메뉴 건너뛰기




Volumn 23, Issue 5, 2015, Pages 921-928

Architecture of the ubiquitylation module of the yeast Ccr4-Not complex

Author keywords

[No Author keywords available]

Indexed keywords

CCR4 PROTEIN, S CEREVISIAE; CDC36 PROTEIN, S CEREVISIAE; CDC39 PROTEIN, S CEREVISIAE; CELL CYCLE PROTEIN; MOT2 PROTEIN, S CEREVISIAE; PROTEIN BINDING; REPRESSOR PROTEIN; RIBONUCLEASE; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSCRIPTION FACTOR; UBC4 PROTEIN, S CEREVISIAE; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE;

EID: 84930191835     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.03.011     Document Type: Article
Times cited : (33)

References (51)
  • 3
    • 0032874875 scopus 로고    scopus 로고
    • The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5
    • Y. Bai, C. Salvadore, Y.C. Chiang, M.A. Collart, H.Y. Liu, and C.L. Denis The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5 Mol. Cell. Biol. 19 1999 6642 6651
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6642-6651
    • Bai, Y.1    Salvadore, C.2    Chiang, Y.C.3    Collart, M.A.4    Liu, H.Y.5    Denis, C.L.6
  • 4
    • 84868094761 scopus 로고    scopus 로고
    • Architecture of the nuclease module of the yeast Ccr4-not complex: The Not1-Caf1-Ccr4 interaction
    • J. Basquin, V.V. Roudko, M. Rode, C. Basquin, B. Séraphin, and E. Conti Architecture of the nuclease module of the yeast Ccr4-not complex: the Not1-Caf1-Ccr4 interaction Mol. Cell 48 2012 207 218
    • (2012) Mol. Cell , vol.48 , pp. 207-218
    • Basquin, J.1    Roudko, V.V.2    Rode, M.3    Basquin, C.4    Séraphin, B.5    Conti, E.6
  • 5
    • 84874586399 scopus 로고    scopus 로고
    • NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain
    • P. Bawankar, B. Loh, L. Wohlbold, S. Schmidt, and E. Izaurralde NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT complex that docks onto the NOT1 N-terminal domain RNA Biol. 10 2013 228 244
    • (2013) RNA Biol. , vol.10 , pp. 228-244
    • Bawankar, P.1    Loh, B.2    Wohlbold, L.3    Schmidt, S.4    Izaurralde, E.5
  • 6
    • 84898869373 scopus 로고    scopus 로고
    • Structural basis for the Nanos-mediated recruitment of the CCR4-NOT complex and translational repression
    • D. Bhandari, T. Raisch, O. Weichenrieder, S. Jonas, and E. Izaurralde Structural basis for the Nanos-mediated recruitment of the CCR4-NOT complex and translational repression Genes Dev. 28 2014 888 901
    • (2014) Genes Dev. , vol.28 , pp. 888-901
    • Bhandari, D.1    Raisch, T.2    Weichenrieder, O.3    Jonas, S.4    Izaurralde, E.5
  • 9
    • 80053580757 scopus 로고    scopus 로고
    • GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets
    • J.E. Braun, E. Huntzinger, M. Fauser, and E. Izaurralde GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets Mol. Cell 44 2011 120 133
    • (2011) Mol. Cell , vol.44 , pp. 120-133
    • Braun, J.E.1    Huntzinger, E.2    Fauser, M.3    Izaurralde, E.4
  • 12
    • 0035824883 scopus 로고    scopus 로고
    • Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex
    • J. Chen, J. Rappsilber, Y.C. Chiang, P. Russell, M. Mann, and C.L. Denis Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex J. Mol. Biol. 314 2001 683 694
    • (2001) J. Mol. Biol. , vol.314 , pp. 683-694
    • Chen, J.1    Rappsilber, J.2    Chiang, Y.C.3    Russell, P.4    Mann, M.5    Denis, C.L.6
  • 14
    • 0028268566 scopus 로고
    • NOT1(CDC39), NOT2(CDC36), NOT3, and NOT4 encode a global-negative regulator of transcription that differentially affects TATA-element utilization
    • M.A. Collart, and K. Struhl NOT1(CDC39), NOT2(CDC36), NOT3, and NOT4 encode a global-negative regulator of transcription that differentially affects TATA-element utilization Genes Dev. 8 1994 525 537
    • (1994) Genes Dev. , vol.8 , pp. 525-537
    • Collart, M.A.1    Struhl, K.2
  • 15
    • 0027788114 scopus 로고
    • Tertiary structures of class i ubiquitin-conjugating enzymes are highly conserved: Crystal structure of yeast Ubc4
    • W.J. Cook, L.C. Jeffrey, Y. Xu, and V. Chau Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: crystal structure of yeast Ubc4 Biochemistry 32 1993 13809 13817
    • (1993) Biochemistry , vol.32 , pp. 13809-13817
    • Cook, W.J.1    Jeffrey, L.C.2    Xu, Y.3    Chau, V.4
  • 16
    • 84861211197 scopus 로고    scopus 로고
    • Oxidative-stress-induced nuclear to cytoplasmic relocalization is required for Not4-dependent cyclin C destruction
    • K.F. Cooper, M.S. Scarnati, E. Krasley, M.J. Mallory, C. Jin, M.J. Law, and R. Strich Oxidative-stress-induced nuclear to cytoplasmic relocalization is required for Not4-dependent cyclin C destruction J. Cell Sci. 125 2012 1015 1026
    • (2012) J. Cell Sci. , vol.125 , pp. 1015-1026
    • Cooper, K.F.1    Scarnati, M.S.2    Krasley, E.3    Mallory, M.J.4    Jin, C.5    Law, M.J.6    Strich, R.7
  • 17
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • K. Cowtan The Buccaneer software for automated model building. 1. Tracing protein chains Acta Crystallogr. D Biol. Crystallogr. 62 2006 1002 1011
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 18
    • 0035875115 scopus 로고    scopus 로고
    • The yeast POP2 gene encodes a nuclease involved in mRNA deadenylation
    • M.C. Daugeron, F. Mauxion, and B. Séraphin The yeast POP2 gene encodes a nuclease involved in mRNA deadenylation Nucleic Acids Res. 29 2001 2448 2455
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2448-2455
    • Daugeron, M.C.1    Mauxion, F.2    Séraphin, B.3
  • 19
    • 66849136862 scopus 로고    scopus 로고
    • Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome
    • L.N. Dimitrova, K. Kuroha, T. Tatematsu, and T. Inada Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome J. Biol. Chem. 284 2009 10343 10352
    • (2009) J. Biol. Chem. , vol.284 , pp. 10343-10352
    • Dimitrova, L.N.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 20
    • 1842607157 scopus 로고    scopus 로고
    • Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches
    • C. Dominguez, A.M.J.J. Bonvin, G.S. Winkler, F.M.A. van Schaik, H.T.M. Timmers, and R. Boelens Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches Structure 12 2004 633 644
    • (2004) Structure , vol.12 , pp. 633-644
    • Dominguez, C.1    Bonvin, A.M.J.J.2    Winkler, G.S.3    Van Schaik, F.M.A.4    Timmers, H.T.M.5    Boelens, R.6
  • 21
    • 0028304670 scopus 로고
    • Ccr4 is a glucose-regulated transcription factor whose leucine-rich repeat binds several proteins important for placing Ccr4 in its proper promoter context
    • M.P. Draper, H.Y. Liu, A.H. Nelsbach, S.P. Mosley, and C.L. Denis Ccr4 is a glucose-regulated transcription factor whose leucine-rich repeat binds several proteins important for placing Ccr4 in its proper promoter context Mol. Cell. Biol. 14 1994 4522 4531
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4522-4531
    • Draper, M.P.1    Liu, H.Y.2    Nelsbach, A.H.3    Mosley, S.P.4    Denis, C.L.5
  • 27
    • 84864560759 scopus 로고    scopus 로고
    • Proteolytic degradation of the Yap1 transcription factor is regulated by subcellular localization and the E3 ubiquitin ligase Not4
    • K. Gulshan, B. Thommandru, and W.S. Moye-Rowley Proteolytic degradation of the Yap1 transcription factor is regulated by subcellular localization and the E3 ubiquitin ligase Not4 J. Biol. Chem. 287 2012 26796 26805
    • (2012) J. Biol. Chem. , vol.287 , pp. 26796-26805
    • Gulshan, K.1    Thommandru, B.2    Moye-Rowley, W.S.3
  • 28
    • 0035971097 scopus 로고    scopus 로고
    • The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers
    • H. Hanzawa, M.J. de Ruwe, T.K. Albert, P.C. van Der Vliet, H.T. Timmers, and R. Boelens The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers J. Biol. Chem. 276 2001 10185 10190
    • (2001) J. Biol. Chem. , vol.276 , pp. 10185-10190
    • Hanzawa, H.1    De Ruwe, M.J.2    Albert, T.K.3    Van Der Vliet, P.C.4    Timmers, H.T.5    Boelens, R.6
  • 29
    • 84893761159 scopus 로고    scopus 로고
    • Structure of the human FANCL RING-Ube2T complex reveals determinants of cognate E3-E2 selection
    • C. Hodson, A. Purkiss, J.A. Miles, and H. Walden Structure of the human FANCL RING-Ube2T complex reveals determinants of cognate E3-E2 selection Structure 22 2014 337 344
    • (2014) Structure , vol.22 , pp. 337-344
    • Hodson, C.1    Purkiss, A.2    Miles, J.A.3    Walden, H.4
  • 31
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 34
    • 0037169544 scopus 로고    scopus 로고
    • Interaction between Not1p, a component of the Ccr4-not complex, a global regulator of transcription, and Dhh1p, a putative RNA helicase
    • L. Maillet, and M.A. Collart Interaction between Not1p, a component of the Ccr4-not complex, a global regulator of transcription, and Dhh1p, a putative RNA helicase J. Biol. Chem. 277 2002 2835 2842
    • (2002) J. Biol. Chem. , vol.277 , pp. 2835-2842
    • Maillet, L.1    Collart, M.A.2
  • 36
    • 84891145553 scopus 로고    scopus 로고
    • Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast
    • R. Matsuda, K. Ikeuchi, S. Nomura, and T. Inada Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast Genes Cells 19 2014 1 12
    • (2014) Genes Cells , vol.19 , pp. 1-12
    • Matsuda, R.1    Ikeuchi, K.2    Nomura, S.3    Inada, T.4
  • 37
    • 84874594044 scopus 로고    scopus 로고
    • C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complex
    • F. Mauxion, B. Prève, and B. Séraphin C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT complex RNA Biol. 10 2013 267 276
    • (2013) RNA Biol. , vol.10 , pp. 267-276
    • Mauxion, F.1    Prève, B.2    Séraphin, B.3
  • 39
    • 65249123408 scopus 로고    scopus 로고
    • Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression
    • D.P. Mersman, H.-N. Du, I.M. Fingerman, P.F. South, and S.D. Briggs Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression Genes Dev. 23 2009 951 962
    • (2009) Genes Dev. , vol.23 , pp. 951-962
    • Mersman, D.P.1    Du, H.-N.2    Fingerman, I.M.3    South, P.F.4    Briggs, S.D.5
  • 40
    • 34548548790 scopus 로고    scopus 로고
    • Modulation of Ubc4p/Ubc5p-mediated stress responses by the RING-finger-dependent ubiquitin-protein ligase Not4p in Saccharomyces cerevisiae
    • K.W. Mulder, A. Inagaki, E. Cameroni, F. Mousson, G.S. Winkler, C. De Virgilio, M.A. Collart, and H.T.M. Timmers Modulation of Ubc4p/Ubc5p-mediated stress responses by the RING-finger-dependent ubiquitin-protein ligase Not4p in Saccharomyces cerevisiae Genetics 176 2007 181 192
    • (2007) Genetics , vol.176 , pp. 181-192
    • Mulder, K.W.1    Inagaki, A.2    Cameroni, E.3    Mousson, F.4    Winkler, G.S.5    De Virgilio, C.6    Collart, M.A.7    Timmers, H.T.M.8
  • 42
    • 84905668594 scopus 로고    scopus 로고
    • The role of the E3 ligase Not4 in cotranslational quality control
    • O.O. Panasenko The role of the E3 ligase Not4 in cotranslational quality control Front. Genet. 5 2014 141
    • (2014) Front. Genet. , vol.5 , pp. 141
    • Panasenko, O.O.1
  • 43
    • 79953150421 scopus 로고    scopus 로고
    • Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29
    • O.O. Panasenko, and M.A. Collart Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29 Mol. Cell. Biol. 31 2011 1610 1623
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1610-1623
    • Panasenko, O.O.1    Collart, M.A.2
  • 44
    • 84856026751 scopus 로고    scopus 로고
    • Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligase
    • O.O. Panasenko, and M.A. Collart Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligase Mol. Microbiol. 83 2012 640 653
    • (2012) Mol. Microbiol. , vol.83 , pp. 640-653
    • Panasenko, O.O.1    Collart, M.A.2
  • 45
    • 33846008044 scopus 로고    scopus 로고
    • The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex
    • O. Panasenko, E. Landrieux, M. Feuermann, A. Finka, N. Paquet, and M.A. Collart The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex J. Biol. Chem. 281 2006 31389 31398
    • (2006) J. Biol. Chem. , vol.281 , pp. 31389-31398
    • Panasenko, O.1    Landrieux, E.2    Feuermann, M.3    Finka, A.4    Paquet, N.5    Collart, M.A.6
  • 46
    • 84870622730 scopus 로고    scopus 로고
    • The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex
    • A.P. Petit, L. Wohlbold, P. Bawankar, E. Huntzinger, S. Schmidt, E. Izaurralde, and O. Weichenrieder The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex Nucleic Acids Res. 40 2012 11058 11072
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11058-11072
    • Petit, A.P.1    Wohlbold, L.2    Bawankar, P.3    Huntzinger, E.4    Schmidt, S.5    Izaurralde, E.6    Weichenrieder, O.7
  • 47
    • 79960928455 scopus 로고    scopus 로고
    • Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin
    • H. Sandler, J. Kreth, H.T.M. Timmers, and G. Stoecklin Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin Nucleic Acids Res. 39 2011 4373 4386
    • (2011) Nucleic Acids Res. , vol.39 , pp. 4373-4386
    • Sandler, H.1    Kreth, J.2    Timmers, H.T.M.3    Stoecklin, G.4
  • 48
    • 77649252314 scopus 로고    scopus 로고
    • NANOS2 interacts with the CCR4-NOT deadenylation complex and leads to suppression of specific RNAs
    • A. Suzuki, K. Igarashi, K.-I. Aisaki, J. Kanno, and Y. Saga NANOS2 interacts with the CCR4-NOT deadenylation complex and leads to suppression of specific RNAs Proc. Natl. Acad. Sci. USA 107 2010 3594 3599
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 3594-3599
    • Suzuki, A.1    Igarashi, K.2    Aisaki, K.-I.3    Kanno, J.4    Saga, Y.5
  • 50
    • 0037086657 scopus 로고    scopus 로고
    • Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae
    • M. Tucker, R.R. Staples, M.A. Valencia-Sanchez, D. Muhlrad, and R. Parker Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae EMBO J. 21 2002 1427 1436
    • (2002) EMBO J. , vol.21 , pp. 1427-1436
    • Tucker, M.1    Staples, R.R.2    Valencia-Sanchez, M.A.3    Muhlrad, D.4    Parker, R.5
  • 51
    • 84877801967 scopus 로고    scopus 로고
    • RNA decay machines: Deadenylation by the Ccr4-Not and Pan2-Pan3 complexes
    • E. Wahle, and S. Winkler RNA decay machines: deadenylation by the Ccr4-Not and Pan2-Pan3 complexes Biochim. Biophys. Acta 1829 2013 561 570
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 561-570
    • Wahle, E.1    Winkler, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.