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Volumn 5, Issue MARCH2016, 2016, Pages

The Rqc2/Tae2 subunit of the ribosome-associated quality control (RQC) complex marks ribosome-stalled nascent polypeptide chains for aggregation

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; GREEN FLUORESCENT PROTEIN; LISTERIN E3 UBIQUITIN PROTEIN LIGASE 1; POLYPEPTIDE; PROTEIN AGGREGATE; RIBOSOME ASSOCIATED QUALITY CONTROL COMPLEX; RIBOSOME ASSOCIATED QUALITY CONTROL COMPLEX 2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; PEPTIDE; RNA BINDING PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TAE2 PROTEIN, S CEREVISIAE;

EID: 84964290546     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.11794     Document Type: Article
Times cited : (115)

References (37)
  • 1
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S. 2009. A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137:146–158. doi: 10.1016/j.cell.2009.02.044
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 2
    • 19444364594 scopus 로고    scopus 로고
    • The other trinucleotide repeat: Polyalanine expansion disorders
    • Albrecht A, Mundlos S. 2005. The other trinucleotide repeat: polyalanine expansion disorders. Current Opinion in Genetics & Development 15:285–293. doi: 10.1016/j.gde.2005.04.003
    • (2005) Current Opinion in Genetics & Development , vol.15 , pp. 285-293
    • Albrecht, A.1    Mundlos, S.2
  • 3
    • 34548101963 scopus 로고    scopus 로고
    • J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation
    • Aron R, Higurashi T, Sahi C, Craig EA, Craig E. 2007. J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. The EMBO Journal 26:3794–3803. doi: 10.1038/sj.emboj.7601811
    • (2007) The EMBO Journal , vol.26 , pp. 3794-3803
    • Aron, R.1    Higurashi, T.2    Sahi, C.3    Craig, E.A.4    Craig, E.5
  • 4
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson MH, Joazeiro CAP. 2010. Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 467:470–473. doi: 10.1038/nature09371
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.P.2
  • 7
    • 43349089502 scopus 로고    scopus 로고
    • Validation of tandem mass spectrometry database search results using DTASelect
    • Cociorva D, L. Tabb D, Yates JR. 2007. Validation of tandem mass spectrometry database search results using DTASelect. Current Protocols in Bioinformatics 13. doi: 10.1002/0471250953.bi1304s16
    • (2007) Current Protocols in Bioinformatics , pp. 13
    • Cociorva, D.1    Tabb, D.2    Yates, J.R.3
  • 8
    • 84897086751 scopus 로고    scopus 로고
    • False start: Cotranslational protein ubiquitination and cytosolic protein quality control
    • Comyn SA, Chan GT, Mayor T. 2014. False start: Cotranslational protein ubiquitination and cytosolic protein quality control. Journal of Proteomics 100:92–101. doi: 10.1016/j.jprot.2013.08.005
    • (2014) Journal of Proteomics , vol.100 , pp. 92-101
    • Comyn, S.A.1    Chan, G.T.2    Mayor, T.3
  • 10
    • 80455122748 scopus 로고    scopus 로고
    • Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins
    • Fang NN, Ng AHM, Measday V, Mayor T. 2011. Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nature Cell Biology 13:1344–1352. doi: 10.1038/ncb2343
    • (2011) Nature Cell Biology , vol.13 , pp. 1344-1352
    • Fang, N.N.1    Ng, A.2    Measday, V.3    Mayor, T.4
  • 11
    • 84905483291 scopus 로고    scopus 로고
    • Functional diversification of Hsp40: Distinct J-protein functional requirements for two prions allow for chaperone-dependent prion selection
    • Harris JM, Nguyen PP, Patel MJ, Sporn ZA, Hines JK. 2014. Functional diversification of Hsp40: distinct J-protein functional requirements for two prions allow for chaperone-dependent prion selection. PLoS Genetics 10: e1004510. doi: 10.1371/journal.pgen.1004510
    • (2014) Plos Genetics , vol.10
    • Harris, J.M.1    Nguyen, P.P.2    Patel, M.J.3    Sporn, Z.A.4    Hines, J.K.5
  • 12
    • 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 & Development 21:519–524. doi: 10.1101/gad.1490207
    • (2007) Genes & Development , vol.21 , pp. 519-524
    • Ito-Harashima, S.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 13
  • 14
    • 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. The Journal of Cell Biology 189:57–68. doi: 10.1083/jcb.200910074
    • (2010) The Journal of Cell Biology , 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
  • 15
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S, Lindquist S. 2000. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proceedings of the National Academy of Sciences of the United States of America 97:1589–1594. doi: 10.1073/pnas.97.4.1589
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 16
    • 84883142045 scopus 로고    scopus 로고
    • Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1
    • Letzring DP, Wolf AS, Brule CE, Grayhack EJ. 2013. Translation of CGA codon repeats in yeast involves quality control components and ribosomal protein L1. RNA 19:1208–1217. doi: 10.1261/rna.039446.113
    • (2013) RNA , vol.19 , pp. 1208-1217
    • Letzring, D.P.1    Wolf, A.S.2    Brule, C.E.3    Grayhack, E.J.4
  • 17
    • 84865103439 scopus 로고    scopus 로고
    • Prions in yeast
    • Liebman SW, Chernoff YO. 2012. Prions in yeast. Genetics 191:1041–1072. doi: 10.1534/genetics.111.137760
    • (2012) Genetics , vol.191 , pp. 1041-1072
    • Liebman, S.W.1    Chernoff, Y.O.2
  • 18
    • 34247574716 scopus 로고    scopus 로고
    • Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells
    • Liu C, Apodaca J, Davis L, Rao H. 2007. Proteasome inhibition in wild-type yeast Saccharomyces cerevisiae cells. BioTechniques 42:158–162. doi: 10.2144/000112389
    • (2007) Biotechniques , vol.42 , pp. 158-162
    • Liu, C.1    Apodaca, J.2    Davis, L.3    Rao, H.4
  • 19
    • 0032417527 scopus 로고    scopus 로고
    • The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains
    • Lopez-Buesa P, Pfund C, Craig EA. 1998. The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proceedings of the National Academy of Sciences of the United States of America 95:15253–15258. doi: 10.1073/pnas.95.26.15253
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , pp. 15253-15258
    • Lopez-Buesa, P.1    Pfund, C.2    Craig, E.A.3
  • 20
    • 84894085209 scopus 로고    scopus 로고
    • Protecting the proteome: Eukaryotic cotranslational quality control pathways
    • Lykke-Andersen J, Bennett EJ. 2014. Protecting the proteome: Eukaryotic cotranslational quality control pathways. The Journal of Cell Biology 204:467–476. doi: 10.1083/jcb.201311103
    • (2014) The Journal of Cell Biology , vol.204 , pp. 467-476
    • Lykke-Andersen, J.1    Bennett, E.J.2
  • 22
    • 84950160369 scopus 로고    scopus 로고
    • Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation
    • Mogk A, Kummer E, Bukau B. 2015. Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation. Frontiers in Molecular Biosciences 2. doi: 10.3389/fmolb.2015.00022
    • (2015) Frontiers in Molecular Biosciences , pp. 2
    • Mogk, A.1    Kummer, E.2    Bukau, B.3
  • 24
    • 84879920420 scopus 로고    scopus 로고
    • PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the sis1p chaperone
    • Park S-H, Kukushkin Y, Gupta R, Chen T, Konagai A, Hipp MS, Hayer-Hartl M, Hartl FU. 2013. PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the sis1p chaperone. Cell 154:134–145. doi: 10.1016/j.cell.2013.06.003
    • (2013) Cell , vol.154 , pp. 134-145
    • Park, S.-H.1    Kukushkin, Y.2    Gupta, R.3    Chen, T.4    Konagai, A.5    Hipp, M.S.6    Hayer-Hartl, M.7    Hartl, F.U.8
  • 25
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hspl04
    • Parsell DA, Kowal AS, Singer MA, Lindquist S. 1994. Protein disaggregation mediated by heat-shock protein Hspl04. Nature 372:475–478. doi: 10.1038/372475a0
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 26
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider CA, Rasband WS, Eliceiri KW. 2012. NIH Image to ImageJ: 25 years of image analysis. Nature Methods 9:671–675. doi: 10.1038/nmeth.2089
    • (2012) Nature Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 27
    • 84924777167 scopus 로고    scopus 로고
    • Structure and assembly pathway of the ribosome quality control complex
    • Shao S, Brown A, Santhanam B, Hegde RS. 2015. Structure and assembly pathway of the ribosome quality control complex. Molecular Cell 57:433–444. doi: 10.1016/j.molcel.2014.12.015
    • (2015) Molecular Cell , vol.57 , pp. 433-444
    • Shao, S.1    Brown, A.2    Santhanam, B.3    Hegde, R.S.4
  • 29
    • 84863610879 scopus 로고    scopus 로고
    • A study on the effect of surface lysine to arginine mutagenesis on protein stability and structure using green fluorescent protein
    • Sokalingam S, Raghunathan G, Soundrarajan N, Lee S-G. 2012. A study on the effect of surface lysine to arginine mutagenesis on protein stability and structure using green fluorescent protein. PLoS ONE 7:e40410. doi: 10.1371/journal.pone.0040410
    • (2012) Plos ONE , vol.7
    • Sokalingam, S.1    Raghunathan, G.2    Soundrarajan, N.3    Lee, S.-G.4
  • 30
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb DL, McDonald WH, Yates JR. 2002. DTASelect and contrast: tools for assembling and comparing protein identifications from shotgun proteomics. Journal of Proteome Research 1:21–26. doi: 10.1021/pr015504q
    • (2002) Journal of Proteome Research , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates, J.R.3
  • 31
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid structure: Conformational diversity and consequences
    • Toyama BH, Weissman JS. 2011. Amyloid structure: conformational diversity and consequences. Annual Review of Biochemistry 80:557–585. doi: 10.1146/annurev-biochem-090908-120656
    • (2011) Annual Review of Biochemistry , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 32
    • 84879034688 scopus 로고    scopus 로고
    • Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome
    • Verma R, Oania RS, Kolawa NJ, Deshaies RJ. 2013. Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome. eLife 2:e00308. doi: 10.7554/eLife.00308
    • (2013) Elife , vol.2 , pp. e00308
    • Verma, R.1    Oania, R.S.2    Kolawa, N.J.3    Deshaies, R.J.4
  • 33
    • 84930384193 scopus 로고    scopus 로고
    • Ubiquitination of newly synthesized proteins at the ribosome
    • Wang F, Canadeo LA, Huibregtse JM. 2015. Ubiquitination of newly synthesized proteins at the ribosome. Biochimie 114:127–133. doi: 10.1016/j.biochi.2015.02.006
    • (2015) Biochimie , vol.114 , pp. 127-133
    • Wang, F.1    Canadeo, L.A.2    Huibregtse, J.M.3
  • 34
    • 35548981256 scopus 로고    scopus 로고
    • A genomic screen in yeast reveals novel aspects of nonstop mRNA metabolism
    • Wilson MA, Meaux S, van Hoof A. 2007. A genomic screen in yeast reveals novel aspects of nonstop mRNA metabolism. Genetics 177:773–784. doi: 10.1534/genetics.107.073205
    • (2007) Genetics , vol.177 , pp. 773-784
    • Wilson, M.A.1    Meaux, S.2    Van Hoof, A.3
  • 35
    • 0032694248 scopus 로고    scopus 로고
    • The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 sis1
    • Yan W, Craig EA. 1999. The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 sis1. Molecular and Cellular Biology 19:7751–7758. doi: 10.1128/MCB.19.11.7751
    • (1999) Molecular and Cellular Biology , vol.19 , pp. 7751-7758
    • Yan, W.1    Craig, E.A.2
  • 36
    • 84873512659 scopus 로고    scopus 로고
    • Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability
    • Yang Z, Hong JY, Derkatch IL, Liebman SW. 2013. Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability. PLoS Genetics 9:e1003236. doi: 10.1371/journal.pgen.1003236
    • (2013) Plos Genetics , vol.9
    • Yang, Z.1    Hong, J.Y.2    Derkatch, I.L.3    Liebman, S.W.4
  • 37
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 Complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. 1998. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 Complex) that forms a stress-sensitive complex with HSF1. Cell 94:471–480. doi: 10.1016/S0092-8674(00)81588-3
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5


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