    Marsh, D.J.6
  • 44
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinase
    • Komander D, Clague MJ, Urbe S. Breaking the chains: structure and function of the deubiquitinase. Nat Rev Mol Cell Biol 2009;10:550-63.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3


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