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Volumn 75, Issue 2, 2007, Pages 397-406

An online monitoring system based on a synthetic sigma32-dependent tandem promoter for visualization of insoluble proteins in the cytoplasm of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CELL LYSIS; HETEROLOGOUS PROTEINS; LUCIFERASE INDUCTION; TANDEM PROMOTERS;

EID: 34249880371     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0815-6     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 0029923189 scopus 로고    scopus 로고
    • Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies
    • Betton J, Hofnung M (1996) Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies. J Biol Chem 271:8046-8052
    • (1996) J Biol Chem , vol.271 , pp. 8046-8052
    • Betton, J.1    Hofnung, M.2
  • 2
    • 0033428522 scopus 로고    scopus 로고
    • Hyperosmotic shock induces the sigma32 and sigmaE stress regulons of Escherichia coli
    • Bianchi AA, Baneyx F (1999a) Hyperosmotic shock induces the sigma32 and sigmaE stress regulons of Escherichia coli. Mol Microbiol 34:1029-1038
    • (1999) Mol Microbiol , vol.34 , pp. 1029-1038
    • Bianchi, A.A.1    Baneyx, F.2
  • 3
    • 0032702687 scopus 로고    scopus 로고
    • Stress responses as a tool to detect and characterize the mode of action of antibacterial agents
    • Bianchi AA, Baneyx F (1999b) Stress responses as a tool to detect and characterize the mode of action of antibacterial agents. Appl Environ Microbiol 65:5023-5027
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5023-5027
    • Bianchi, A.A.1    Baneyx, F.2
  • 4
    • 0028805520 scopus 로고
    • Both ambient temperature and the DnaK chaperone machine modulate the heat shock response in Escherichia coli by regulating the switch between sigma 70 and sigma 32 factors assembled with RNA polymerase
    • Blaszczak A, Zylicz M, Georgopoulos C, Liberek K (1995) Both ambient temperature and the DnaK chaperone machine modulate the heat shock response in Escherichia coli by regulating the switch between sigma 70 and sigma 32 factors assembled with RNA polymerase. EMBO J 14:5085-5093
    • (1995) EMBO J , vol.14 , pp. 5085-5093
    • Blaszczak, A.1    Zylicz, M.2    Georgopoulos, C.3    Liberek, K.4
  • 6
    • 0037468523 scopus 로고    scopus 로고
    • Role of molecular chaperones in inclusion body formation
    • Carrio MM, Villaverde A (2003) Role of molecular chaperones in inclusion body formation. FEBS Lett 537:215-521
    • (2003) FEBS Lett , vol.537 , pp. 215-521
    • Carrio, M.M.1    Villaverde, A.2
  • 7
    • 0027445907 scopus 로고
    • Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
    • Chuang SE, Burland V, Plunkett 3rd G, Daniels DL, Blattner FR (1993) Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. Gene 134:1-6
    • (1993) Gene , vol.134 , pp. 1-6
    • Chuang, S.E.1    Burland, V.2    Plunkett III, G.3    Daniels, D.L.4    Blattner, F.R.5
  • 9
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri A, Whitehorn EA, Tate E, Stemmer WP (1996) Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat Biotechnol 14:315-319
    • (1996) Nat Biotechnol , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 10
    • 0032581533 scopus 로고    scopus 로고
    • Construction of versatile high-level expression vectors for Bartonella henselae and the use of green fluorescent protein as a new expression marker
    • Dehio M, Knorre A, Lanz C, Dehio C (1998) Construction of versatile high-level expression vectors for Bartonella henselae and the use of green fluorescent protein as a new expression marker. Gene 215:223-229
    • (1998) Gene , vol.215 , pp. 223-229
    • Dehio, M.1    Knorre, A.2    Lanz, C.3    Dehio, C.4
  • 11
    • 0023367975 scopus 로고
    • Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene
    • Erickson JW, Vaughn V, Walter WA, Neidhardt CF, Gross CA (1987) Regulation of the promoters and transcripts of rpoH, the Escherichia coli heat shock regulatory gene. Genes Dev 1:419-432
    • (1987) Genes Dev , vol.1 , pp. 419-432
    • Erickson, J.W.1    Vaughn, V.2    Walter, W.A.3    Neidhardt, C.F.4    Gross, C.A.5
  • 12
    • 0026696625 scopus 로고
    • Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32
    • Gamer J, Bujard H, Bukau B (1992) Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32. Cell 69:833-842
    • (1992) Cell , vol.69 , pp. 833-842
    • Gamer, J.1    Bujard, H.2    Bukau, B.3
  • 13
    • 0030044799 scopus 로고    scopus 로고
    • A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32
    • Gamer J, Multhaup G, Tomoyasu T, McCarty JS, Rüdiger S, Schönfeld HJ, Schirra C, Bujard H, Bukau B (1996) A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J 15:607-617
    • (1996) EMBO J , vol.15 , pp. 607-617
    • Gamer, J.1    Multhaup, G.2    Tomoyasu, T.3    McCarty, J.S.4    Rüdiger, S.5    Schönfeld, H.J.6    Schirra, C.7    Bujard, H.8    Bukau, B.9
  • 14
    • 0021225289 scopus 로고
    • The htpR gene product of E. coli is a sigma factor for heat-shock promoters
    • Grossman AD, Erickson JW, Gross CA (1984) The htpR gene product of E. coli is a sigma factor for heat-shock promoters. Cell 38:383-390
    • (1984) Cell , vol.38 , pp. 383-390
    • Grossman, A.D.1    Erickson, J.W.2    Gross, C.A.3
  • 15
    • 0023322682 scopus 로고
    • Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli
    • Grossman AD, Straus DB, Walter WA, Gross CA (1987) Sigma 32 synthesis can regulate the synthesis of heat shock proteins in Escherichia coli. Genes Dev 1:179-184
    • (1987) Genes Dev , vol.1 , pp. 179-184
    • Grossman, A.D.1    Straus, D.B.2    Walter, W.A.3    Gross, C.A.4
  • 17
    • 0034693456 scopus 로고    scopus 로고
    • Monitoring of genes that respond to overproduction of an insoluble recombinant protein in Escherichia coli glucose-limited fed-batch fermentations
    • Jürgen B, Lin HY, Riemschneider S, Scharf C, Neubauer P, Schmid R, Hecker M, Schweder T (2000) Monitoring of genes that respond to overproduction of an insoluble recombinant protein in Escherichia coli glucose-limited fed-batch fermentations. Biotechnol Bioeng 70:217-224
    • (2000) Biotechnol Bioeng , vol.70 , pp. 217-224
    • Jürgen, B.1    Lin, H.Y.2    Riemschneider, S.3    Scharf, C.4    Neubauer, P.5    Schmid, R.6    Hecker, M.7    Schweder, T.8
  • 18
    • 0027983768 scopus 로고
    • Induction of heat shock proteins by abnormal proteins results from stabilization and not increased synthesis of sigma 32 in Escherichia coli
    • Kanemori M, Mori H, Yura T (1994) Induction of heat shock proteins by abnormal proteins results from stabilization and not increased synthesis of sigma 32 in Escherichia coli. J Bacteriol 176:5648-5653
    • (1994) J Bacteriol , vol.176 , pp. 5648-5653
    • Kanemori, M.1    Mori, H.2    Yura, T.3
  • 19
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust RB, Waugh DS (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8:1668-1674
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 21
    • 0035987265 scopus 로고    scopus 로고
    • The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
    • Kuczyńska-Wiśnik D, Kedzierska S, Matuszewska E, Lund P, Taylor A, Lipinska B, Laskowska E (2002) The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. Microbiology 148:1757-1765
    • (2002) Microbiology , vol.148 , pp. 1757-1765
    • Kuczyńska-Wiśnik, D.1    Kedzierska, S.2    Matuszewska, E.3    Lund, P.4    Taylor, A.5    Lipinska, B.6    Laskowska, E.7
  • 22
    • 0021719522 scopus 로고
    • Nucleotide sequence of the heat shock regulatory gene of E. coli suggests its protein product may be a transcription factor
    • Landick R, Vaughn V, Lau ET, VanBogelen RA, Erickson JW, Neidhardt FC (1984) Nucleotide sequence of the heat shock regulatory gene of E. coli suggests its protein product may be a transcription factor. Cell 38:175-182
    • (1984) Cell , vol.38 , pp. 175-182
    • Landick, R.1    Vaughn, V.2    Lau, E.T.3    Vanbogelen, R.A.4    Erickson, J.W.5    Neidhardt, F.C.6
  • 23
    • 0021253812 scopus 로고
    • Low-copy-number plasmid-cloning vectors amplifiable by derepression of an inserted foreign promoter
    • Larsen JE, Gerdes K, Light J, Molin S (1984) Low-copy-number plasmid-cloning vectors amplifiable by derepression of an inserted foreign promoter. Gene 28:45-54
    • (1984) Gene , vol.28 , pp. 45-54
    • Larsen, J.E.1    Gerdes, K.2    Light, J.3    Molin, S.4
  • 24
    • 0039870135 scopus 로고    scopus 로고
    • IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock
    • Laskowska E, Wawrzynow A, Taylor A (1996) IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock. Biochimie 78:117-122
    • (1996) Biochimie , vol.78 , pp. 117-122
    • Laskowska, E.1    Wawrzynow, A.2    Taylor, A.3
  • 25
    • 0036213467 scopus 로고    scopus 로고
    • Gene expression response to misfolded protein as a screen for soluble recombinant protein
    • Lesley SA, Graziano J, Cho CY, Knuth MW, Klock HE (2002) Gene expression response to misfolded protein as a screen for soluble recombinant protein. Protein Eng 15:153-160
    • (2002) Protein Eng , vol.15 , pp. 153-160
    • Lesley, S.A.1    Graziano, J.2    Cho, C.Y.3    Knuth, M.W.4    Klock, H.E.5
  • 26
    • 0027504094 scopus 로고
    • Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins
    • Liberek K, Georgopoulos C (1993) Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins. Proc Natl Acad Sci USA 90:11019-11023
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11019-11023
    • Liberek, K.1    Georgopoulos, C.2
  • 27
    • 0026600222 scopus 로고
    • The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor
    • Liberek K, Galitski TP, Zylicz M, Georgopoulos C (1992) The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor. Proc Natl Acad Sci USA 89:3516-3520
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3516-3520
    • Liberek, K.1    Galitski, T.P.2    Zylicz, M.3    Georgopoulos, C.4
  • 28
    • 0033989215 scopus 로고    scopus 로고
    • Green fluorescent protein as a quantitative reporter of relative promoter activity in E. coli
    • Lissemore JL, Jankowski JT, Thomas CB, Mascotti DP, deHaseth PL (2000) Green fluorescent protein as a quantitative reporter of relative promoter activity in E. coli. Biotechniques 28:82-84, 86, 88-89
    • (2000) Biotechniques , vol.28 , pp. 82-84
    • Lissemore, J.L.1    Jankowski, J.T.2    Thomas, C.B.3    Mascotti, D.P.4    Dehaseth, P.L.5
  • 29
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • Mogk A, Schlieker C, Friedrich KL, Schönfeld HJ, Vierling E, Bukau B (2003) Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem 278:31033-31042
    • (2003) J Biol Chem , vol.278 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.L.3    Schönfeld, H.J.4    Vierling, E.5    Bukau, B.6
  • 30
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK J-GrpE set and ClpB chaperones
    • Motohashi K, Watanabe Y, Yohda M, Yoshida M (1999) Heat-inactivated proteins are rescued by the DnaK J-GrpE set and ClpB chaperones. Proc Natl Acad Sci USA 96:7184-7189
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 31
    • 0019890564 scopus 로고
    • Positive regulatory gene for temperature-controlled proteins in Escherichia coli
    • Neidhardt FC, VanBogelen RA (1981) Positive regulatory gene for temperature-controlled proteins in Escherichia coli. Biochem Biophys Res Commun 100:894-900
    • (1981) Biochem Biophys Res Commun , vol.100 , pp. 894-900
    • Neidhardt, F.C.1    Vanbogelen, R.A.2
  • 32
    • 0024709959 scopus 로고
    • Induction of a heat shock-like response by unfolded protein in Escherichia coli: Dependence on protein level not protein degradation
    • Parsell DA, Sauer RT (1989) Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation. Genes Dev 3:1226-1232
    • (1989) Genes Dev , vol.3 , pp. 1226-1232
    • Parsell, D.A.1    Sauer, R.T.2
  • 34
    • 0032006484 scopus 로고    scopus 로고
    • Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin
    • Sachdev D, Chirgwin JM (1998) Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin. Protein Expr Purif 12:122-132
    • (1998) Protein Expr Purif , vol.12 , pp. 122-132
    • Sachdev, D.1    Chirgwin, J.M.2
  • 35
    • 0023240043 scopus 로고
    • The heat shock response of E. coli is regulated by changes in the concentration of sigma 32
    • Straus DB, Walter WA, Gross CA (1987) The heat shock response of E. coli is regulated by changes in the concentration of sigma 32. Nature 329:348-351
    • (1987) Nature , vol.329 , pp. 348-351
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 36
    • 0025632973 scopus 로고
    • DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32
    • Straus D, Walter W, Gross CA (1990) DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32. Genes Dev 4:2202-2209
    • (1990) Genes Dev , vol.4 , pp. 2202-2209
    • Straus, D.1    Walter, W.2    Gross, C.A.3
  • 37
    • 0034604704 scopus 로고    scopus 로고
    • Evidence for an active role of the DnaK chaperone system in the degradation of sigma(32)
    • Tatsuta T, Joob DM, Calendar R, Akiyama Y, Ogura T (2000) Evidence for an active role of the DnaK chaperone system in the degradation of sigma(32). FEBS Lett 478:271-275
    • (2000) FEBS Lett , vol.478 , pp. 271-275
    • Tatsuta, T.1    Joob, D.M.2    Calendar, R.3    Akiyama, Y.4    Ogura, T.5
  • 38
    • 0031705810 scopus 로고    scopus 로고
    • Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: Comparison with ClpA, ClpB, and HtpG in vivo
    • Thomas JG, Baneyx F (1998) Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG in vivo. J Bacteriol 180:5165-5172
    • (1998) J Bacteriol , vol.180 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2
  • 39
    • 0029968943 scopus 로고    scopus 로고
    • Recombinant protein expression at low temperatures under the transcriptional control of the major Escherichia coli cold shock promoter cspA
    • Vasina JA, Baneyx F (1996) Recombinant protein expression at low temperatures under the transcriptional control of the major Escherichia coli cold shock promoter cspA. Appl Environ Microbiol 62:1444-1447
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1444-1447
    • Vasina, J.A.1    Baneyx, F.2
  • 40
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veinger L, Diamant S, Buchner J, Goloubinoff P (1998) The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem 273:11032-11037
    • (1998) J Biol Chem , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 42
    • 0033600804 scopus 로고    scopus 로고
    • Increased synthesis of an Escherichia coli membrane protein suppresses F exclusion of bacteriophage T7
    • Wang WF, Margolin W, Molineux IJ (1999) Increased synthesis of an Escherichia coli membrane protein suppresses F exclusion of bacteriophage T7. J Mol Biol 292:501-512
    • (1999) J Mol Biol , vol.292 , pp. 501-512
    • Wang, W.F.1    Margolin, W.2    Molineux, I.J.3
  • 43
    • 0035130371 scopus 로고    scopus 로고
    • Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
    • Wigley WC, Stidham RD, Smith NM, Hunt JF, Thomas PJ (2001) Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein. Nat Biotechnol 19:131-136
    • (2001) Nat Biotechnol , vol.19 , pp. 131-136
    • Wigley, W.C.1    Stidham, R.D.2    Smith, N.M.3    Hunt, J.F.4    Thomas, P.J.5
  • 44
    • 0020092887 scopus 로고
    • Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K-12
    • Yamamori T, Yura T (1982) Genetic control of heat-shock protein synthesis and its bearing on growth and thermal resistance in Escherichia coli K-12. Proc Natl Acad Sci USA 79:860-864
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 860-864
    • Yamamori, T.1    Yura, T.2
  • 45
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation a novel multi-chaperone system from Escherichia coli
    • Zolkiewski M (1999) ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation A novel multi-chaperone system from Escherichia coli. J Biol Chem 274:28083-28086
    • (1999) J Biol Chem , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1


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