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Volumn 79, Issue 2, 2013, Pages 559-568

Combinatorial mutagenesis and selection of improved signal sequences and their application for high-level production of translocated heterologous proteins in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BIOINFORMATICS ANALYSIS; COMPARATIVE STUDIES; E. COLI; EXPRESSION LEVELS; HETEROLOGOUS PROTEIN PRODUCTION; HETEROLOGOUS PROTEINS; HIGH-CELL-DENSITY CULTIVATIONS; HIGH-LEVEL PRODUCTION; HOST CELLS; MUTANT LIBRARIES; NOVEL DESIGN; PRODUCTION LEVEL; REPORTER GENE; SIGNAL PEPTIDE; SIGNAL SEQUENCE; TOLERANCE LEVELS;

EID: 84871868618     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02407-12     Document Type: Article
Times cited : (22)

References (50)
  • 1
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • Choi JH, Lee SY. 2004. Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl. Microbiol. Biotechnol. 64: 625-635.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 2
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • Esposito D, Chatterjee DK. 2006. Enhancement of soluble protein expression through the use of fusion tags. Curr. Opin. Biotechnol. 17:353-358.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 5
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides SC. 1996. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60:512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 6
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F, Mujacic M. 2004. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22:1399-1408.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 8
    • 33749164003 scopus 로고    scopus 로고
    • Formation of active inclusion bodies in the periplasm of Escherichia coli
    • Arié JP, Miot M, Sassoon N, Betton JM. 2006. Formation of active inclusion bodies in the periplasm of Escherichia coli. Mol. Microbiol. 62: 427-437.
    • (2006) Mol. Microbiol. , vol.62 , pp. 427-437
    • Arié, J.P.1    Miot, M.2    Sassoon, N.3    Betton, J.M.4
  • 10
    • 62349139780 scopus 로고    scopus 로고
    • Periplasmically exported lupanine hydroxylase undergoes transition from soluble to functional inclusion bodies in Escherichia coli
    • Stampolidis P, Kaderbhai NN, Kaderbhai MA. 2009. Periplasmically exported lupanine hydroxylase undergoes transition from soluble to functional inclusion bodies in Escherichia coli. Arch. Biochem. Biophys. 484: 8-15.
    • (2009) Arch. Biochem. Biophys. , vol.484 , pp. 8-15
    • Stampolidis, P.1    Kaderbhai, N.N.2    Kaderbhai, M.A.3
  • 11
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • Ventura S, Villaverde A. 2006. Protein quality in bacterial inclusion bodies. Trends Biotechnol. 24:179-185.
    • (2006) Trends Biotechnol. , vol.24 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 12
    • 84862577056 scopus 로고    scopus 로고
    • Membrane proteases in the bacterial protein secretion and quality control pathway
    • Dalbey RE, Wang P, van Dijl JM. 2012. Membrane proteases in the bacterial protein secretion and quality control pathway. Microbiol. Mol. Biol. Rev. 76:311-330.
    • (2012) Microbiol. Mol. Biol. Rev. , vol.76 , pp. 311-330
    • Dalbey, R.E.1    Wang, P.2    van Dijl, J.M.3
  • 13
    • 50049087513 scopus 로고    scopus 로고
    • Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane: distinct translocases and mechanisms
    • Natale P, Brüser T, Driessen AJ. 2008. Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane: distinct translocases and mechanisms. Biochim. Biophys. Acta 1778:1735-1756.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1735-1756
    • Natale, P.1    Brüser, T.2    Driessen, A.J.3
  • 14
    • 34548206622 scopus 로고    scopus 로고
    • Interactions that drive Sec-dependent bacterial protein transport
    • Rusch SL, Kendall DA. 2007. Interactions that drive Sec-dependent bacterial protein transport. Biochemistry 46:9665-9673.
    • (2007) Biochemistry , vol.46 , pp. 9665-9673
    • Rusch, S.L.1    Kendall, D.A.2
  • 15
    • 33748101074 scopus 로고    scopus 로고
    • Systematic screening of all signal peptides from Bacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in Gram-positive bacteria
    • Brockmeier U, Caspers M, Freudl R, Jockwer A, Noll T, Eggert T. 2006. Systematic screening of all signal peptides from Bacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in Gram-positive bacteria. J. Mol. Biol. 362:393-402.
    • (2006) J. Mol. Biol. , vol.362 , pp. 393-402
    • Brockmeier, U.1    Caspers, M.2    Freudl, R.3    Jockwer, A.4    Noll, T.5    Eggert, T.6
  • 16
    • 77952882027 scopus 로고    scopus 로고
    • Improvement of Sec-dependent secretion of a heterologous model protein in Bacillus subtilis by saturation mutagenesis of the N-domain of the AmyE signal peptide
    • Caspers M, Brockmeier U, Degering C, Eggert T, Freudl R. 2010. Improvement of Sec-dependent secretion of a heterologous model protein in Bacillus subtilis by saturation mutagenesis of the N-domain of the AmyE signal peptide. Appl. Microbiol. Biotechnol. 86:1877-1885.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1877-1885
    • Caspers, M.1    Brockmeier, U.2    Degering, C.3    Eggert, T.4    Freudl, R.5
  • 17
    • 33846938509 scopus 로고    scopus 로고
    • The presence of N-terminal secretion signal sequences leads to strong stimulation of the total expression levels of three tested medically important proteins during high-celldensity cultivations of Escherichia coli
    • Sletta H, Tøndervik A, Hakvâg S, Aune TEV, Nedal A, Aune R, Evensen G, Valla S, Ellingsen TE, Brautaset T. 2007. The presence of N-terminal secretion signal sequences leads to strong stimulation of the total expression levels of three tested medically important proteins during high-celldensity cultivations of Escherichia coli. Appl. Environ. Microbiol. 73:906-912.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 906-912
    • Sletta, H.1    Tøndervik, A.2    Hakvâg, S.3    Aune, T.E.V.4    Nedal, A.5    Aune, R.6    Evensen, G.7    Valla, S.8    Ellingsen, T.E.9    Brautaset, T.10
  • 18
    • 84455204799 scopus 로고    scopus 로고
    • Signal peptidase I: cleaving the way to mature proteins
    • Auclair SM, Bhanu MK, Kendall DA. 2012. Signal peptidase I: cleaving the way to mature proteins. Protein Sci. 21:13-25.
    • (2012) Protein Sci. , vol.21 , pp. 13-25
    • Auclair, S.M.1    Bhanu, M.K.2    Kendall, D.A.3
  • 19
    • 4444356342 scopus 로고    scopus 로고
    • Whole genome analysis reveals a high incidence of non-optimal codons in secretory signal sequences of Escherichia coli
    • Power PM, Jones RA, Beacham IR, Bucholtz C, Jennings MP. 2004. Whole genome analysis reveals a high incidence of non-optimal codons in secretory signal sequences of Escherichia coli. Biochem. Biophys. Res. Commun. 322:7.
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 7
    • Power, P.M.1    Jones, R.A.2    Beacham, I.R.3    Bucholtz, C.4    Jennings, M.P.5
  • 20
    • 34848845616 scopus 로고    scopus 로고
    • Selection for efficient translation initiation biases codon usage at second amino acid position in secretory proteins
    • Zalucki YM, Power PM, Jennings MP. 2007. Selection for efficient translation initiation biases codon usage at second amino acid position in secretory proteins. Nucleic Acids Res. 35:5748-5754.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5748-5754
    • Zalucki, Y.M.1    Power, P.M.2    Jennings, M.P.3
  • 21
    • 37549050221 scopus 로고    scopus 로고
    • Secretory signal sequence non-optimal codons are required for expression and export of C-lactamase
    • Zalucki YM, Gittins KL, Jennings MP. 2008. Secretory signal sequence non-optimal codons are required for expression and export of C-lactamase. Biochem. Biophys. Res. Commun. 366:135-141.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 135-141
    • Zalucki, Y.M.1    Gittins, K.L.2    Jennings, M.P.3
  • 22
    • 77952541173 scopus 로고    scopus 로고
    • Signal sequence non-optimal codons are required for the correct folding of mature maltose binding protein
    • Zalucki YM, Jones CE, Ng PSK, Schulz BL, Jennings MP. 2010. Signal sequence non-optimal codons are required for the correct folding of mature maltose binding protein. Biochim. Biophys. Acta 1798:1244-1249.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1244-1249
    • Zalucki, Y.M.1    Jones, C.E.2    Ng, P.S.K.3    Schulz, B.L.4    Jennings, M.P.5
  • 24
    • 10444232073 scopus 로고    scopus 로고
    • Broad-host-range plasmid pJB658 can be used for industrial-level production of a secreted host-toxic single-chain antibody fragment in Escherichia coli
    • Sletta H, Nedal A, Aune TEV, Hellebust H, Hakvâg S, Aune R, Ellingsen TE, Valla S, Brautaset T. 2004. Broad-host-range plasmid pJB658 can be used for industrial-level production of a secreted host-toxic single-chain antibody fragment in Escherichia coli. Appl. Environ. Microbiol. 70:7033-7039.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 7033-7039
    • Sletta, H.1    Nedal, A.2    Aune, T.E.V.3    Hellebust, H.4    Hakvâg, S.5    Aune, R.6    Ellingsen, T.E.7    Valla, S.8    Brautaset, T.9
  • 25
    • 33645781503 scopus 로고    scopus 로고
    • Directed evolution strategies for improved enzymatic performance
    • Hibbert E, Dalby P. 2005. Directed evolution strategies for improved enzymatic performance. Microb. Cell Fact. 4:29.
    • (2005) Microb. Cell Fact. , vol.4 , pp. 29
    • Hibbert, E.1    Dalby, P.2
  • 28
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer WPC. 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.C.1
  • 29
    • 0032031010 scopus 로고    scopus 로고
    • Engineering human DNA alkyltransferases for gene therapy using random sequence mutagenesis
    • Encell LP, Coates MM, Loeb LA. 1998. Engineering human DNA alkyltransferases for gene therapy using random sequence mutagenesis. Cancer Res. 58:1013-1020.
    • (1998) Cancer Res. , vol.58 , pp. 1013-1020
    • Encell, L.P.1    Coates, M.M.2    Loeb, L.A.3
  • 31
    • 77953606369 scopus 로고    scopus 로고
    • Directed evolution of the transcription factor XylS for development of improved expression systems
    • Aune TEV, Bakke I, Drabløs F, Lale R, Brautaset T, Valla S. 2010. Directed evolution of the transcription factor XylS for development of improved expression systems. Microb. Biotechnol. 3:38-47.
    • (2010) Microb. Biotechnol. , vol.3 , pp. 38-47
    • Aune, T.E.V.1    Bakke, I.2    Drabløs, F.3    Lale, R.4    Brautaset, T.5    Valla, S.6
  • 33
    • 77953573252 scopus 로고    scopus 로고
    • The expression of recombinant genes in Escherichia coli can be strongly stimulated at the transcript production level by mutating the DNA-region corresponding to the 5=-untranslated part of mRNA
    • Berg L, Lale R, Bakke I, Burroughs N, Valla S. 2009. The expression of recombinant genes in Escherichia coli can be strongly stimulated at the transcript production level by mutating the DNA-region corresponding to the 5=-untranslated part of mRNA. Microb. Biotechnol. 2:379-389.
    • (2009) Microb. Biotechnol. , vol.2 , pp. 379-389
    • Berg, L.1    Lale, R.2    Bakke, I.3    Burroughs, N.4    Valla, S.5
  • 35
    • 0026044557 scopus 로고
    • Mutagenesis of conserved residues within the active site of Escherichia coli alkaline phosphatase yields enzymes with increased kcat
    • Mandecki W, Shallcross MA, Sowadski J, Tomazic-Allen S. 1991. Mutagenesis of conserved residues within the active site of Escherichia coli alkaline phosphatase yields enzymes with increased kcat. Protein Eng.
    • (1991) Protein Eng. , vol.4 , pp. 801-804
    • Mandecki, W.1    Shallcross, M.A.2    Sowadski, J.3    Tomazic-allen, S.4
  • 36
    • 0019857117 scopus 로고
    • The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli
    • Kikuchi Y, Yoda K, Yamasaki M, Tamura G. 1981. The nucleotide sequence of the promoter and the amino-terminal region of alkaline phosphatase structural gene (phoA) of Escherichia coli. Nucleic Acids Res. 9:8.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 8
    • Kikuchi, Y.1    Yoda, K.2    Yamasaki, M.3    Tamura, G.4
  • 37
    • 0034125742 scopus 로고    scopus 로고
    • Pm promoter expression mutants and their use in broad-host-range RK2 plasmid vectors
    • Winther-Larsen HC, Blatny JM, Valand B, Brautaset T, Valla S. 2000. Pm promoter expression mutants and their use in broad-host-range RK2 plasmid vectors. Metab. Eng. 2:92-103.
    • (2000) Metab. Eng. , vol.2 , pp. 92-103
    • Winther-larsen, H.C.1    Blatny, J.M.2    Valand, B.3    Brautaset, T.4    Valla, S.5
  • 38
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H. 2011. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 8:785-786.
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 39
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • Salis HM, Mirsky EA, Voigt CA. 2009. Automated design of synthetic ribosome binding sites to control protein expression. Nat. Biotechnol. 27:946-950.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 41
    • 8044237717 scopus 로고    scopus 로고
    • High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions
    • Horn U, Strittmatter W, Krebber A, Knüpfer U, Kujau M, Wenderoth R, Müller K, Matzku S, Plückthun A, Riesenberg D. 1996. High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions. Appl. Microbiol. Biotechnol. 46: 524-532.
    • (1996) Appl. Microbiol. Biotechnol. , vol.46 , pp. 524-532
    • Horn, U.1    Strittmatter, W.2    Krebber, A.3    Knüpfer, U.4    Kujau, M.5    Wenderoth, R.6    Müller, K.7    Matzku, S.8    Plückthun, A.9    Riesenberg, D.10
  • 43
    • 0023191360 scopus 로고
    • Construction and use of signal sequence selection vectors in Escherichia coli and Bacillus subtilis
    • Smith H, Bron S, van Ee J, Venema G. 1987. Construction and use of signal sequence selection vectors in Escherichia coli and Bacillus subtilis. J. Bacteriol. 169:3321-3328.
    • (1987) J. Bacteriol. , vol.169 , pp. 3321-3328
    • Smith, H.1    Bron, S.2    van Ee, J.3    Venema, G.4
  • 44
    • 0023823396 scopus 로고
    • Characterization of signal-sequence-coding regions selected from the Bacillus subtilis chromosome
    • Smith H, de Jong A, Bron S, Venema G. 1988. Characterization of signal-sequence-coding regions selected from the Bacillus subtilis chromosome. Gene 70:351-361.
    • (1988) Gene , vol.70 , pp. 351-361
    • Smith, H.1    de Jong, A.2    Bron, S.3    Venema, G.4
  • 45
    • 64849114915 scopus 로고    scopus 로고
    • Coding-sequence determinants of gene expression in Escherichia coli
    • Kudla G, Murray AW, Tollervey D, Plotkin JB. 2009. Coding-sequence determinants of gene expression in Escherichia coli. Science 324:255-258.
    • (2009) Science , vol.324 , pp. 255-258
    • Kudla, G.1    Murray, A.W.2    Tollervey, D.3    Plotkin, J.B.4
  • 46
    • 0026772152 scopus 로고
    • Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases
    • van Dijl JM, de Jong A, Vehmaanpera J, Venema G, Bron S. 1992. Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases. EMBO J. 11:2819-2828.
    • (1992) EMBO J. , vol.11 , pp. 2819-2828
    • van Dijl, J.M.1    de Jong, A.2    Vehmaanpera, J.3    Venema, G.4    Bron, S.5
  • 47
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg D, Schwarz E, Komaromy M, Wall R. 1984. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 48
    • 0011864425 scopus 로고
    • Fusions of secreted proteins to alkaline phosphatase: an approach for studying protein secretion
    • Hoffman CS, Wright A. 1985. Fusions of secreted proteins to alkaline phosphatase: an approach for studying protein secretion. Proc. Natl. Acad. Sci. U. S. A. 82:5107-5111.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 5107-5111
    • Hoffman, C.S.1    Wright, A.2
  • 49
    • 0000632797 scopus 로고
    • TnphoA: a transposon probe for protein export signals
    • Manoil C, Beckwith J. 1985. TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. U. S. A. 82:8129-8133.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 50
    • 0030819591 scopus 로고    scopus 로고
    • Improved broad-host-range RK2 vectors useful for high and low regulated gene expression levels in gram-negative bacteria
    • Blatny JM, Brautaset T, Winther-Larsen HC, Karunakaran P, Valla S. 1997. Improved broad-host-range RK2 vectors useful for high and low regulated gene expression levels in gram-negative bacteria. Plasmid 38:35-51.
    • (1997) Plasmid , vol.38 , pp. 35-51
    • Blatny, J.M.1    Brautaset, T.2    Winther-larsen, H.C.3    Karunakaran, P.4    Valla, S.5


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