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Volumn 28, Issue 4, 2012, Pages 925-930

Coexpression of molecular chaperone enhances activity and export of organophosphorus hydrolase in Escherichia coli

Author keywords

Molecular chaperone; Organophosphorus hydrolase; Periplasmic translocation; Twin arginine translocation pathway; Whole cell biocatalyst

Indexed keywords

MOLECULAR CHAPERONES; ORGANOPHOSPHORUS HYDROLASE; PERIPLASMIC TRANSLOCATION; TWIN-ARGININE TRANSLOCATIONS; WHOLE CELL BIOCATALYSTS;

EID: 84864835788     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1556     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 78649899395 scopus 로고    scopus 로고
    • Enzymatic and whole cell catalysis: finding new strategies for old processes
    • de Carvalho C. Enzymatic and whole cell catalysis: finding new strategies for old processes. Biotechnol Adv. 2011; 29: 75-83.
    • (2011) Biotechnol Adv. , vol.29 , pp. 75-83
    • de Carvalho, C.1
  • 2
    • 0029687854 scopus 로고    scopus 로고
    • Effects of ultraviolet light irradiation in biotreatment of organophosphates
    • Hung SC, Liao JC. Effects of ultraviolet light irradiation in biotreatment of organophosphates. Appl Biochem Biotechnol. 1996; 56: 37-47.
    • (1996) Appl Biochem Biotechnol. , vol.56 , pp. 37-47
    • Hung, S.C.1    Liao, J.C.2
  • 4
    • 0003242424 scopus 로고    scopus 로고
    • The development of a new biosensor based on recombinant E. coli for the direct detection of organophosphorus neurotoxins
    • Rainina EI, Efremenco EN, Varfolomeyev SD, Simonian AL, Wild JR. The development of a new biosensor based on recombinant E. coli for the direct detection of organophosphorus neurotoxins. Biosens Bioelectron. 1996; 11: 991-1000.
    • (1996) Biosens Bioelectron. , vol.11 , pp. 991-1000
    • Rainina, E.I.1    Efremenco, E.N.2    Varfolomeyev, S.D.3    Simonian, A.L.4    Wild, J.R.5
  • 5
    • 0043020726 scopus 로고
    • Permeable cells
    • Felix HR. Permeable cells. Anal Biochem. 1982; 120: 710-715.
    • (1982) Anal Biochem. , vol.120 , pp. 710-715
    • Felix, H.R.1
  • 6
    • 4043119792 scopus 로고    scopus 로고
    • Periplasmic expression as a basis for whole cell kinetic screening of unnatural enzyme reactivities
    • Sroga GE, Dordick JS. Periplasmic expression as a basis for whole cell kinetic screening of unnatural enzyme reactivities. Methods Enzymol. 2004; 388: 145-156.
    • (2004) Methods Enzymol. , vol.388 , pp. 145-156
    • Sroga, G.E.1    Dordick, J.S.2
  • 7
    • 79959796838 scopus 로고    scopus 로고
    • Recombinant protein secretion via the type III secretion system
    • Le TDV, Hong SH. Recombinant protein secretion via the type III secretion system. Korean J Chem Eng. 2011; 28: 1573-1579.
    • (2011) Korean J Chem Eng. , vol.28 , pp. 1573-1579
    • Le, T.D.V.1    Hong, S.H.2
  • 8
    • 0942297855 scopus 로고    scopus 로고
    • Functional display of foreign protein on surface of Escherichia coli using N-terminal domain of ice nucleation protein
    • Li L, Kang DG, Cha HJ. Functional display of foreign protein on surface of Escherichia coli using N-terminal domain of ice nucleation protein. Biotechnol Bioeng. 2004; 85: 214-221.
    • (2004) Biotechnol Bioeng. , vol.85 , pp. 214-221
    • Li, L.1    Kang, D.G.2    Cha, H.J.3
  • 9
    • 0030855956 scopus 로고    scopus 로고
    • Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase
    • Richins RD, Kaneva I, Mulchandani A, Chen W. Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase. Nat Biotechnol. 1997; 15: 984-987.
    • (1997) Nat Biotechnol. , vol.15 , pp. 984-987
    • Richins, R.D.1    Kaneva, I.2    Mulchandani, A.3    Chen, W.4
  • 10
    • 0035125229 scopus 로고    scopus 로고
    • Cell surface display of organophosphorus hydrolase using ice nucleation protein
    • Shimazu M, Mulchandani A, Chen W. Cell surface display of organophosphorus hydrolase using ice nucleation protein. Biotechnol Prog. 2001; 17: 76-80.
    • (2001) Biotechnol Prog. , vol.17 , pp. 76-80
    • Shimazu, M.1    Mulchandani, A.2    Chen, W.3
  • 11
    • 52349118100 scopus 로고    scopus 로고
    • Efficient cell surface display of organophosphorous hydrolase using N-terminal domain of ice nucleation protein in Escherichia coli
    • Kang DG, Li L, Ha JH, Choi SS, Cha HJ. Efficient cell surface display of organophosphorous hydrolase using N-terminal domain of ice nucleation protein in Escherichia coli. Korean J Chem Eng. 2008; 25: 804-807.
    • (2008) Korean J Chem Eng. , vol.25 , pp. 804-807
    • Kang, D.G.1    Li, L.2    Ha, J.H.3    Choi, S.S.4    Cha, H.J.5
  • 12
    • 0024340489 scopus 로고
    • Structure-activity relationship in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Donarski WJ, Dumas DP, Heitmeyer DP, Lewis VE, Raushel FM. Structure-activity relationship in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry. 1989; 28: 4650-4655.
    • (1989) Biochemistry. , vol.28 , pp. 4650-4655
    • Donarski, W.J.1    Dumas, D.P.2    Heitmeyer, D.P.3    Lewis, V.E.4    Raushel, F.M.5
  • 13
    • 0024008341 scopus 로고
    • Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase
    • McDaniel CS, Harper LL, Wild JR. Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase. J Bacteriol. 1988; 170: 2306-2311.
    • (1988) J Bacteriol. , vol.170 , pp. 2306-2311
    • McDaniel, C.S.1    Harper, L.L.2    Wild, J.R.3
  • 14
    • 0024332036 scopus 로고
    • Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein
    • Mulbry WW, Karns JS. Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein. J Bacteriol. 1989; 171: 6740-6746.
    • (1989) J Bacteriol. , vol.171 , pp. 6740-6746
    • Mulbry, W.W.1    Karns, J.S.2
  • 15
    • 0030711517 scopus 로고    scopus 로고
    • Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate
    • Grimsley JK, Scholtz JM, Pace CN, Wild JR. Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate. Biochemistry. 1997; 36: 14366-14374.
    • (1997) Biochemistry. , vol.36 , pp. 14366-14374
    • Grimsley, J.K.1    Scholtz, J.M.2    Pace, C.N.3    Wild, J.R.4
  • 16
    • 0028933772 scopus 로고
    • Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorous hydrolase
    • Lai K, Stolowich NJ, Wild JR. Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorous hydrolase. Arch Biochem Biophys. 1995; 318: 59-64.
    • (1995) Arch Biochem Biophys. , vol.318 , pp. 59-64
    • Lai, K.1    Stolowich, N.J.2    Wild, J.R.3
  • 17
    • 33646042541 scopus 로고    scopus 로고
    • Enhanced biodegradation of toxic organophosphate compounds using recombinant Escherichia coli with sec pathway-driven periplasmic secretion of organophosphorus hydrolase
    • Kang DG, Choi SS, Cha HJ. Enhanced biodegradation of toxic organophosphate compounds using recombinant Escherichia coli with sec pathway-driven periplasmic secretion of organophosphorus hydrolase. Biotechnol Prog. 2006; 22: 406-410.
    • (2006) Biotechnol Prog. , vol.22 , pp. 406-410
    • Kang, D.G.1    Choi, S.S.2    Cha, H.J.3
  • 18
    • 23044481815 scopus 로고    scopus 로고
    • Functional periplasmic secretion of organophosphorous hydrolase using the twin-arginine translocation pathway in Escherichia coli
    • Kang DG, Lim GB, Cha HJ. Functional periplasmic secretion of organophosphorous hydrolase using the twin-arginine translocation pathway in Escherichia coli. J Biotechnol. 2005; 118: 379-385.
    • (2005) J Biotechnol. , vol.118 , pp. 379-385
    • Kang, D.G.1    Lim, G.B.2    Cha, H.J.3
  • 19
    • 34447548232 scopus 로고    scopus 로고
    • Molecular chaperones: multiple functions, pathologies, and potential applications
    • Macario AJL, de Macario EC. Molecular chaperones: multiple functions, pathologies, and potential applications. Front Biosci. 2007; 12: 2588-2600.
    • (2007) Front Biosci. , vol.12 , pp. 2588-2600
    • Macario, A.J.L.1    de Macario, E.C.2
  • 20
    • 2442718034 scopus 로고    scopus 로고
    • Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain archaea
    • Macario AJL, Malz M, de Macario EC. Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain archaea. Front Biosci. 2004; 9: 1318-1332.
    • (2004) Front Biosci. , vol.9 , pp. 1318-1332
    • Macario, A.J.L.1    Malz, M.2    de Macario, E.C.3
  • 21
    • 66749187185 scopus 로고    scopus 로고
    • Multiple chaperonins in bacteria-why so many?
    • Lund PA. Multiple chaperonins in bacteria-why so many? FEMS Microbiol Rev. 2009; 33: 785-800.
    • (2009) FEMS Microbiol Rev. , vol.33 , pp. 785-800
    • Lund, P.A.1
  • 22
    • 0345483102 scopus 로고
    • Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis
    • Tilly K, Murialdo H, Georgopoulos C. Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc Natl Acad Sci USA. 1981; 78: 1629-1633.
    • (1981) Proc Natl Acad Sci USA. , vol.78 , pp. 1629-1633
    • Tilly, K.1    Murialdo, H.2    Georgopoulos, C.3
  • 23
    • 0034995184 scopus 로고    scopus 로고
    • The structural basis of protein targeting and translocation in bacteria
    • Driessen AJM, Manting EH, van der Does C. The structural basis of protein targeting and translocation in bacteria. Nat Struct Biol. 2001; 8: 492-498.
    • (2001) Nat Struct Biol. , vol.8 , pp. 492-498
    • Driessen, A.J.M.1    Manting, E.H.2    van der Does, C.3
  • 24
    • 0025375220 scopus 로고
    • Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli
    • Phillips GJ, Silhavy TJ. Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli. Nature. 1990; 344: 882-884.
    • (1990) Nature. , vol.344 , pp. 882-884
    • Phillips, G.J.1    Silhavy, T.J.2
  • 26
    • 77949915908 scopus 로고    scopus 로고
    • DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis
    • Li HM, Chang LM, Howell JM, Turner RJ. DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis. Biochim Biophys Acta-Proteins Proteomics. 2010; 1804: 1301-1309.
    • (2010) Biochim Biophys Acta-Proteins Proteomics. , vol.1804 , pp. 1301-1309
    • Li, H.M.1    Chang, L.M.2    Howell, J.M.3    Turner, R.J.4
  • 27
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • Oresnik IJ, Ladner CL, Turner RJ. Identification of a twin-arginine leader-binding protein. Mol Microbiol. 2001; 40: 323-331.
    • (2001) Mol Microbiol. , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 28
    • 0029745210 scopus 로고    scopus 로고
    • Involvement of the GroE chaperonins in the nickel-dependent anaerobic biosynthesis of NiFe-hydrogenases of Escherichia coli
    • Rodrigue A, Batia N, Muller M, Fayet O, Bohm R, Mandrand-Berthelot MA, Wu LF. Involvement of the GroE chaperonins in the nickel-dependent anaerobic biosynthesis of NiFe-hydrogenases of Escherichia coli. J Bacteriol. 1996; 178: 4453-4460.
    • (1996) J Bacteriol. , vol.178 , pp. 4453-4460
    • Rodrigue, A.1    Batia, N.2    Muller, M.3    Fayet, O.4    Bohm, R.5    Mandrand-Berthelot, M.A.6    Wu, L.F.7
  • 30
    • 0025836538 scopus 로고
    • Limits of diffusion in the hydrolysis of substrates by the phophotriesterase from Pseudomonas diminuta
    • Caldwell SR, Newcomb JR, Schlecht KA, Raushel FM. Limits of diffusion in the hydrolysis of substrates by the phophotriesterase from Pseudomonas diminuta. Biochemistry. 1991; 30: 7438-7444.
    • (1991) Biochemistry. , vol.30 , pp. 7438-7444
    • Caldwell, S.R.1    Newcomb, J.R.2    Schlecht, K.A.3    Raushel, F.M.4
  • 31
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley AP. The complete general secretory pathway in gram-negative bacteria. Microbiol Rev. 1993; 57: 50-108.
    • (1993) Microbiol Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 32
    • 0019947629 scopus 로고
    • Secretory protein translocation across membranes-the role of the docking protein
    • Meyer DI, Krause E, Dobberstein B. Secretory protein translocation across membranes-the role of the docking protein. Nature. 1982; 297: 647-650.
    • (1982) Nature. , vol.297 , pp. 647-650
    • Meyer, D.I.1    Krause, E.2    Dobberstein, B.3
  • 34
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks BC. A common export pathway for proteins binding complex redox cofactors? Mol Microbiol. 1996; 22: 393-404.
    • (1996) Mol Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 35
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz G, Dobberstein B. Common principles of protein translocation across membranes. Science. 1996; 271: 1519-1526.
    • (1996) Science. , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 36
    • 0026787702 scopus 로고
    • Protein-specific energy requirements for protein transport across or into thylakoid membranes, two lumenal proteins are transported in the absence of ATP
    • Cline K, Ettinger WF, Theg SM. Protein-specific energy requirements for protein transport across or into thylakoid membranes, two lumenal proteins are transported in the absence of ATP. J Biol Chem. 1992; 267: 2688-2696.
    • (1992) J Biol Chem. , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.F.2    Theg, S.M.3
  • 37
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • DeLisa MP, Tullman D, Georgiou G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc Natl Acad Sci USA. 2003; 100: 6115-6120.
    • (2003) Proc Natl Acad Sci USA. , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 38
    • 0033565687 scopus 로고    scopus 로고
    • The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding
    • Halbig D, Wiegert T, Blaudeck N, Freudl R, Sprenger GA. The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding. Eur J Biochem. 1999; 263: 543-551.
    • (1999) Eur J Biochem. , vol.263 , pp. 543-551
    • Halbig, D.1    Wiegert, T.2    Blaudeck, N.3    Freudl, R.4    Sprenger, G.A.5
  • 39
    • 0033532176 scopus 로고    scopus 로고
    • Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway
    • Rodrigue A, Chanal A, Beck K, Muller M, Wu LF. Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway. J Biol Chem. 1999; 274: 13223-13228.
    • (1999) J Biol Chem. , vol.274 , pp. 13223-13228
    • Rodrigue, A.1    Chanal, A.2    Beck, K.3    Muller, M.4    Wu, L.F.5
  • 40
    • 33645365498 scopus 로고    scopus 로고
    • Coexpression of TorD enhances the trans-port of GFP via the TAT pathway
    • Li SY, Chang BY, Lin SC. Coexpression of TorD enhances the trans-port of GFP via the TAT pathway. J Biotechnol. 2006; 122: 412-421.
    • (2006) J Biotechnol. , vol.122 , pp. 412-421
    • Li, S.Y.1    Chang, B.Y.2    Lin, S.C.3


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