메뉴 건너뛰기




Volumn 38, Issue 3, 2009, Pages 789-796

The hydrophobic patch of ubiquitin is required to protect transactivator-promoter complexes from destabilization by the proteasomal ATPases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; LYSINE; PROTEASOME; TRANSCRIPTION FACTOR GAL4; UBIQUITIN; DNA BINDING PROTEIN; GAL4 PROTEIN, S CEREVISIAE; ISOLEUCINE; RPT1 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSACTIVATOR PROTEIN; TRANSCRIPTION FACTOR;

EID: 77950342666     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp1066     Document Type: Article
Times cited : (9)

References (40)
  • 1
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: paradigm of a self-compartmentalizing protease
    • Baumeister,W., Walz,J., Zuhl,F. and Seemuller,E. (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell, 92, 367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 2
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier,M., Staszewski,L.M. and Bohmann,D. (1994) Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell, 78, 787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 3
    • 0028205667 scopus 로고
    • Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway
    • Chowdary,D.R., Dermody,J.J., Jha,K.K. and Ozer,H.L. (1994) Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol. Cell. Biol., 14, 1997-2003.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1997-2003
    • Chowdary, D.R.1    Dermody, J.J.2    Jha, K.K.3    Ozer, H.L.4
  • 4
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc
    • Salghetti,S.E., Kim,S.Y. and Tansey,W.P. (1999) Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc. EMBO J., 18, 717-726.
    • (1999) EMBO J. , vol.18 , pp. 717-726
    • Salghetti, S.E.1    Kim, S.Y.2    Tansey, W.P.3
  • 5
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella,V.J., Rando,O.J., Goldberg,A.L. and Maniatis,T. (1994) The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell, 78, 773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 7
    • 33644857820 scopus 로고    scopus 로고
    • Genomic association of the proteasome demonstrates overlapping gene regulatory activity with transcription factor substrates
    • Auld,K.L., Brown,C.R., Casolari,J.M., Komili,S. and Silver,P.A. (2006) Genomic association of the proteasome demonstrates overlapping gene regulatory activity with transcription factor substrates. Mol. Cell, 21, 861-871.
    • (2006) Mol. Cell , vol.21 , pp. 861-871
    • Auld, K.L.1    Brown, C.R.2    Casolari, J.M.3    Komili, S.4    Silver, P.A.5
  • 8
    • 33748753648 scopus 로고    scopus 로고
    • Widespread, but non-identical, association of proteasomal 19 and 20 S proteins with yeast chromatin
    • Sikder,D., Johnston,S.A. and Kodadek,T. (2006) Widespread, but non-identical, association of proteasomal 19 and 20 S proteins with yeast chromatin. J. Biol. Chem., 281, 27346-27355.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27346-27355
    • Sikder, D.1    Johnston, S.A.2    Kodadek, T.3
  • 9
    • 27544486193 scopus 로고    scopus 로고
    • The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators
    • Lee,D., Ezhkova,E., Li,B., Pattenden,S.G., Tansey,W.P. and Workman,J.L. (2005) The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators. Cell, 123, 423-436.
    • (2005) Cell , vol.123 , pp. 423-436
    • Lee, D.1    Ezhkova, E.2    Li, B.3    Pattenden, S.G.4    Tansey, W.P.5    Workman, J.L.6
  • 10
    • 1242271997 scopus 로고    scopus 로고
    • Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3
    • Ezhkova,E. and Tansey,W.P. (2004) Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3. Mol. Cell, 13, 435-442.
    • (2004) Mol. Cell , vol.13 , pp. 435-442
    • Ezhkova, E.1    Tansey, W.P.2
  • 11
    • 0035947238 scopus 로고    scopus 로고
    • The 19S regulatroy particle of the proteasome is required for efficient transcriiption elongation by RNZ Polymerase II
    • Ferdous,A., Gonzalez,F., Sun,L., Kodadek,T. and Johnston,S.A. (2001) The 19S regulatroy particle of the proteasome is required for efficient transcriiption elongation by RNZ Polymerase II. Mol. Cell, 7, 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
  • 12
    • 0037159223 scopus 로고    scopus 로고
    • A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA Polymerase II
    • Ferdous,A., Kodadek,T. and Johnston,S.A. (2002) A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA Polymerase II. Biochemistry, 41, 12798-12805.
    • (2002) Biochemistry , vol.41 , pp. 12798-12805
    • Ferdous, A.1    Kodadek, T.2    Johnston, S.A.3
  • 14
    • 40149102342 scopus 로고    scopus 로고
    • The 19S proteasome ATPase Sug1 plays a critical role in regulating MHC class II transcription
    • Bhat,K.P., Turner,J.D., Myers,S.E., Cape,A.D., Ting,J.P. and Greer,S.F. (2008) The 19S proteasome ATPase Sug1 plays a critical role in regulating MHC class II transcription. Mol. Immunol., 45, 2214-2224.
    • (2008) Mol. Immunol. , vol.45 , pp. 2214-2224
    • Bhat, K.P.1    Turner, J.D.2    Myers, S.E.3    Cape, A.D.4    Ting, J.P.5    Greer, S.F.6
  • 15
    • 33644993615 scopus 로고    scopus 로고
    • The proteasomal ATPase complex is required for stress-induced transcription in yeast
    • Sulahian,R., Sikder,D., Johnston,S.A. and Kodadek,T. (2006) The proteasomal ATPase complex is required for stress-induced transcription in yeast. Nucleic Acids Res., 34, 1351-1357.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1351-1357
    • Sulahian, R.1    Sikder, D.2    Johnston, S.A.3    Kodadek, T.4
  • 16
    • 29244472462 scopus 로고    scopus 로고
    • Identification of Gal4 activation domain-binding proteins in the 26S proteasome by periodate-triggered cross-linking
    • Archer,C.T., Burdine,L. and Kodadek,T. (2005) Identification of Gal4 activation domain-binding proteins in the 26S proteasome by periodate-triggered cross-linking. Mol. Biosyst., 1, 366-372.
    • (2005) Mol. Biosyst. , vol.1 , pp. 366-372
    • Archer, C.T.1    Burdine, L.2    Kodadek, T.3
  • 17
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • Fernando Gonzalez,A.D., Thomas,K. and Stephen,A.J. (2002) Recruitment of a 19S proteasome subcomplex to an activated promoter. Science, 296, 548-550.
    • (2002) Science , vol.296 , pp. 548-550
    • Fernando Gonzalez, A.D.1    Thomas, K.2    Stephen, A.J.3
  • 18
    • 33846132939 scopus 로고    scopus 로고
    • The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters
    • Ferdous,A., Sikder,D., Gillette,T., Nalley,K., Kodadek,T. and Johnston,S.A. (2007) The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters. Genes Dev., 21, 112-123.
    • (2007) Genes Dev. , vol.21 , pp. 112-123
    • Ferdous, A.1    Sikder, D.2    Gillette, T.3    Nalley, K.4    Kodadek, T.5    Johnston, S.A.6
  • 19
    • 52049114924 scopus 로고    scopus 로고
    • Physical and functional interactions of monoubiquitylated transactivators with the proteasome
    • Archer,C.T., Burdine,L., Liu,B., Ferdous,A., Johnston,S.A. and Kodadek,T. (2008) Physical and functional interactions of monoubiquitylated transactivators with the proteasome. J. Biol. Chem., 283, 21789-21798.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21789-21798
    • Archer, C.T.1    Burdine, L.2    Liu, B.3    Ferdous, A.4    Johnston, S.A.5    Kodadek, T.6
  • 20
    • 45549098595 scopus 로고    scopus 로고
    • Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo
    • Archer,C.T., Delahodde,A., Gonzalez,F., Johnston,S.A. and Kodadek,T. (2008) Activation domain-dependent monoubiquitylation of Gal4 protein is essential for promoter binding in vivo. J. Biol. Chem., 283, 12614-12623.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12614-12623
    • Archer, C.T.1    Delahodde, A.2    Gonzalez, F.3    Johnston, S.A.4    Kodadek, T.5
  • 21
    • 0029619753 scopus 로고
    • Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S protease subunit S5a
    • Deveraux,Q., van Nocker,S., Mahaffey,D., Vierstra,R. and Rechsteiner,M. (1995) Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S protease subunit S5a. J. Biol. Chem., 270, 29660-29663.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29660-29663
    • Deveraux, Q.1    van Nocker, S.2    Mahaffey, D.3    Vierstra, R.4    Rechsteiner, M.5
  • 22
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker,S., Sadis,S., Rubin,D.M., Glickman,M., Fu,H., Coux,O., Wefes,I., Finley,D. and Vierstra,R.D. (1996) The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol., 16, 6020-6028.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 23
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam,Y.A., Lawson,T.G., Velayutham,M., Zweier,J.L. and Pickart,C.M. (2002) A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature, 416, 763-767.
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.M.5
  • 26
    • 35349022538 scopus 로고    scopus 로고
    • Label transfer chemistry for the characterization of protein-protein interactions
    • Liu,B., Archer,C.T., Burdine,L., Gillette,T.G. and Kodadek,T. (2007) Label transfer chemistry for the characterization of protein-protein interactions. J. Amer. Chem. Soc., 129, 12348-12349.
    • (2007) J. Amer. Chem. Soc. , vol.129 , pp. 12348-12349
    • Liu, B.1    Archer, C.T.2    Burdine, L.3    Gillette, T.G.4    Kodadek, T.5
  • 27
    • 0035971226 scopus 로고    scopus 로고
    • Evidence that proteolysis of Gal4 cannot explain the transcriptional effects of proteasome ATPase mutations
    • Russell,S.J. and Johnston,S.A. (2001) Evidence that proteolysis of Gal4 cannot explain the transcriptional effects of proteasome ATPase mutations. J. Biol. Chem., 276, 9825-9831.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9825-9831
    • Russell, S.J.1    Johnston, S.A.2
  • 28
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma,R., Oania,R., Graumann,J. and Deshaies,R.J. (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell, 118, 99-110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 29
    • 0017251147 scopus 로고
    • Genetic co-regulation of galactose and melibiose utilization in Saccharomyces
    • Kew,O.M. and Douglas,H.C. (1976) Genetic co-regulation of galactose and melibiose utilization in Saccharomyces. J. Bacteriol., 125, 33-41.
    • (1976) J. Bacteriol. , vol.125 , pp. 33-41
    • Kew, O.M.1    Douglas, H.C.2
  • 30
    • 0028316184 scopus 로고
    • Structure of tetraubiquitin shows how multiubiquitin chains can be formed
    • Cook,W.J., Jeffrey,L.C., Kasperek,E. and Pickart,C.M. (1994) Structure of tetraubiquitin shows how multiubiquitin chains can be formed. J. Mol. Biol., 236, 601-609.
    • (1994) J. Mol. Biol. , vol.236 , pp. 601-609
    • Cook, W.J.1    Jeffrey, L.C.2    Kasperek, E.3    Pickart, C.M.4
  • 31
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • Varadan,R., Walker,O., Pickart,C. and Fushman,D. (2002) Structural properties of polyubiquitin chains in solution. J. Mol. Biol., 324, 637-647.
    • (2002) J. Mol. Biol. , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.3    Fushman, D.4
  • 35
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1 8A resolution
    • Vijay-Kumar,S., Bugg,C.E. and Cook,W.J. (1987) Structure of ubiquitin refined at 1.8A resolution. J. Mol. Biol., 194, 531-544.
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 36
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling
    • Varadan,R., Assfalg,M., Haririnia,A., Raasi,S., Pickart,C. and Fushman,D. (2004) Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. J. Biol. Chem., 279, 7055-7063.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7055-7063
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6
  • 37
    • 0030897577 scopus 로고    scopus 로고
    • The DNA binding and activation domains of Gal4p are sufficient for conveying its regulatory signals
    • Ding,W.V. and Johnston,S.A. (1997) The DNA binding and activation domains of Gal4p are sufficient for conveying its regulatory signals. Mol. Cell. Biol., 17, 2538-2549.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2538-2549
    • Ding, W.V.1    Johnston, S.A.2
  • 38
    • 0018869713 scopus 로고
    • Function of positive regulatory gene gal4 in the synthesis of galactose pathway enzymes in Saccharomyces cerevisiae: evidence that the GAL81 region codes for part of the gal4 protein
    • Matsumoto,K., Adachi,Y., Toh-e,A. and Oshima,Y. (1980) Function of positive regulatory gene gal4 in the synthesis of galactose pathway enzymes in Saccharomyces cerevisiae: evidence that the GAL81 region codes for part of the gal4 protein. J. Bacteriol., 141, 508-527.
    • (1980) J. Bacteriol. , vol.141 , pp. 508-527
    • Matsumoto, K.1    Adachi, Y.2    Toh-e, A.3    Oshima, Y.4
  • 39
    • 0141625302 scopus 로고    scopus 로고
    • Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation
    • Swanson,K.A., Kang,R.S., Stamenova,S.D., Hicke,L. and Radhakrishnan,I. (2003) Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. EMBO J., 22, 4597-4606.
    • (2003) EMBO J. , vol.22 , pp. 4597-4606
    • Swanson, K.A.1    Kang, R.S.2    Stamenova, S.D.3    Hicke, L.4    Radhakrishnan, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.