메뉴 건너뛰기




Volumn 9, Issue 6, 2013, Pages

Latent Effects of Hsp90 Mutants Revealed at Reduced Expression Levels

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90; MUTANT PROTEIN;

EID: 84879619070     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1003600     Document Type: Article
Times cited : (64)

References (62)
  • 1
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer WP, (1994) Rapid evolution of a protein in vitro by DNA shuffling. Nature 370: 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 2
    • 0023764283 scopus 로고
    • Pattern of nucleotide substitution at major histocompatibility complex class I loci reveals overdominant selection
    • Hughes AL, Nei M, (1988) Pattern of nucleotide substitution at major histocompatibility complex class I loci reveals overdominant selection. Nature 335: 167-170.
    • (1988) Nature , vol.335 , pp. 167-170
    • Hughes, A.L.1    Nei, M.2
  • 3
    • 0033639150 scopus 로고    scopus 로고
    • Statistical methods for detecting molecular adaptation
    • Yang Z, Bielawski JP, (2000) Statistical methods for detecting molecular adaptation. Trends Ecol Evol 15: 496-503.
    • (2000) Trends Ecol Evol , vol.15 , pp. 496-503
    • Yang, Z.1    Bielawski, J.P.2
  • 4
    • 0016669094 scopus 로고
    • Evolution at two levels in humans and chimpanzees
    • King MC, Wilson AC, (1975) Evolution at two levels in humans and chimpanzees. Science 188: 107-116.
    • (1975) Science , vol.188 , pp. 107-116
    • King, M.C.1    Wilson, A.C.2
  • 5
    • 79952063440 scopus 로고    scopus 로고
    • The developmental role of Agouti in color pattern evolution
    • Manceau M, Domingues VS, Mallarino R, Hoekstra HE, (2011) The developmental role of Agouti in color pattern evolution. Science 331: 1062-1065.
    • (2011) Science , vol.331 , pp. 1062-1065
    • Manceau, M.1    Domingues, V.S.2    Mallarino, R.3    Hoekstra, H.E.4
  • 6
    • 23144432213 scopus 로고    scopus 로고
    • Optimality and evolutionary tuning of the expression level of a protein
    • Dekel E, Alon U, (2005) Optimality and evolutionary tuning of the expression level of a protein. Nature 436: 588-592.
    • (2005) Nature , vol.436 , pp. 588-592
    • Dekel, E.1    Alon, U.2
  • 8
    • 77953212314 scopus 로고    scopus 로고
    • The relationship among gene expression, the evolution of gene dosage, and the rate of protein evolution
    • Gout JF, Kahn D, Duret L, (2010) The relationship among gene expression, the evolution of gene dosage, and the rate of protein evolution. PLoS Genet 6: e1000944.
    • (2010) PLoS Genet , vol.6
    • Gout, J.F.1    Kahn, D.2    Duret, L.3
  • 10
    • 84865619780 scopus 로고    scopus 로고
    • Solubility-promoting function of hsp90 contributes to client maturation and robust cell growth
    • Pursell NW, Mishra P, Bolon DN, (2012) Solubility-promoting function of hsp90 contributes to client maturation and robust cell growth. Eukaryot Cell 11: 1033-1041.
    • (2012) Eukaryot Cell , vol.11 , pp. 1033-1041
    • Pursell, N.W.1    Mishra, P.2    Bolon, D.N.3
  • 12
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation
    • Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM, (1994) Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci U S A 91: 8324-8328.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 14
    • 2942565781 scopus 로고    scopus 로고
    • The distribution of fitness effects caused by single-nucleotide substitutions in an RNA virus
    • Sanjuan R, Moya A, Elena SF, (2004) The distribution of fitness effects caused by single-nucleotide substitutions in an RNA virus. Proc Natl Acad Sci U S A 101: 8396-8401.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8396-8401
    • Sanjuan, R.1    Moya, A.2    Elena, S.F.3
  • 15
    • 36348963100 scopus 로고    scopus 로고
    • Distribution of fitness and virulence effects caused by single-nucleotide substitutions in Tobacco Etch virus
    • Carrasco P, de la Iglesia F, Elena SF, (2007) Distribution of fitness and virulence effects caused by single-nucleotide substitutions in Tobacco Etch virus. J Virol 81: 12979-12984.
    • (2007) J Virol , vol.81 , pp. 12979-12984
    • Carrasco, P.1    de la Iglesia, F.2    Elena, S.F.3
  • 16
    • 73649127602 scopus 로고    scopus 로고
    • The fitness effects of random mutations in single-stranded DNA and RNA bacteriophages
    • Domingo-Calap P, Cuevas JM, Sanjuan R, (2009) The fitness effects of random mutations in single-stranded DNA and RNA bacteriophages. PLoS Genet 5: e1000742.
    • (2009) PLoS Genet , vol.5
    • Domingo-Calap, P.1    Cuevas, J.M.2    Sanjuan, R.3
  • 17
    • 77955475761 scopus 로고    scopus 로고
    • Distribution of fitness effects caused by single-nucleotide substitutions in bacteriophage f1
    • Peris JB, Davis P, Cuevas JM, Nebot MR, Sanjuan R, (2010) Distribution of fitness effects caused by single-nucleotide substitutions in bacteriophage f1. Genetics 185: 603-609.
    • (2010) Genetics , vol.185 , pp. 603-609
    • Peris, J.B.1    Davis, P.2    Cuevas, J.M.3    Nebot, M.R.4    Sanjuan, R.5
  • 18
    • 79959992592 scopus 로고    scopus 로고
    • A biophysical protein folding model accounts for most mutational fitness effects in viruses
    • Wylie CS, Shakhnovich EI, (2011) A biophysical protein folding model accounts for most mutational fitness effects in viruses. Proc Natl Acad Sci U S A 108: 9916-9921.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9916-9921
    • Wylie, C.S.1    Shakhnovich, E.I.2
  • 19
    • 36049027813 scopus 로고    scopus 로고
    • Protein stability imposes limits on organism complexity and speed of molecular evolution
    • Zeldovich KB, Chen P, Shakhnovich EI, (2007) Protein stability imposes limits on organism complexity and speed of molecular evolution. Proc Natl Acad Sci U S A 104: 16152-16157.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16152-16157
    • Zeldovich, K.B.1    Chen, P.2    Shakhnovich, E.I.3
  • 20
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • Tokuriki N, Tawfik DS, (2009) Stability effects of mutations and protein evolvability. Curr Opin Struct Biol 19: 596-604.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 21
    • 0029055565 scopus 로고
    • The control of flux: 21 years on
    • Kacser H, Fell DA, (1995) The control of flux: 21 years on. Biochem Soc Trans 23: 341-366.
    • (1995) Biochem Soc Trans , vol.23 , pp. 341-366
    • Kacser, H.1    Fell, D.A.2
  • 22
    • 0024421221 scopus 로고
    • hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
    • Borkovich KA, Farrelly FW, Finkelstein DB, Taulien J, Lindquist S, (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9: 3919-3930.
    • (1989) Mol Cell Biol , vol.9 , pp. 3919-3930
    • Borkovich, K.A.1    Farrelly, F.W.2    Finkelstein, D.B.3    Taulien, J.4    Lindquist, S.5
  • 23
    • 78449233935 scopus 로고    scopus 로고
    • Pervasive cryptic epistasis in molecular evolution
    • Lunzer M, Golding GB, Dean AM, (2010) Pervasive cryptic epistasis in molecular evolution. PLoS Genet 6: e1001162.
    • (2010) PLoS Genet , vol.6
    • Lunzer, M.1    Golding, G.B.2    Dean, A.M.3
  • 24
    • 27144538817 scopus 로고    scopus 로고
    • The biochemical architecture of an ancient adaptive landscape
    • Lunzer M, Miller SP, Felsheim R, Dean AM, (2005) The biochemical architecture of an ancient adaptive landscape. Science 310: 499-501.
    • (2005) Science , vol.310 , pp. 499-501
    • Lunzer, M.1    Miller, S.P.2    Felsheim, R.3    Dean, A.M.4
  • 25
    • 84872272432 scopus 로고    scopus 로고
    • Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness
    • Bershtein S, Mu W, Serohijos AW, Zhou J, Shakhnovich EI, (2013) Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness. Mol Cell 49: 133-144.
    • (2013) Mol Cell , vol.49 , pp. 133-144
    • Bershtein, S.1    Mu, W.2    Serohijos, A.W.3    Zhou, J.4    Shakhnovich, E.I.5
  • 26
    • 0019869334 scopus 로고
    • The molecular basis of dominance
    • Kacser H, Burns JA, (1981) The molecular basis of dominance. Genetics 97: 639-666.
    • (1981) Genetics , vol.97 , pp. 639-666
    • Kacser, H.1    Burns, J.A.2
  • 28
    • 0015989446 scopus 로고
    • A linear steady-state treatment of enzymatic chains. General properties, control and effector strength
    • Heinrich R, Rapoport TA, (1974) A linear steady-state treatment of enzymatic chains. General properties, control and effector strength. Eur J Biochem 42: 89-95.
    • (1974) Eur J Biochem , vol.42 , pp. 89-95
    • Heinrich, R.1    Rapoport, T.A.2
  • 29
    • 33645076253 scopus 로고    scopus 로고
    • An equivalence principle for the incorporation of favorable mutations in asexual populations
    • Hegreness M, Shoresh N, Hartl D, Kishony R, (2006) An equivalence principle for the incorporation of favorable mutations in asexual populations. Science 311: 1615-1617.
    • (2006) Science , vol.311 , pp. 1615-1617
    • Hegreness, M.1    Shoresh, N.2    Hartl, D.3    Kishony, R.4
  • 30
    • 0345306751 scopus 로고    scopus 로고
    • The origins of genome complexity
    • Lynch M, Conery JS, (2003) The origins of genome complexity. Science 302: 1401-1404.
    • (2003) Science , vol.302 , pp. 1401-1404
    • Lynch, M.1    Conery, J.S.2
  • 31
    • 42449128411 scopus 로고    scopus 로고
    • Population genomics of the wild yeast Saccharomyces paradoxus: Quantifying the life cycle
    • Tsai IJ, Bensasson D, Burt A, Koufopanou V, (2008) Population genomics of the wild yeast Saccharomyces paradoxus: Quantifying the life cycle. Proc Natl Acad Sci U S A 105: 4957-4962.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4957-4962
    • Tsai, I.J.1    Bensasson, D.2    Burt, A.3    Koufopanou, V.4
  • 32
    • 2942533020 scopus 로고    scopus 로고
    • The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
    • Harris SF, Shiau AK, Agard DA, (2004) The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 12: 1087-1097.
    • (2004) Structure , vol.12 , pp. 1087-1097
    • Harris, S.F.1    Shiau, A.K.2    Agard, D.A.3
  • 33
    • 84856702590 scopus 로고    scopus 로고
    • Protein model discrimination using mutational sensitivity derived from deep sequencing
    • Adkar BV, Tripathi A, Sahoo A, Bajaj K, Goswami D, et al. (2012) Protein model discrimination using mutational sensitivity derived from deep sequencing. Structure 20: 371-381.
    • (2012) Structure , vol.20 , pp. 371-381
    • Adkar, B.V.1    Tripathi, A.2    Sahoo, A.3    Bajaj, K.4    Goswami, D.5
  • 34
    • 84862025262 scopus 로고    scopus 로고
    • Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing
    • Whitehead TA, Chevalier A, Song Y, Dreyfus C, Fleishman SJ, et al. (2012) Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing. Nat Biotechnol 30: 543-548.
    • (2012) Nat Biotechnol , vol.30 , pp. 543-548
    • Whitehead, T.A.1    Chevalier, A.2    Song, Y.3    Dreyfus, C.4    Fleishman, S.J.5
  • 36
    • 84866782988 scopus 로고    scopus 로고
    • Fitness analyses of all possible point mutations for regions of genes in yeast
    • Hietpas R, Roscoe B, Jiang L, Bolon DN, (2012) Fitness analyses of all possible point mutations for regions of genes in yeast. Nat Protoc 7: 1382-1396.
    • (2012) Nat Protoc , vol.7 , pp. 1382-1396
    • Hietpas, R.1    Roscoe, B.2    Jiang, L.3    Bolon, D.N.4
  • 37
    • 84864577143 scopus 로고    scopus 로고
    • Predictive bcl-2 family binding models rooted in experiment or structure
    • Debartolo J, Dutta S, Reich L, Keating AE, (2012) Predictive bcl-2 family binding models rooted in experiment or structure. J Mol Biol 422: 124-144.
    • (2012) J Mol Biol , vol.422 , pp. 124-144
    • Debartolo, J.1    Dutta, S.2    Reich, L.3    Keating, A.E.4
  • 38
    • 77957963240 scopus 로고    scopus 로고
    • Rapid construction of empirical RNA fitness landscapes
    • Pitt JN, Ferre-D'Amare AR, (2010) Rapid construction of empirical RNA fitness landscapes. Science 330: 376-379.
    • (2010) Science , vol.330 , pp. 376-379
    • Pitt, J.N.1    Ferre-D'Amare, A.R.2
  • 40
    • 84867644046 scopus 로고    scopus 로고
    • A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function
    • Araya CL, Fowler DM, Chen W, Muniez I, Kelly JW, et al. (2012) A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function. Proc Natl Acad Sci U S A 109: 16858-16863.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 16858-16863
    • Araya, C.L.1    Fowler, D.M.2    Chen, W.3    Muniez, I.4    Kelly, J.W.5
  • 41
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression
    • Mumberg D, Muller R, Funk M, (1994) Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res 22: 5767-5768.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 42
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase
    • Nathan DF, Lindquist S, (1995) Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 15: 3917-3925.
    • (1995) Mol Cell Biol , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 43
    • 84875703570 scopus 로고    scopus 로고
    • Analyses of the Effects of All Ubiquitin Point Mutants on Yeast Growth Rate
    • Roscoe BP, Thayer KM, Zeldovich KB, Fushman D, Bolon DN, (2013) Analyses of the Effects of All Ubiquitin Point Mutants on Yeast Growth Rate. J Mol Biol 425: 1363-77.
    • (2013) J Mol Biol , vol.425 , pp. 1363-1377
    • Roscoe, B.P.1    Thayer, K.M.2    Zeldovich, K.B.3    Fushman, D.4    Bolon, D.N.5
  • 44
    • 36849083947 scopus 로고    scopus 로고
    • Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers
    • Wayne N, Bolon DN, (2007) Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers. J Biol Chem 282: 35386-35395.
    • (2007) J Biol Chem , vol.282 , pp. 35386-35395
    • Wayne, N.1    Bolon, D.N.2
  • 46
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA, (1990) Dominant forces in protein folding. Biochemistry 29: 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 47
    • 0014680905 scopus 로고
    • Non-Darwinian evolution
    • King JL, Jukes TH, (1969) Non-Darwinian evolution. Science 164: 788-798.
    • (1969) Science , vol.164 , pp. 788-798
    • King, J.L.1    Jukes, T.H.2
  • 48
  • 49
    • 79960601166 scopus 로고    scopus 로고
    • Slow protein evolutionary rates are dictated by surface-core association
    • Toth-Petroczy A, Tawfik DS, (2011) Slow protein evolutionary rates are dictated by surface-core association. Proc Natl Acad Sci U S A 108: 11151-11156.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 11151-11156
    • Toth-Petroczy, A.1    Tawfik, D.S.2
  • 50
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, et al. (2006) Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 440: 1013-1017.
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.1    Roe, S.M.2    Vaughan, C.K.3    Meyer, P.4    Panaretou, B.5
  • 51
    • 79551470095 scopus 로고    scopus 로고
    • Role of conformational sampling in computing mutation-induced changes in protein structure and stability
    • Kellogg EH, Leaver-Fay A, Baker D, (2011) Role of conformational sampling in computing mutation-induced changes in protein structure and stability. Proteins 79: 830-838.
    • (2011) Proteins , vol.79 , pp. 830-838
    • Kellogg, E.H.1    Leaver-Fay, A.2    Baker, D.3
  • 52
    • 0025639253 scopus 로고
    • Enzyme activity and fitness: Evolution in solution
    • Dykhuizen DE, Dean AM, (1990) Enzyme activity and fitness: Evolution in solution. Trends Ecol Evol 5: 257-262.
    • (1990) Trends Ecol Evol , vol.5 , pp. 257-262
    • Dykhuizen, D.E.1    Dean, A.M.2
  • 55
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg D, Muller R, Funk M, (1995) Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156: 119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 56
    • 0021591657 scopus 로고
    • Mutationally altered 3′ ends of yeast CYC1 mRNA affect transcript stability and translational efficiency
    • Zaret KS, Sherman F, (1984) Mutationally altered 3′ ends of yeast CYC1 mRNA affect transcript stability and translational efficiency. J Mol Biol 177: 107-135.
    • (1984) J Mol Biol , vol.177 , pp. 107-135
    • Zaret, K.S.1    Sherman, F.2
  • 57
    • 33847608289 scopus 로고    scopus 로고
    • Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC
    • Li MZ, Elledge SJ, (2007) Harnessing homologous recombination in vitro to generate recombinant DNA via SLIC. Nat Methods 4: 251-256.
    • (2007) Nat Methods , vol.4 , pp. 251-256
    • Li, M.Z.1    Elledge, S.J.2
  • 58
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S, Henikoff JG, (1992) Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci U S A 89: 10915-10919.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 59
    • 79551674254 scopus 로고    scopus 로고
    • Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast
    • Geiler-Samerotte KA, Dion MF, Budnik BA, Wang SM, Hartl DL, et al. (2010) Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast. Proc Natl Acad Sci U S A 108: 680-685.
    • (2010) Proc Natl Acad Sci U S A , vol.108 , pp. 680-685
    • Geiler-Samerotte, K.A.1    Dion, M.F.2    Budnik, B.A.3    Wang, S.M.4    Hartl, D.L.5
  • 60
    • 0022727854 scopus 로고
    • Toxic effects of excess cloned centromeres
    • Futcher B, Carbon J, (1986) Toxic effects of excess cloned centromeres. Mol Cell Biol 6: 2213-2222.
    • (1986) Mol Cell Biol , vol.6 , pp. 2213-2222
    • Futcher, B.1    Carbon, J.2
  • 61
    • 0020554886 scopus 로고
    • Copy number control by a yeast centromere
    • Tschumper G, Carbon J, (1983) Copy number control by a yeast centromere. Gene 23: 221-232.
    • (1983) Gene , vol.23 , pp. 221-232
    • Tschumper, G.1    Carbon, J.2
  • 62
    • 0023430660 scopus 로고
    • Saccharomyces cerevisiae mutants that tolerate centromere plasmids at high copy number
    • Tschumper G, Carbon J, (1987) Saccharomyces cerevisiae mutants that tolerate centromere plasmids at high copy number. Proc Natl Acad Sci U S A 84: 7203-7207.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 7203-7207
    • Tschumper, G.1    Carbon, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.