메뉴 건너뛰기




Volumn 39, Issue 1, 2008, Pages 74-83

Cellular response to accumulation of recombinant proteins in the E. coli inner membrane: Implications for proteolysis and productivity of the secretory expression system

Author keywords

Cellular stress response; Co translocational proteolysis; Escherichia coli; Inner membrane protease; OmpA signal peptide; Secretory expression

Indexed keywords

BIOLOGICAL MEMBRANES; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE EXPRESSION; PROTEOLYSIS;

EID: 43049118976     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2007.08.014     Document Type: Article
Times cited : (9)

References (53)
  • 1
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein Expression in Escherichia coli
    • Baneyx F. Recombinant protein Expression in Escherichia coli. Curr. Opin. Biotechnol. 10 (1999) 411-421
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 2
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 11 (2004) 1399-1408
    • (2004) Nat. Biotechnol. , vol.22 , Issue.11 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 3
    • 0033772459 scopus 로고    scopus 로고
    • Expressing genes in different Escherichia coli compartments
    • Cornelis P. Expressing genes in different Escherichia coli compartments. Curr. Opin. Biotechnol. 11 (2000) 450-454
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 450-454
    • Cornelis, P.1
  • 4
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • Choi J.H., and Lee S.Y. Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl. Microbiol. Biotechnol. 65 (2004) 625-635
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 5
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S.C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60 (1996) 512-538
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 6
    • 0032411723 scopus 로고    scopus 로고
    • The genetics of disulfide bond metabolism
    • Rietsch A., and Beckwith J. The genetics of disulfide bond metabolism. Annu. Rev. Genet. 32 (1998) 163-184
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 163-184
    • Rietsch, A.1    Beckwith, J.2
  • 7
    • 0037294121 scopus 로고    scopus 로고
    • Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli
    • Shokri A., Sanden A.M., and Larsson G. Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli. Appl. Microbiol. Biotechnol. 60 (2003) 654-664
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 654-664
    • Shokri, A.1    Sanden, A.M.2    Larsson, G.3
  • 9
    • 0013564318 scopus 로고
    • Cellular location affects protein stability in Escherichia coli
    • Talmadge K., and Gilbert W. Cellular location affects protein stability in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 79 (1982) 1830-1833
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 1830-1833
    • Talmadge, K.1    Gilbert, W.2
  • 10
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman S. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30 (1996) 465-506
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 11
    • 0035996719 scopus 로고    scopus 로고
    • Using secretion to solve a solubility problem: high-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGaseF
    • Loo T., Patchett M.L., Norris G.E., and Lott J.S. Using secretion to solve a solubility problem: high-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGaseF. Prot. Expr. Purif. 24 (2002) 90-98
    • (2002) Prot. Expr. Purif. , vol.24 , pp. 90-98
    • Loo, T.1    Patchett, M.L.2    Norris, G.E.3    Lott, J.S.4
  • 12
    • 0014010845 scopus 로고    scopus 로고
    • The release of enzymes by osmotic shock from Escherichia coli in exponential phase
    • Nossal N.G., and Heppel L.A. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J. Biol. Chem. 241 (1996) 3055-3062
    • (1996) J. Biol. Chem. , vol.241 , pp. 3055-3062
    • Nossal, N.G.1    Heppel, L.A.2
  • 13
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high level
    • Miroux B., and Walker J.E. Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high level. J. Mol. Biol. 260 (1996) 289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 14
    • 0033230145 scopus 로고    scopus 로고
    • Secretion-dependent proteolysis of heterologous protein by recombinant Escherichia coli is connected to an increased activity of the energy-generating dissimilatory pathway
    • Schmidt M., Viaplana E., Hoffmann F., Marten S., Villaverde A., and Rinas U. Secretion-dependent proteolysis of heterologous protein by recombinant Escherichia coli is connected to an increased activity of the energy-generating dissimilatory pathway. Biotechnol. Bioeng. 66 (1999) 61-67
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 61-67
    • Schmidt, M.1    Viaplana, E.2    Hoffmann, F.3    Marten, S.4    Villaverde, A.5    Rinas, U.6
  • 15
    • 20444424633 scopus 로고    scopus 로고
    • Cell death caused by hyper-expression of a secretory exoglucanase in Escherichia coli
    • Fu Z.B., Ng K.L., Lam T.L., and Wong W.K.R. Cell death caused by hyper-expression of a secretory exoglucanase in Escherichia coli. Prot. Expr. Purif. 42 (2005) 67-77
    • (2005) Prot. Expr. Purif. , vol.42 , pp. 67-77
    • Fu, Z.B.1    Ng, K.L.2    Lam, T.L.3    Wong, W.K.R.4
  • 16
    • 0037855839 scopus 로고    scopus 로고
    • Low temperature and glucose enhanced T7 RNA polymerase-based plasmid stability for increasing expression of glucagon-like peptide-2 in Escherichia coli
    • Zhang Y., Taiming L., and Liu J. Low temperature and glucose enhanced T7 RNA polymerase-based plasmid stability for increasing expression of glucagon-like peptide-2 in Escherichia coli. Prot. Expr. Purif. 29 (2003) 132-139
    • (2003) Prot. Expr. Purif. , vol.29 , pp. 132-139
    • Zhang, Y.1    Taiming, L.2    Liu, J.3
  • 17
    • 0034135677 scopus 로고    scopus 로고
    • The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli
    • Ignatova Z., Enfors S.O., Hobbie M., Taruttis S., Vogt C., and Kasche V. The relative importance of intracellular proteolysis and transport on the yield of the periplasmic enzyme penicillin amidase in Escherichia coli. Enzyme Microbiol. Technol. 26 (2000) 165-170
    • (2000) Enzyme Microbiol. Technol. , vol.26 , pp. 165-170
    • Ignatova, Z.1    Enfors, S.O.2    Hobbie, M.3    Taruttis, S.4    Vogt, C.5    Kasche, V.6
  • 18
    • 0031148990 scopus 로고    scopus 로고
    • Enhancement of extracellular production of a Cellulomonas fimi exoglucanase in Escherichia coli by the reduction of promoter strength
    • Lam T.L., Wong R.S.C., and Wong W.K.R. Enhancement of extracellular production of a Cellulomonas fimi exoglucanase in Escherichia coli by the reduction of promoter strength. Enzyme Microbiol. Technol. 20 (1997) 482-488
    • (1997) Enzyme Microbiol. Technol. , vol.20 , pp. 482-488
    • Lam, T.L.1    Wong, R.S.C.2    Wong, W.K.R.3
  • 20
    • 9244231763 scopus 로고    scopus 로고
    • Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli
    • Simmons L.C., and Yansura D.G. Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli. Nat. Biotechnol. 14 (1996) 629-634
    • (1996) Nat. Biotechnol. , vol.14 , pp. 629-634
    • Simmons, L.C.1    Yansura, D.G.2
  • 22
    • 0033935592 scopus 로고    scopus 로고
    • Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. endoxylanase signal sequence
    • Choi J.H., Jeong K.J., and Lee S.Y. Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. endoxylanase signal sequence. Appl. Microbiol. Biotechnol. 53 (2000) 640-645
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 640-645
    • Choi, J.H.1    Jeong, K.J.2    Lee, S.Y.3
  • 24
    • 0030595041 scopus 로고    scopus 로고
    • Different PrlA proteins increase the efficiency of periplasmic production of human interleukin-6 in Escherichia coli
    • Perez-Perez J., Barbero J.L., Marquez G., and Gutierrez J. Different PrlA proteins increase the efficiency of periplasmic production of human interleukin-6 in Escherichia coli. J. Biotechnol. 49 (1996) 245-247
    • (1996) J. Biotechnol. , vol.49 , pp. 245-247
    • Perez-Perez, J.1    Barbero, J.L.2    Marquez, G.3    Gutierrez, J.4
  • 25
  • 26
    • 0031797633 scopus 로고    scopus 로고
    • Extracellular expression of human epidermal growth factor encoded by an Escherichia coli K-12 plasmid stabilized by the ytl2-inc R system of Salmonella typhimurium
    • Wong D.H.K., Lam K.H.E., Chan C.K.P., Wong Y.C.V., Wong W.K.R., and Hackett J. Extracellular expression of human epidermal growth factor encoded by an Escherichia coli K-12 plasmid stabilized by the ytl2-inc R system of Salmonella typhimurium. J. Ind. Microbiol. Biotechnol. 21 (1998) 31-36
    • (1998) J. Ind. Microbiol. Biotechnol. , vol.21 , pp. 31-36
    • Wong, D.H.K.1    Lam, K.H.E.2    Chan, C.K.P.3    Wong, Y.C.V.4    Wong, W.K.R.5    Hackett, J.6
  • 27
    • 0345801344 scopus 로고    scopus 로고
    • Streptokinase - a clinically important thrombolytic agent
    • Banerjee A., Chisti Y., and Banerjee U.C. Streptokinase - a clinically important thrombolytic agent. Biotechnol. Adv. 22 (2004) 287-307
    • (2004) Biotechnol. Adv. , vol.22 , pp. 287-307
    • Banerjee, A.1    Chisti, Y.2    Banerjee, U.C.3
  • 28
    • 0021245163 scopus 로고
    • Streptokinase: cloning, expression and excretion by Escherichia coli
    • Malke H., and Ferretti J.J. Streptokinase: cloning, expression and excretion by Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 81 (1984) 3557-3561
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3557-3561
    • Malke, H.1    Ferretti, J.J.2
  • 30
    • 0031751888 scopus 로고    scopus 로고
    • Overexpression of streptokinase using a fed-batch strategy
    • Yazdani S.S., and Mukherjee K.J. Overexpression of streptokinase using a fed-batch strategy. Biotechnol. Lett. 20 10 (1998) 923-927
    • (1998) Biotechnol. Lett. , vol.20 , Issue.10 , pp. 923-927
    • Yazdani, S.S.1    Mukherjee, K.J.2
  • 31
    • 0033369368 scopus 로고    scopus 로고
    • Two streptokinase genes are expressed with different solubility in Escherichia coli W3110
    • Pupo E., Baghbaderani B.A., Lugo V., Fernandez J., Paez R., and Torrens I. Two streptokinase genes are expressed with different solubility in Escherichia coli W3110. Biotechnol. Lett. 21 (1999) 1119-1123
    • (1999) Biotechnol. Lett. , vol.21 , pp. 1119-1123
    • Pupo, E.1    Baghbaderani, B.A.2    Lugo, V.3    Fernandez, J.4    Paez, R.5    Torrens, I.6
  • 32
    • 33845569361 scopus 로고    scopus 로고
    • Effects of post-induction feed strategies on secretory production of recombinant streptokinase in Escherichia coli
    • Ramalingam S., Gautam P., Mukherjee K.J., and Jayaraman G. Effects of post-induction feed strategies on secretory production of recombinant streptokinase in Escherichia coli. Biochem. Eng. J. 33 (2007) 33-41
    • (2007) Biochem. Eng. J. , vol.33 , pp. 33-41
    • Ramalingam, S.1    Gautam, P.2    Mukherjee, K.J.3    Jayaraman, G.4
  • 33
    • 0031841932 scopus 로고    scopus 로고
    • Effect of signal peptide change on the extracellular processing of streptokinase from Escherichia coli: requirement for secondary structure at the cleavage junction
    • Pratap J., and Dikshit K.L. Effect of signal peptide change on the extracellular processing of streptokinase from Escherichia coli: requirement for secondary structure at the cleavage junction. Mol. Gen. Genet. 258 (1998) 326-333
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 326-333
    • Pratap, J.1    Dikshit, K.L.2
  • 34
    • 0035723632 scopus 로고    scopus 로고
    • Continuous-culture studies on the stability and expression of recombinant streptokinase in Escherichia coli
    • Yazdani S.S., and Mukherjee K.J. Continuous-culture studies on the stability and expression of recombinant streptokinase in Escherichia coli. Bioprocess. Biosyst. Eng. 24 (2002) 341-346
    • (2002) Bioprocess. Biosyst. Eng. , vol.24 , pp. 341-346
    • Yazdani, S.S.1    Mukherjee, K.J.2
  • 35
    • 0030175042 scopus 로고    scopus 로고
    • Periplasmic Expression of Biologically Active Vesicular Stomatitis Virus Phosphoprotein P in Escherichia coli
    • Pahari S., Pari A., and Chattopadhyay D.J. Periplasmic Expression of Biologically Active Vesicular Stomatitis Virus Phosphoprotein P in Escherichia coli. Prot. Expr. Purif. 7 (1996) 384-388
    • (1996) Prot. Expr. Purif. , vol.7 , pp. 384-388
    • Pahari, S.1    Pari, A.2    Chattopadhyay, D.J.3
  • 36
    • 0035503217 scopus 로고    scopus 로고
    • EcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli
    • Dartigalongue C., Loferer H., and Raina S. EcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli. EMBO J. 20 21 (2001) 5908-5918
    • (2001) EMBO J. , vol.20 , Issue.21 , pp. 5908-5918
    • Dartigalongue, C.1    Loferer, H.2    Raina, S.3
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0037106027 scopus 로고    scopus 로고
    • Affinity panning of peptide libraries using anti-streptokinase monoclonal antibodies: selection of an inhibitor of plasminogen active site
    • Parhami-Seren B., Krudysz J., and Tsantili P. Affinity panning of peptide libraries using anti-streptokinase monoclonal antibodies: selection of an inhibitor of plasminogen active site. J. Immunol. Methods 267 (2002) 185-198
    • (2002) J. Immunol. Methods , vol.267 , pp. 185-198
    • Parhami-Seren, B.1    Krudysz, J.2    Tsantili, P.3
  • 39
    • 0027909877 scopus 로고
    • Response dynamics of 26-, 34-, 39-, 54- and 80-kDa proteases in induced cultures of recombinant Escherichia coli
    • Harcum S.W., and Bentley W.E. Response dynamics of 26-, 34-, 39-, 54- and 80-kDa proteases in induced cultures of recombinant Escherichia coli. Biotechnol. Bioeng. 42 (1993) 675-685
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 675-685
    • Harcum, S.W.1    Bentley, W.E.2
  • 41
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn J.M., Neher S.B., Kim Y.I., Sauer R.T., and Baker T.A. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell. 11 (2003) 671-683
    • (2003) Mol. Cell. , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 42
    • 0027519423 scopus 로고
    • Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli
    • Wojtkowiak D., Georgopoulos C., and Zylicz M. Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli. J. Biol. Chem. 268 30 (1993) 22609-22617
    • (1993) J. Biol. Chem. , vol.268 , Issue.30 , pp. 22609-22617
    • Wojtkowiak, D.1    Georgopoulos, C.2    Zylicz, M.3
  • 43
    • 0031000010 scopus 로고    scopus 로고
    • Secretion-dependent proteolysis of recombinant proteins is associated with inhibition of cell growth in Escherichia coli
    • Viaplana E., Rebordosa X., Pinol J., and Villaverde A. Secretion-dependent proteolysis of recombinant proteins is associated with inhibition of cell growth in Escherichia coli. Biotechnol. Lett. 19 4 (1997) 373-377
    • (1997) Biotechnol. Lett. , vol.19 , Issue.4 , pp. 373-377
    • Viaplana, E.1    Rebordosa, X.2    Pinol, J.3    Villaverde, A.4
  • 44
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • Strauch K.L., and Bechwith J. Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J. Bacteriol. 171 5 (1989) 2689-2696
    • (1989) J. Bacteriol. , vol.171 , Issue.5 , pp. 2689-2696
    • Strauch, K.L.1    Bechwith, J.2
  • 45
    • 0025855940 scopus 로고
    • Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo
    • Baneyx F., and Georgiou G. Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo. J. Bacteriol. 173 (1991) 2696-2703
    • (1991) J. Bacteriol. , vol.173 , pp. 2696-2703
    • Baneyx, F.1    Georgiou, G.2
  • 46
    • 0026513218 scopus 로고
    • Tsp: A tail-specific protease that selectively degrades proteins with non-polar C termini
    • Silber K.R., Keiler K.C., and Sauer R.T. Tsp: A tail-specific protease that selectively degrades proteins with non-polar C termini. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 295-299
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 295-299
    • Silber, K.R.1    Keiler, K.C.2    Sauer, R.T.3
  • 47
    • 0026675533 scopus 로고
    • Control of in vivo proteolysis in the production of recombinant proteins
    • Enfors S.O. Control of in vivo proteolysis in the production of recombinant proteins. Trends Biotechnol. 10 (1992) 310-315
    • (1992) Trends Biotechnol. , vol.10 , pp. 310-315
    • Enfors, S.O.1
  • 50
    • 0031940586 scopus 로고    scopus 로고
    • Isolation of recombinant secretory proteins by limited induction and quantitative harvest
    • Rosenberg H.F. Isolation of recombinant secretory proteins by limited induction and quantitative harvest. BioTechniques 24 (1998) 188-191
    • (1998) BioTechniques , vol.24 , pp. 188-191
    • Rosenberg, H.F.1
  • 51
    • 1542285366 scopus 로고    scopus 로고
    • Secretion capacity limitations of the Sec pathway in Escherichia coli
    • Mergulhao F.J., and Monteiro G.A. Secretion capacity limitations of the Sec pathway in Escherichia coli. J. Microb. Biotechnol. 14 (2004) 128-133
    • (2004) J. Microb. Biotechnol. , vol.14 , pp. 128-133
    • Mergulhao, F.J.1    Monteiro, G.A.2
  • 52
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • Schein C.H. Production of soluble recombinant proteins in bacteria. Bio/Technology 7 (1989) 1141-1148
    • (1989) Bio/Technology , vol.7 , pp. 1141-1148
    • Schein, C.H.1
  • 53
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant streptokinase in the cytoplasm of Escherichia coli
    • Sorenson H.P., and Mortensen K.K. Soluble expression of recombinant streptokinase in the cytoplasm of Escherichia coli. Microbiol. Cell. Factory 4 (2005) 1
    • (2005) Microbiol. Cell. Factory , vol.4 , pp. 1
    • Sorenson, H.P.1    Mortensen, K.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.