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Volumn 34, Issue 14, 2015, Pages 1905-1924

Not4-dependent translational repression is important for cellular protein homeostasis in yeast

Author keywords

Ccr4 Not complex; Not4; protein homeostasis; ribosome stalling; translational repression

Indexed keywords

MESSENGER RNA; POLYLYSINE; PROTEIN DERIVATIVE; PROTEIN NOT4; PROTEOME; UNCLASSIFIED DRUG; CAP BINDING PROTEIN; CCR4 PROTEIN, S CEREVISIAE; DCP1 PROTEIN, S CEREVISIAE; DEAD BOX PROTEIN; DHH1 PROTEIN, S CEREVISIAE; NOT4 PROTEIN, S CEREVISIAE; RIBONUCLEASE; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 84948573230     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201490194     Document Type: Article
Times cited : (44)

References (74)
  • 3
    • 0034100041 scopus 로고    scopus 로고
    • Glucose depletion rapidly inhibits translation initiation in yeast
    • Ashe MP, De Long SK, Sachs AB, (2000) Glucose depletion rapidly inhibits translation initiation in yeast. Mol Biol Cell 11: 833-848
    • (2000) Mol Biol Cell , vol.11 , pp. 833-848
    • Ashe, M.P.1    De Long, S.K.2    Sachs, A.B.3
  • 4
    • 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
    • Bai Y, Salvadore C, Chiang YC, Collart MA, Liu HY, Denis CL, (1999) The CCR4 and CAF1 proteins of the CCR4 NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5. Mol Cell Biol 19: 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
  • 5
    • 84868094761 scopus 로고    scopus 로고
    • Architecture of the nuclease module of the yeast Ccr4 not complex: The Not1-Caf1-Ccr4 interaction
    • Basquin J, Roudko VV, Rode M, Basquin C, Seraphin B, Conti E, (2012) Architecture of the nuclease module of the yeast Ccr4 not complex: the Not1-Caf1-Ccr4 interaction. Mol Cell 48: 207-218
    • (2012) Mol Cell , vol.48 , pp. 207-218
    • Basquin, J.1    Roudko, V.V.2    Rode, M.3    Basquin, C.4    Seraphin, B.5    Conti, E.6
  • 6
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson MH, Joazeiro CA, (2010) Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 467: 470-473
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 7
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann CB, Davies A, Cost GJ, Caputo E, Li J, Hieter P, Boeke JD, (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14: 115-132
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 9
    • 80053580757 scopus 로고    scopus 로고
    • GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets
    • Braun JE, Huntzinger E, Fauser M, Izaurralde E, (2011) GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets. Mol Cell 44: 120-133
    • (2011) Mol Cell , vol.44 , pp. 120-133
    • Braun, J.E.1    Huntzinger, E.2    Fauser, M.3    Izaurralde, E.4
  • 10
    • 84875465945 scopus 로고    scopus 로고
    • Positively charged residues are the major determinants of ribosomal velocity
    • Charneski CA, Hurst LD, (2013) Positively charged residues are the major determinants of ribosomal velocity. PLoS Biol 11: e1001508
    • (2013) PLoS Biol , vol.11 , pp. e1001508
    • Charneski, C.A.1    Hurst, L.D.2
  • 12
    • 0035824883 scopus 로고    scopus 로고
    • Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex
    • Chen J, Rappsilber J, Chiang YC, Russell P, Mann M, Denis CL, (2001) Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex. J Mol Biol 314: 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
  • 13
    • 84899839442 scopus 로고    scopus 로고
    • Fragile X mental retardation protein regulates translation by binding directly to the ribosome
    • Chen E, Sharma MR, Shi X, Agrawal RK, Joseph S, (2014a) Fragile X mental retardation protein regulates translation by binding directly to the ribosome. Mol Cell 54: 407-417
    • (2014) Mol Cell , vol.54 , pp. 407-417
    • Chen, E.1    Sharma, M.R.2    Shi, X.3    Agrawal, R.K.4    Joseph, S.5
  • 15
    • 0035674477 scopus 로고    scopus 로고
    • The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes
    • Coller JM, Tucker M, Sheth U, Valencia-Sanchez MA, Parker R, (2001) The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 7: 1717-1727
    • (2001) RNA , vol.7 , pp. 1717-1727
    • Coller, J.M.1    Tucker, M.2    Sheth, U.3    Valencia-Sanchez, M.A.4    Parker, R.5
  • 16
    • 25144482816 scopus 로고    scopus 로고
    • General translational repression by activators of mRNA decapping
    • Coller J, Parker R, (2005) General translational repression by activators of mRNA decapping. Cell 122: 875-886
    • (2005) Cell , vol.122 , pp. 875-886
    • Coller, J.1    Parker, R.2
  • 17
    • 57749207970 scopus 로고    scopus 로고
    • Methods to determine mRNA half-life in Saccharomyces cerevisiae
    • Coller J, (2008) Methods to determine mRNA half-life in Saccharomyces cerevisiae. Methods Enzymol 448: 267-284
    • (2008) Methods Enzymol , vol.448 , pp. 267-284
    • Coller, J.1
  • 18
    • 77956503398 scopus 로고    scopus 로고
    • Translational repression by deadenylases
    • Cooke A, Prigge A, Wickens M, (2010) Translational repression by deadenylases. J Biol Chem 285: 28506-28513
    • (2010) J Biol Chem , vol.285 , pp. 28506-28513
    • Cooke, A.1    Prigge, A.2    Wickens, M.3
  • 20
    • 66849136862 scopus 로고    scopus 로고
    • Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome
    • Dimitrova LN, Kuroha K, Tatematsu T, Inada T, (2009) Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome. J Biol Chem 284: 10343-10352
    • (2009) J Biol Chem , vol.284 , pp. 10343-10352
    • Dimitrova, L.N.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 21
    • 0035015174 scopus 로고    scopus 로고
    • Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: A putative ribosomal 'skip'
    • Donnelly ML, Luke G, Mehrotra A, Li X, Hughes LE, Gani D, Ryan MD, (2001) Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: a putative ribosomal 'skip'. J Gen Virol 82: 1013-1025
    • (2001) J Gen Virol , vol.82 , pp. 1013-1025
    • Donnelly, M.L.1    Luke, G.2    Mehrotra, A.3    Li, X.4    Hughes, L.E.5    Gani, D.6    Ryan, M.D.7
  • 24
    • 84883210213 scopus 로고    scopus 로고
    • Principles of cotranslational ubiquitination and quality control at the ribosome
    • Duttler S, Pechmann S, Frydman J, (2013) Principles of cotranslational ubiquitination and quality control at the ribosome. Mol Cell 50: 379-393
    • (2013) Mol Cell , vol.50 , pp. 379-393
    • Duttler, S.1    Pechmann, S.2    Frydman, J.3
  • 27
    • 84867847719 scopus 로고    scopus 로고
    • Surveillance pathways rescuing eukaryotic ribosomes lost in translation
    • Graille M, Seraphin B, (2012) Surveillance pathways rescuing eukaryotic ribosomes lost in translation. Nat Rev Mol Cell Biol 13: 727-735
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 727-735
    • Graille, M.1    Seraphin, B.2
  • 28
    • 84864560759 scopus 로고    scopus 로고
    • Proteolytic degradation of the Yap1 transcription factor is regulated by subcellular localization and the E3 ubiquitin ligase Not4
    • Gulshan K, Thommandru B, Moye-Rowley WS, (2012) Proteolytic degradation of the Yap1 transcription factor is regulated by subcellular localization and the E3 ubiquitin ligase Not4. J Biol Chem 287: 26796-26805
    • (2012) J Biol Chem , vol.287 , pp. 26796-26805
    • Gulshan, K.1    Thommandru, B.2    Moye-Rowley, W.S.3
  • 31
    • 84898429935 scopus 로고    scopus 로고
    • The Not4 E3 ligase and CCR4 deadenylase play distinct roles in protein quality control
    • Halter D, Collart MA, Panasenko OO, (2014) The Not4 E3 ligase and CCR4 deadenylase play distinct roles in protein quality control. PLoS ONE 9: e86218
    • (2014) PLoS ONE , vol.9 , pp. e86218
    • Halter, D.1    Collart, M.A.2    Panasenko, O.O.3
  • 32
    • 0031886351 scopus 로고    scopus 로고
    • Dhh1p, a putative RNA helicase, associates with the general transcription factors Pop2p and Ccr4p from Saccharomyces cerevisiae
    • Hata H, Mitsui H, Liu H, Bai Y, Denis CL, Shimizu Y, Sakai A, (1998) Dhh1p, a putative RNA helicase, associates with the general transcription factors Pop2p and Ccr4p from Saccharomyces cerevisiae. Genetics 148: 571-579
    • (1998) Genetics , vol.148 , pp. 571-579
    • Hata, H.1    Mitsui, H.2    Liu, H.3    Bai, Y.4    Denis, C.L.5    Shimizu, Y.6    Sakai, A.7
  • 33
    • 77956660837 scopus 로고    scopus 로고
    • Ubc4 and Not4 regulate steady-state levels of DNA polymerase-alpha to promote efficient and accurate DNA replication
    • Haworth J, Alver RC, Anderson M, Bielinsky AK, (2010) Ubc4 and Not4 regulate steady-state levels of DNA polymerase-alpha to promote efficient and accurate DNA replication. Mol Biol Cell 21: 3205-3219
    • (2010) Mol Biol Cell , vol.21 , pp. 3205-3219
    • Haworth, J.1    Alver, R.C.2    Anderson, M.3    Bielinsky, A.K.4
  • 34
    • 1642363230 scopus 로고    scopus 로고
    • Loss of translational control in yeast compromised for the major mRNA decay pathway
    • Holmes LE, Campbell SG, De Long SK, Sachs AB, Ashe MP, (2004) Loss of translational control in yeast compromised for the major mRNA decay pathway. Mol Cell Biol 24: 2998-3010
    • (2004) Mol Cell Biol , vol.24 , pp. 2998-3010
    • Holmes, L.E.1    Campbell, S.G.2    De Long, S.K.3    Sachs, A.B.4    Ashe, M.P.5
  • 35
    • 70249141564 scopus 로고    scopus 로고
    • Co-translational mRNA decay in Saccharomyces cerevisiae
    • Hu W, Sweet TJ, Chamnongpol S, Baker KE, Coller J, (2009) Co-translational mRNA decay in Saccharomyces cerevisiae. Nature 461: 225-229
    • (2009) Nature , vol.461 , pp. 225-229
    • Hu, W.1    Sweet, T.J.2    Chamnongpol, S.3    Baker, K.E.4    Coller, J.5
  • 36
    • 76349083121 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decapping occurs on polyribosomes in Saccharomyces cerevisiae
    • Hu W, Petzold C, Coller J, Baker KE, (2010) Nonsense-mediated mRNA decapping occurs on polyribosomes in Saccharomyces cerevisiae. Nat Struct Mol Biol 17: 244-247
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 244-247
    • Hu, W.1    Petzold, C.2    Coller, J.3    Baker, K.E.4
  • 37
    • 18444393975 scopus 로고    scopus 로고
    • Translation of aberrant mRNAs lacking a termination codon or with a shortened 3′-UTR is repressed after initiation in yeast
    • Inada T, Aiba H, (2005) Translation of aberrant mRNAs lacking a termination codon or with a shortened 3′-UTR is repressed after initiation in yeast. EMBO J 24: 1584-1595
    • (2005) EMBO J , vol.24 , pp. 1584-1595
    • Inada, T.1    Aiba, H.2
  • 38
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • Ingolia NT, Lareau LF, Weissman JS, (2011) Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 147: 789-802
    • (2011) Cell , vol.147 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3
  • 39
    • 33947159090 scopus 로고    scopus 로고
    • Translation of the poly(A) tail plays crucial roles in nonstop mRNA surveillance via translation repression and protein destabilization by proteasome in yeast
    • Ito-Harashima S, Kuroha K, Tatematsu T, Inada T, (2007) Translation of the poly(A) tail plays crucial roles in nonstop mRNA surveillance via translation repression and protein destabilization by proteasome in yeast. Genes Dev 21: 519-524
    • (2007) Genes Dev , vol.21 , pp. 519-524
    • Ito-Harashima, S.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 40
    • 34248580923 scopus 로고    scopus 로고
    • Translational control of maternal Cyclin B mRNA by Nanos in the Drosophila germline
    • Kadyrova LY, Habara Y, Lee TH, Wharton RP, (2007) Translational control of maternal Cyclin B mRNA by Nanos in the Drosophila germline. Development 134: 1519-1527
    • (2007) Development , vol.134 , pp. 1519-1527
    • Kadyrova, L.Y.1    Habara, Y.2    Lee, T.H.3    Wharton, R.P.4
  • 41
    • 77950562866 scopus 로고    scopus 로고
    • A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes
    • Koplin A, Preissler S, Ilina Y, Koch M, Scior A, Erhardt M, Deuerling E, (2010) A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J Cell Biol 189: 57-68
    • (2010) J Cell Biol , vol.189 , pp. 57-68
    • Koplin, A.1    Preissler, S.2    Ilina, Y.3    Koch, M.4    Scior, A.5    Erhardt, M.6    Deuerling, E.7
  • 44
    • 34247574716 scopus 로고    scopus 로고
    • Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells
    • 160, 162
    • Liu C, Apodaca J, Davis LE, Rao H, (2007) Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells. Biotechniques 42: 158, 160, 162
    • (2007) Biotechniques , vol.42 , pp. 158
    • Liu, C.1    Apodaca, J.2    Davis, L.E.3    Rao, H.4
  • 45
    • 54249096045 scopus 로고    scopus 로고
    • Electrostatics in the ribosomal tunnel modulate chain elongation rates
    • Lu J, Deutsch C, (2008) Electrostatics in the ribosomal tunnel modulate chain elongation rates. J Mol Biol 384: 73-86
    • (2008) J Mol Biol , vol.384 , pp. 73-86
    • Lu, J.1    Deutsch, C.2
  • 46
    • 0034692875 scopus 로고    scopus 로고
    • The essential function of Not1 lies within the Ccr4-Not complex
    • Maillet L, Tu C, Hong YK, Shuster EO, Collart MA, (2000) The essential function of Not1 lies within the Ccr4-Not complex. J Mol Biol 303: 131-143
    • (2000) J Mol Biol , vol.303 , pp. 131-143
    • Maillet, L.1    Tu, C.2    Hong, Y.K.3    Shuster, E.O.4    Collart, M.A.5
  • 47
    • 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
    • Maillet L, Collart MA, (2002) 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: 2835-2842
    • (2002) J Biol Chem , vol.277 , pp. 2835-2842
    • Maillet, L.1    Collart, M.A.2
  • 49
    • 84891145553 scopus 로고    scopus 로고
    • Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast
    • Matsuda R, Ikeuchi K, Nomura S, Inada T, (2014) Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast. Genes Cells 19: 1-12
    • (2014) Genes Cells , vol.19 , pp. 1-12
    • Matsuda, R.1    Ikeuchi, K.2    Nomura, S.3    Inada, T.4
  • 50
    • 50249175909 scopus 로고    scopus 로고
    • Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins
    • Medicherla B, Goldberg AL, (2008) Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins. J Cell Biol 182: 663-673
    • (2008) J Cell Biol , vol.182 , pp. 663-673
    • Medicherla, B.1    Goldberg, A.L.2
  • 51
    • 65249123408 scopus 로고    scopus 로고
    • Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression
    • Mersman DP, Du HN, Fingerman IM, South PF, Briggs SD, (2009) Polyubiquitination of the demethylase Jhd2 controls histone methylation and gene expression. Genes Dev 23: 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
  • 52
    • 0027932513 scopus 로고
    • Premature translational termination triggers mRNA decapping
    • Muhlrad D, Parker R, (1994) Premature translational termination triggers mRNA decapping. Nature 370: 578-581
    • (1994) Nature , vol.370 , pp. 578-581
    • Muhlrad, D.1    Parker, R.2
  • 53
    • 16344395154 scopus 로고    scopus 로고
    • The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p
    • Muhlrad D, Parker R, (2005) The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p. EMBO J 24: 1033-1045
    • (2005) EMBO J , vol.24 , pp. 1033-1045
    • Muhlrad, D.1    Parker, R.2
  • 54
    • 34548548790 scopus 로고    scopus 로고
    • Modulation of Ubc4p/Ubc5p-mediated stress responses by the RING-finger-dependent ubiquitin-protein ligase Not4p in Saccharomyces cerevisiae
    • Mulder KW, Inagaki A, Cameroni E, Mousson F, Winkler GS, De Virgilio C, Collart MA, Timmers HT, (2007) Modulation of Ubc4p/Ubc5p-mediated stress responses by the RING-finger-dependent ubiquitin-protein ligase Not4p in Saccharomyces cerevisiae. Genetics 176: 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.8
  • 55
    • 77956540817 scopus 로고    scopus 로고
    • Decapping activators in Saccharomyces cerevisiae act by multiple mechanisms
    • Nissan T, Rajyaguru P, She M, Song H, Parker R, (2010) Decapping activators in Saccharomyces cerevisiae act by multiple mechanisms. Mol Cell 39: 773-783
    • (2010) Mol Cell , vol.39 , pp. 773-783
    • Nissan, T.1    Rajyaguru, P.2    She, M.3    Song, H.4    Parker, R.5
  • 56
    • 33846008044 scopus 로고    scopus 로고
    • The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex
    • Panasenko O, Landrieux E, Feuermann M, Finka A, Paquet N, Collart MA, (2006) The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complex. J Biol Chem 281: 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
  • 57
    • 84856026751 scopus 로고    scopus 로고
    • Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligase
    • Panasenko OO, Collart MA, (2012) Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligase. Mol Microbiol 83: 640-653
    • (2012) Mol Microbiol , vol.83 , pp. 640-653
    • Panasenko, O.O.1    Collart, M.A.2
  • 58
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R, Sheth U, (2007) P bodies and the control of mRNA translation and degradation. Mol Cell 25: 635-646
    • (2007) Mol Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 59
    • 84906874947 scopus 로고    scopus 로고
    • Human DDX6 effects miRNA-mediated gene silencing via direct binding to CNOT1
    • Rouya C, Siddiqui N, Morita M, Duchaine TF, Fabian MR, Sonenberg N, (2014) Human DDX6 effects miRNA-mediated gene silencing via direct binding to CNOT1. RNA 20: 1398-1409
    • (2014) RNA , vol.20 , pp. 1398-1409
    • Rouya, C.1    Siddiqui, N.2    Morita, M.3    Duchaine, T.F.4    Fabian, M.R.5    Sonenberg, N.6
  • 60
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae
    • Schmitt ME, Brown TA, Trumpower BL, (1990) A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res 18: 3091-3092
    • (1990) Nucleic Acids Res , vol.18 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3
  • 61
    • 0032778953 scopus 로고    scopus 로고
    • Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae
    • Schwartz DC, Parker R, (1999) Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of mRNAs in Saccharomyces cerevisiae. Mol Cell Biol 19: 5247-5256
    • (1999) Mol Cell Biol , vol.19 , pp. 5247-5256
    • Schwartz, D.C.1    Parker, R.2
  • 62
    • 0033773044 scopus 로고    scopus 로고
    • MRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E
    • Schwartz DC, Parker R, (2000) mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Mol Cell Biol 20: 7933-7942
    • (2000) Mol Cell Biol , vol.20 , pp. 7933-7942
    • Schwartz, D.C.1    Parker, R.2
  • 63
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • Seufert W, Jentsch S, (1990) Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J 9: 543-550
    • (1990) EMBO J , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 64
    • 84908047269 scopus 로고    scopus 로고
    • Reconstitution of a minimal ribosome-associated ubiquitination pathway with purified factors
    • Shao S, Hegde RS, (2014) Reconstitution of a minimal ribosome-associated ubiquitination pathway with purified factors. Mol Cell 55: 880-890
    • (2014) Mol Cell , vol.55 , pp. 880-890
    • Shao, S.1    Hegde, R.S.2
  • 65
    • 84861841297 scopus 로고    scopus 로고
    • Translation drives mRNA quality control
    • Shoemaker CJ, Green R, (2012) Translation drives mRNA quality control. Nat Struct Mol Biol 19: 594-601
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 594-601
    • Shoemaker, C.J.1    Green, R.2
  • 66
    • 84863688029 scopus 로고    scopus 로고
    • The DEAD-box protein Dhh1 promotes decapping by slowing ribosome movement
    • Sweet T, Kovalak C, Coller J, (2012) The DEAD-box protein Dhh1 promotes decapping by slowing ribosome movement. PLoS Biol 10: e1001342
    • (2012) PLoS Biol , vol.10 , pp. e1001342
    • Sweet, T.1    Kovalak, C.2    Coller, J.3
  • 68
    • 0032940545 scopus 로고    scopus 로고
    • Analysis of mutations in the yeast mRNA decapping enzyme
    • Tharun S, Parker R, (1999) Analysis of mutations in the yeast mRNA decapping enzyme. Genetics 151: 1273-1285
    • (1999) Genetics , vol.151 , pp. 1273-1285
    • Tharun, S.1    Parker, R.2
  • 69
    • 0035930337 scopus 로고    scopus 로고
    • Targeting an mRNA for decapping: Displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs
    • Tharun S, Parker R, (2001) Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol Cell 8: 1075-1083
    • (2001) Mol Cell , vol.8 , pp. 1075-1083
    • Tharun, S.1    Parker, R.2
  • 70
    • 84861456756 scopus 로고    scopus 로고
    • Dom34:hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3′ end of aberrant mRNA
    • Tsuboi T, Kuroha K, Kudo K, Makino S, Inoue E, Kashima I, Inada T, (2012) Dom34:hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3′ end of aberrant mRNA. Mol Cell 46: 518-529
    • (2012) Mol Cell , vol.46 , pp. 518-529
    • Tsuboi, T.1    Kuroha, K.2    Kudo, K.3    Makino, S.4    Inoue, E.5    Kashima, I.6    Inada, T.7
  • 71
    • 0035830508 scopus 로고    scopus 로고
    • The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae
    • Tucker M, Valencia-Sanchez MA, Staples RR, Chen J, Denis CL, Parker R, (2001) The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell 104: 377-386
    • (2001) Cell , vol.104 , pp. 377-386
    • Tucker, M.1    Valencia-Sanchez, M.A.2    Staples, R.R.3    Chen, J.4    Denis, C.L.5    Parker, R.6
  • 73
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation of mRNAs lacking a termination codon
    • van Hoof A, Frischmeyer PA, Dietz HC, Parker R, (2002) Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 295: 2262-2264
    • (2002) Science , vol.295 , pp. 2262-2264
    • Van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 74
    • 84861911071 scopus 로고    scopus 로고
    • Translational control by changes in poly(A) tail length: Recycling mRNAs
    • Weill L, Belloc E, Bava FA, Mendez R, (2012) Translational control by changes in poly(A) tail length: recycling mRNAs. Nat Struct Mol Biol 19: 577-585
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 577-585
    • Weill, L.1    Belloc, E.2    Bava, F.A.3    Mendez, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.