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Volumn 6, Issue , 2016, Pages

Distinct stress conditions result in aggregation of proteins with similar properties

Author keywords

[No Author keywords available]

Indexed keywords

AZETIDINE 2 CARBOXYLIC ACID; CAENORHABDITIS ELEGANS PROTEIN; FUNGAL PROTEIN; PROTEIN AGGREGATE;

EID: 84964290605     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep24554     Document Type: Article
Times cited : (108)

References (43)
  • 1
    • 84906794886 scopus 로고    scopus 로고
    • Proteostasis impairment in protein-misfolding and -aggregation diseases
    • Hipp, M. S., Park, S. H. & Hartl, F. U. Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends Cell Biol 24, 506-514 (2014).
    • (2014) Trends Cell Biol , vol.24 , pp. 506-514
    • Hipp, M.S.1    Park, S.H.2    Hartl, F.U.3
  • 2
    • 77957782470 scopus 로고    scopus 로고
    • Biology of amyloid: Structure, function, and regulation
    • Greenwald, J. & Riek, R. Biology of amyloid: structure, function, and regulation. Structure 18, 1244-1260 (2010).
    • (2010) Structure , vol.18 , pp. 1244-1260
    • Greenwald, J.1    Riek, R.2
  • 4
    • 84861763129 scopus 로고    scopus 로고
    • Proteome folding and aggregation
    • Vendruscolo, M. Proteome folding and aggregation. Curr Opin Struct Biol 22, 138-143 (2012).
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 138-143
    • Vendruscolo, M.1
  • 6
    • 84903363791 scopus 로고    scopus 로고
    • The yeast peroxiredoxin tsa1 protects against protein-aggregate-induced oxidative stress
    • Weids, A. J. & Grant, C. M. The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced oxidative stress. J Cell Sci 127, 1327-1335 (2014).
    • (2014) J Cell Sci , vol.127 , pp. 1327-1335
    • Weids, A.J.1    Grant, C.M.2
  • 7
    • 77649293067 scopus 로고    scopus 로고
    • Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing
    • Winkler, J. et al. Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing. EMBO J 29, 910-923 (2010).
    • (2010) EMBO J , vol.29 , pp. 910-923
    • Winkler, J.1
  • 8
    • 77950562866 scopus 로고    scopus 로고
    • A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes
    • Koplin, A. et al. A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J Cell Biol 189, 57-68 (2010).
    • (2010) J Cell Biol , vol.189 , pp. 57-68
    • Koplin, A.1
  • 9
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A. & Hayer-Hartl, M. Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332 (2011).
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 11
    • 84929151464 scopus 로고    scopus 로고
    • Heavy metals and metalloids as a cause for protein misfolding and aggregation
    • Tamas, M. J., Sharma, S. K., Ibstedt, S., Jacobson, T. & Christen, P. Heavy metals and metalloids as a cause for protein misfolding and aggregation. Biomolecules 4, 252-267 (2014).
    • (2014) Biomolecules , vol.4 , pp. 252-267
    • Tamas, M.J.1    Sharma, S.K.2    Ibstedt, S.3    Jacobson, T.4    Christen, P.5
  • 13
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G. C., Pohl, J., Flocco, M. T. & Rothman, J. E. Peptide-binding specificity of the molecular chaperone BiP. Nature 353, 726-730 (1991).
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 14
    • 84862550502 scopus 로고    scopus 로고
    • Biology of the heat shock response and protein chaperones: Budding yeast (Saccharomyces cerevisiae) as a model system
    • Verghese, J., Abrams, J., Wang, Y. & Morano, K. A. Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system. Microbiol Mol Biol Rev 76, 115-158 (2012).
    • (2012) Microbiol Mol Biol Rev , vol.76 , pp. 115-158
    • Verghese, J.1    Abrams, J.2    Wang, Y.3    Morano, K.A.4
  • 15
    • 84979217605 scopus 로고    scopus 로고
    • Global analysis of protein aggregation in yeast during physiological conditions and arsenite stress
    • Ibstedt, S., Sideri, T. C., Grant, C. M. & Tamas, M. J. Global analysis of protein aggregation in yeast during physiological conditions and arsenite stress. Biology open 3, 913-923 (2014).
    • (2014) Biology Open , vol.3 , pp. 913-923
    • Ibstedt, S.1    Sideri, T.C.2    Grant, C.M.3    Tamas, M.J.4
  • 16
    • 84872241449 scopus 로고    scopus 로고
    • Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast
    • Jacobson, T. et al. Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast. J Cell Sci 125, 5073-5083 (2012).
    • (2012) J Cell Sci , vol.125 , pp. 5073-5083
    • Jacobson, T.1
  • 17
    • 0035912730 scopus 로고    scopus 로고
    • Protein misfolding and temperature up-shift cause G1 arrest via a common mechanism dependent on heat shock factor in saccharomycescerevisiae
    • Trotter, E. W., Berenfeld, L., Krause, S. A., Petsko, G. A. & Gray, J. V. Protein misfolding and temperature up-shift cause G1 arrest via a common mechanism dependent on heat shock factor in Saccharomycescerevisiae. Proc Natl Acad Sci USA 98, 7313-7318 (2001).
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7313-7318
    • Trotter, E.W.1    Berenfeld, L.2    Krause, S.A.3    Petsko, G.A.4    Gray, J.V.5
  • 18
    • 84898041863 scopus 로고    scopus 로고
    • Pathophysiological importance of aggregated damaged proteins
    • Hohn, A., Jung, T. & Grune, T. Pathophysiological importance of aggregated damaged proteins. Free Radic Biol Med 71, 70-89 (2014).
    • (2014) Free Radic Biol Med , vol.71 , pp. 70-89
    • Hohn, A.1    Jung, T.2    Grune, T.3
  • 19
    • 0034705167 scopus 로고    scopus 로고
    • Protein oxidation in response to increased transcriptional or translational errors
    • Dukan, S. et al. Protein oxidation in response to increased transcriptional or translational errors. Proc Natl Acad Sci USA 97, 5746-5749 (2000).
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5746-5749
    • Dukan, S.1
  • 20
    • 77749239882 scopus 로고    scopus 로고
    • Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site
    • Ling, J. & Soll, D. Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site. Proc Natl Acad Sci USA 107, 4028-4033 (2010).
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4028-4033
    • Ling, J.1    Soll, D.2
  • 21
    • 43549088081 scopus 로고    scopus 로고
    • The yeast tsa1 peroxiredoxin is a ribosome-associated antioxidant
    • Trotter, E. W., Rand, J. D., Vickerstaff, J. & Grant, C. M. The yeast Tsa1 peroxiredoxin is a ribosome-associated antioxidant. Biochem J 412, 73-80 (2008).
    • (2008) Biochem J , vol.412 , pp. 73-80
    • Trotter, E.W.1    Rand, J.D.2    Vickerstaff, J.3    Grant, C.M.4
  • 22
    • 30044436319 scopus 로고    scopus 로고
    • The thioredoxin system protects ribosomes against stress-induced aggregation
    • Rand, J. D. & Grant, C. M. The Thioredoxin System Protects Ribosomes against Stress-induced Aggregation. Mol. Biol. Cell 17, 387-401 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 387-401
    • Rand, J.D.1    Grant, C.M.2
  • 23
    • 9144257282 scopus 로고    scopus 로고
    • The funcat, a functional annotation scheme for systematic classification of proteins from whole genomes
    • Ruepp, A. et al. The FunCat, a functional annotation scheme for systematic classification of proteins from whole genomes. Nucleic Acids Res 32, 5539-5545 (2004).
    • (2004) Nucleic Acids Res , vol.32 , pp. 5539-5545
    • Ruepp, A.1
  • 24
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D. & Yates, J. R. R. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19, 242-247 (2001).
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.R.3
  • 25
    • 33748377124 scopus 로고    scopus 로고
    • Quantification of protein half-lives in the budding yeast proteome
    • Belle, A., Tanay, A., Bitincka, L., Shamir, R. & O'Shea, E. K. Quantification of protein half-lives in the budding yeast proteome. Proc Natl Acad Sci USA 103, 13004-13009 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13004-13009
    • Belle, A.1    Tanay, A.2    Bitincka, L.3    Shamir, R.4    O'Shea, E.K.5
  • 26
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: Implications for their conserved function and the prediction of novel prions
    • Michelitsch, M. D. & Weissman, J. S. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc Natl Acad Sci USA 97, 11910-11915 (2000).
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 27
    • 0037388094 scopus 로고    scopus 로고
    • Genome-wide analysis of mRNA translation profiles in saccharomyces cerevisiae
    • Arava, Y. et al. Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 100, 3889-3894 (2003).
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3889-3894
    • Arava, Y.1
  • 28
    • 84872577837 scopus 로고    scopus 로고
    • The cotranslational function of ribosome-associated hsp70 in eukaryotic protein homeostasis
    • Willmund, F. et al. The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis. Cell 152, 196-209 (2013).
    • (2013) Cell , vol.152 , pp. 196-209
    • Willmund, F.1
  • 29
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in saccharomyces cerevisiae: Implications to protein folding pathways in the cell
    • Gong, Y. et al. An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5, 275 (2009).
    • (2009) Mol Syst Biol , vol.5 , pp. 275
    • Gong, Y.1
  • 30
    • 84933544966 scopus 로고    scopus 로고
    • Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones
    • Pausch, P. et al. Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones. Nat Commun 6, 7494 (2015).
    • (2015) Nat Commun , vol.6 , pp. 7494
    • Pausch, P.1
  • 31
    • 84871188495 scopus 로고    scopus 로고
    • Tor1 regulates protein solubility in saccharomyces cerevisiae
    • Peters, T. W. et al. Tor1 regulates protein solubility in Saccharomyces cerevisiae. Mol Biol Cell 23, 4679-4688 (2012).
    • (2012) Mol Biol Cell , vol.23 , pp. 4679-4688
    • Peters, T.W.1
  • 32
    • 77956795163 scopus 로고    scopus 로고
    • Widespread protein aggregation as an inherent part of aging in C. Elegans
    • David, D. C. et al. Widespread protein aggregation as an inherent part of aging in C. elegans. PLoS Biol 8, e1000450 (2010).
    • (2010) PLoS Biol , vol.8 , pp. e1000450
    • David, D.C.1
  • 33
    • 79957811582 scopus 로고    scopus 로고
    • The aggregation properties of Escherichia coli proteins associated with their cellular abundance
    • Castillo, V., Grana-Montes, R. & Ventura, S. The aggregation properties of Escherichia coli proteins associated with their cellular abundance. Biotechnol J 6, 752-760 (2011).
    • (2011) Biotechnol J , vol.6 , pp. 752-760
    • Castillo, V.1    Grana-Montes, R.2    Ventura, S.3
  • 34
    • 84883443658 scopus 로고    scopus 로고
    • Protein aggregation in bacteria: The thin boundary between functionality and toxicity
    • Bednarska, N. G., Schymkowitz, J., Rousseau, F. & Van Eldere, J. Protein aggregation in bacteria: the thin boundary between functionality and toxicity. Microbiology 159, 1795-1806 (2013).
    • (2013) Microbiology , vol.159 , pp. 1795-1806
    • Bednarska, N.G.1    Schymkowitz, J.2    Rousseau, F.3    Van Eldere, J.4
  • 35
    • 34247882072 scopus 로고    scopus 로고
    • Life on the edge: A link between gene expression levels and aggregation rates of human proteins
    • Tartaglia, G. G., Pechmann, S., Dobson, C. M. & Vendruscolo, M. Life on the edge: a link between gene expression levels and aggregation rates of human proteins. Trends Biochem Sci 32, 204-206 (2007).
    • (2007) Trends Biochem Sci , vol.32 , pp. 204-206
    • Tartaglia, G.G.1    Pechmann, S.2    Dobson, C.M.3    Vendruscolo, M.4
  • 36
    • 84870427355 scopus 로고    scopus 로고
    • Cellular strategies for regulating functional and nonfunctional protein aggregation
    • Gsponer, J. & Babu, M. M. Cellular strategies for regulating functional and nonfunctional protein aggregation. Cell Rep 2, 1425-1437 (2012).
    • (2012) Cell Rep , vol.2 , pp. 1425-1437
    • Gsponer, J.1    Babu, M.M.2
  • 37
    • 84887606872 scopus 로고    scopus 로고
    • Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins
    • Ciryam, P., Tartaglia, G. G., Morimoto, R. I., Dobson, C. M. & Vendruscolo, M. Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins. Cell Rep 5, 781-790 (2013).
    • (2013) Cell Rep , vol.5 , pp. 781-790
    • Ciryam, P.1    Tartaglia, G.G.2    Morimoto, R.I.3    Dobson, C.M.4    Vendruscolo, M.5
  • 38
    • 84855823950 scopus 로고    scopus 로고
    • Proteomic analysis of age-dependent changes in protein solubility identifies genes that modulate lifespan
    • Reis-Rodrigues, P. et al. Proteomic analysis of age-dependent changes in protein solubility identifies genes that modulate lifespan. Aging cell 11, 120-127 (2012).
    • (2012) Aging Cell , vol.11 , pp. 120-127
    • Reis-Rodrigues, P.1
  • 39
    • 79958184768 scopus 로고    scopus 로고
    • Regulation of translation by hydrogen peroxide
    • Grant, C. M. Regulation of translation by hydrogen peroxide. Antioxid Redox Signal 15, 191-203 (2011).
    • (2011) Antioxid Redox Signal , vol.15 , pp. 191-203
    • Grant, C.M.1
  • 40
    • 67649852558 scopus 로고    scopus 로고
    • Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins
    • Pechmann, S., Levy, E. D., Tartaglia, G. G. & Vendruscolo, M. Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins. Proc Natl Acad Sci USA 106, 10159-10164 (2009).
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10159-10164
    • Pechmann, S.1    Levy, E.D.2    Tartaglia, G.G.3    Vendruscolo, M.4
  • 41
    • 29444444251 scopus 로고    scopus 로고
    • How evolutionary pressure against protein aggregation shaped chaperone specificity
    • Rousseau, F., Serrano, L. & Schymkowitz, J. W. How evolutionary pressure against protein aggregation shaped chaperone specificity. J Mol Biol 355, 1037-1047 (2006).
    • (2006) J Mol Biol , vol.355 , pp. 1037-1047
    • Rousseau, F.1    Serrano, L.2    Schymkowitz, J.W.3
  • 42
    • 84876076016 scopus 로고    scopus 로고
    • Aging and the aggregating proteome
    • David, D. C. Aging and the aggregating proteome. Frontiers in genetics 3, 247 (2012).
    • (2012) Frontiers in Genetics , vol.3 , pp. 247
    • David, D.C.1
  • 43
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami, S. et al. Global analysis of protein expression in yeast. Nature 425, 737-741 (2003).
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1


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