메뉴 건너뛰기




Volumn 109, Issue 4, 2012, Pages 983-991

Investigation of the impact of Tat export pathway enhancement on E. coli culture, protein production and early stage recovery

Author keywords

Cell engineering; Clarification; Fermentation; Robustness; Tat pathway

Indexed keywords

BIOPROCESSES; CELL INTEGRITY; DETRIMENTAL EFFECTS; DOWNSTREAM-PROCESSING; E. COLI; FOLDED PROTEINS; GROWTH MEDIUM; INNER MEMBRANES; INTACT CELLS; MEMBRANE INTEGRITY; MEMBRANE PROTEINS; OVER-EXPRESSION; PERIPLASMIC ACCUMULATION; PROTEIN ACCUMULATION; PROTEIN PRODUCTION; SCALE-DOWN; SCALEABLE; SPHEROPLASTS; SUBSTRATE PROTEINS; TAT PATHWAY; TWIN-ARGININE TRANSLOCATIONS; WILD TYPES;

EID: 84857445113     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24384     Document Type: Article
Times cited : (18)

References (38)
  • 1
    • 67650672141 scopus 로고    scopus 로고
    • Advances in product release strategies and impact on bioprocess design
    • Balasundaram B, Harrison S, Bracewell DG. 2009a. Advances in product release strategies and impact on bioprocess design. Trends Biotechnol 27(8):477-485.
    • (2009) Trends Biotechnol , vol.27 , Issue.8 , pp. 477-485
    • Balasundaram, B.1    Harrison, S.2    Bracewell, D.G.3
  • 2
    • 67650692398 scopus 로고    scopus 로고
    • Step change in the efficiency of centrifugation through cell engineering: Coexpression of Staphylococcal nuclease to reduce the viscosity of the bioprocess feedstock
    • Balasundaram B, Nesbeth D, Ward JM, Keshavarz Moore E, Bracewell DG. 2009b. Step change in the efficiency of centrifugation through cell engineering: Coexpression of Staphylococcal nuclease to reduce the viscosity of the bioprocess feedstock. Biotechnol Bioeng 104(1):134-142.
    • (2009) Biotechnol Bioeng , vol.104 , Issue.1 , pp. 134-142
    • Balasundaram, B.1    Nesbeth, D.2    Ward, J.M.3    Keshavarz Moore, E.4    Bracewell, D.G.5
  • 3
    • 0037414423 scopus 로고    scopus 로고
    • Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli
    • Barrett CML, Ray N, Thomas JD, Robinson C, Bolhuis A. 2003. Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli. Biochem Biophys Res Commun 304(2):279-284.
    • (2003) Biochem Biophys Res Commun , vol.304 , Issue.2 , pp. 279-284
    • Barrett, C.M.L.1    Ray, N.2    Thomas, J.D.3    Robinson, C.4    Bolhuis, A.5
  • 4
    • 0014044956 scopus 로고
    • Production and ultrastructure of lysozyme and ethylenediaminetetraacetate-lysozyme spheroplasts of Escherichia coli
    • Birdsell DC, Cota-Robles EH. 1967. Production and ultrastructure of lysozyme and ethylenediaminetetraacetate-lysozyme spheroplasts of Escherichia coli. J Bacteriol 93(1):427-437.
    • (1967) J Bacteriol , vol.93 , Issue.1 , pp. 427-437
    • Birdsell, D.C.1    Cota-Robles, E.H.2
  • 5
    • 0034697250 scopus 로고    scopus 로고
    • Subunit interactions in the twin-arginine translocase complex of Escherichia coli
    • Bolhuis A, Bogsch EG, Robinson C. 2000. Subunit interactions in the twin-arginine translocase complex of Escherichia coli. FEBS Lett 472(1):88-892.
    • (2000) FEBS Lett , vol.472 , Issue.1 , pp. 88-892
    • Bolhuis, A.1    Bogsch, E.G.2    Robinson, C.3
  • 6
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • Bolhuis A, Mathers JE, Thomas JD, Barrett CML, Robinson C. 2001. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J Biol Chem 276(23):20213-20219.
    • (2001) J Biol Chem , vol.276 , Issue.23 , pp. 20213-20219
    • Bolhuis, A.1    Mathers, J.E.2    Thomas, J.D.3    Barrett, C.M.L.4    Robinson, C.5
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72(1-2):248-254.
    • (1976) Anal Biochem , vol.72 , Issue.1-2 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0000366608 scopus 로고
    • Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: In vivo probe for transcriptional control sequences
    • Casadaban MJ, Cohen SN. 1979. Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: In vivo probe for transcriptional control sequences. Proc Natl Acad Sci USA 76(9):4530-4533.
    • (1979) Proc Natl Acad Sci USA , vol.76 , Issue.9 , pp. 4530-4533
    • Casadaban, M.J.1    Cohen, S.N.2
  • 11
    • 0030600480 scopus 로고    scopus 로고
    • A set of compatible tac promoter expression vectors
    • Dykxhoorn DM, St. Pierre R, Linn T. 1996. A set of compatible tac promoter expression vectors. Gene 177(1-2):133-136.
    • (1996) Gene , vol.177 , Issue.1-2 , pp. 133-136
    • Dykxhoorn, D.M.1    St Pierre, R.2    Linn, T.3
  • 13
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: Status report and future prospects
    • Georgiou G, Segatori L. 2005. Preparative expression of secreted proteins in bacteria: Status report and future prospects. Curr Opin Biotechnol 16(5):538-545.
    • (2005) Curr Opin Biotechnol , vol.16 , Issue.5 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 14
    • 33750587201 scopus 로고    scopus 로고
    • Manufacturing of recombinant therapeutic proteins in microbial systems
    • Graumann K, Premstaller A. 2006. Manufacturing of recombinant therapeutic proteins in microbial systems. Biotechnol J 1(2):164-186.
    • (2006) Biotechnol J , vol.1 , Issue.2 , pp. 164-186
    • Graumann, K.1    Premstaller, A.2
  • 15
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith JON. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177(14):4121-4130.
    • (1995) J Bacteriol , vol.177 , Issue.14 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.O.N.4
  • 16
    • 0029945829 scopus 로고    scopus 로고
    • Production of antibody fragments in Escherichia coli
    • Harrison J, Keshavarz-Moore E. 1996. Production of antibody fragments in Escherichia coli. Ann N Y Acad Sci 782:143-158.
    • (1996) Ann N Y Acad Sci , vol.782 , pp. 143-158
    • Harrison, J.1    Keshavarz-Moore, E.2
  • 17
    • 0343133961 scopus 로고    scopus 로고
    • Turbulent breakage of filamentous bacteria in mechanically agitated batch culture
    • Heydarian SM, Ison AP, Lilly MD, Shamlou PA. 2000. Turbulent breakage of filamentous bacteria in mechanically agitated batch culture. Chem Eng Sci 55:1775-1784.
    • (2000) Chem Eng Sci , vol.55 , pp. 1775-1784
    • Heydarian, S.M.1    Ison, A.P.2    Lilly, M.D.3    Shamlou, P.A.4
  • 18
    • 33749364369 scopus 로고    scopus 로고
    • Shear stress analysis of mammalian cell suspensions for prediction of industrial centrifugation and its verification
    • Hutchinson N, Bingham N, Murrell N, Farid S, Hoare M. 2006. Shear stress analysis of mammalian cell suspensions for prediction of industrial centrifugation and its verification. Biotechnol Bioeng 95(3):483-491.
    • (2006) Biotechnol Bioeng , vol.95 , Issue.3 , pp. 483-491
    • Hutchinson, N.1    Bingham, N.2    Murrell, N.3    Farid, S.4    Hoare, M.5
  • 19
    • 0038460119 scopus 로고    scopus 로고
    • Role of the Escherichia coli Tat pathway in outer membrane integrity
    • Ize B, Stanley NR, Buchanan G, Palmer T. 2003. Role of the Escherichia coli Tat pathway in outer membrane integrity. Mol Microbiol 48(5):1183-1193.
    • (2003) Mol Microbiol , vol.48 , Issue.5 , pp. 1183-1193
    • Ize, B.1    Stanley, N.R.2    Buchanan, G.3    Palmer, T.4
  • 20
    • 9144251714 scopus 로고    scopus 로고
    • Novel phenotypes of Escherichia coli tat mutants revealed by global gene expression and phenotypic analysis
    • Ize B, Porcelli I, Lucchini S, Hinton JC, Berks BC, Palmer T. 2004. Novel phenotypes of Escherichia coli tat mutants revealed by global gene expression and phenotypic analysis. J Biol Chem 279(46):47543-47554.
    • (2004) J Biol Chem , vol.279 , Issue.46 , pp. 47543-47554
    • Ize, B.1    Porcelli, I.2    Lucchini, S.3    Hinton, J.C.4    Berks, B.C.5    Palmer, T.6
  • 21
    • 67349255281 scopus 로고    scopus 로고
    • TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli
    • Matos CFRO, Di Cola A, Robinson C. 2009. TatD is a central component of a Tat translocon-initiated quality control system for exported FeS proteins in Escherichia coli. EMBO Rep 10(5):474-479.
    • (2009) EMBO Rep , vol.10 , Issue.5 , pp. 474-479
    • Matos, C.F.R.O.1    Di Cola, A.2    Robinson, C.3
  • 22
    • 5444249124 scopus 로고    scopus 로고
    • Bioprocess equipment: Characterization of energy dissipation rate and its potential to damage cells
    • Mollet M, Ma N, Zhao Y, Brodkey R, Taticek R, Chalmers JJ. 2004. Bioprocess equipment: Characterization of energy dissipation rate and its potential to damage cells. Biotechnol Prog 20(5):1437-1448.
    • (2004) Biotechnol Prog , vol.20 , Issue.5 , pp. 1437-1448
    • Mollet, M.1    Ma, N.2    Zhao, Y.3    Brodkey, R.4    Taticek, R.5    Chalmers, J.J.6
  • 23
    • 0037454676 scopus 로고    scopus 로고
    • Ultra scale-down approach for the prediction of full-scale recovery of ovine polycolonal immunoglobulins used in the manufacture of snake venom-specific Fab fragment
    • Neal G, Christie J, Keshavarz-Moore E, Shamlou PA. 2003. Ultra scale-down approach for the prediction of full-scale recovery of ovine polycolonal immunoglobulins used in the manufacture of snake venom-specific Fab fragment. Biotechnol Bioeng 81(2):149-157.
    • (2003) Biotechnol Bioeng , vol.81 , Issue.2 , pp. 149-157
    • Neal, G.1    Christie, J.2    Keshavarz-Moore, E.3    Shamlou, P.A.4
  • 24
    • 0031549641 scopus 로고    scopus 로고
    • Factors determining more efficient large-scale release of a periplasmic enzyme from E. coli using lysozyme
    • Pierce JJ, Turner C, Keshavarz-Moore E, Dunnill P. 1997. Factors determining more efficient large-scale release of a periplasmic enzyme from E. coli using lysozyme. J Biotechnol 58(1):1-11.
    • (1997) J Biotechnol , vol.58 , Issue.1 , pp. 1-11
    • Pierce, J.J.1    Turner, C.2    Keshavarz-Moore, E.3    Dunnill, P.4
  • 25
    • 0022553762 scopus 로고
    • Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E. coli
    • Randall LL, Hardy SJS. 1986. Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E. coli. Cell 46(6):921-928.
    • (1986) Cell , vol.46 , Issue.6 , pp. 921-928
    • Randall, L.L.1    Hardy, S.J.S.2
  • 26
    • 8844280791 scopus 로고    scopus 로고
    • Tat-dependent protein targeting in prokaryotes and chloroplasts
    • Robinson C, Bolhuis A. 2004. Tat-dependent protein targeting in prokaryotes and chloroplasts. Biochim Biophys Acta (BBA) Mol Cell Res 1694(1-3):135-147.
    • (2004) Biochim Biophys Acta (BBA) Mol Cell Res , vol.1694 , Issue.1-3 , pp. 135-147
    • Robinson, C.1    Bolhuis, A.2
  • 27
    • 0032127435 scopus 로고    scopus 로고
    • Overlapping functions of components of a bacterial Sec-independent protein export pathway
    • Sargent F, Bogsch EG, Stanley NR, Wexler M, Robinson C, Berks BC, Palmer T. 1998. Overlapping functions of components of a bacterial Sec-independent protein export pathway. EMBO J 17(13):3640-3650.
    • (1998) EMBO J , vol.17 , Issue.13 , pp. 3640-3650
    • Sargent, F.1    Bogsch, E.G.2    Stanley, N.R.3    Wexler, M.4    Robinson, C.5    Berks, B.C.6    Palmer, T.7
  • 29
    • 70349319681 scopus 로고    scopus 로고
    • Ultra scale-down prediction using microwell technology of the industrial scale clarification characteristics by centrifugation of mammalian cell broths
    • Tait AS, Aucamp JP, Bugeon A, Hoare M. 2009. Ultra scale-down prediction using microwell technology of the industrial scale clarification characteristics by centrifugation of mammalian cell broths. Biotechnol Bioeng 104(2):321-331.
    • (2009) Biotechnol Bioeng , vol.104 , Issue.2 , pp. 321-331
    • Tait, A.S.1    Aucamp, J.P.2    Bugeon, A.3    Hoare, M.4
  • 30
    • 0035181362 scopus 로고    scopus 로고
    • Export of active green fluorescent protein to the periplasm by the twin arginine translocase (Tat) pathway in Escherichia coli
    • Thomas JD, Daniel RA, Errington J, Robinson C. 2001. Export of active green fluorescent protein to the periplasm by the twin arginine translocase (Tat) pathway in Escherichia coli. Mol Microbiol 39(1):47-53.
    • (2001) Mol Microbiol , vol.39 , Issue.1 , pp. 47-53
    • Thomas, J.D.1    Daniel, R.A.2    Errington, J.3    Robinson, C.4
  • 33
    • 33746163862 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2006
    • Walsh G. 2006. Biopharmaceutical benchmarks 2006. Nat Biotechnol 24(7):769-776.
    • (2006) Nat Biotechnol , vol.24 , Issue.7 , pp. 769-776
    • Walsh, G.1
  • 34
    • 77956458110 scopus 로고    scopus 로고
    • Post-translational modifications of protein biopharmaceuticals
    • Walsh G. 2010. Post-translational modifications of protein biopharmaceuticals. Drug Discov Today 15(17-18):773-780.
    • (2010) Drug Discov Today , vol.15 , Issue.17-18 , pp. 773-780
    • Walsh, G.1
  • 37
    • 0033644297 scopus 로고    scopus 로고
    • The engineering effects of fluids flow on freely suspended biological macro-materials and macromolecules
    • Yim SSS, Shamlou PA. 2000. The engineering effects of fluids flow on freely suspended biological macro-materials and macromolecules. Adv Biochem Eng Biotechnol 67:83-122.
    • (2000) Adv Biochem Eng Biotechnol , vol.67 , pp. 83-122
    • Yim, S.S.S.1    Shamlou, P.A.2
  • 38
    • 34547855540 scopus 로고    scopus 로고
    • Prediction of shear damage of plasmid DNA in pump and centrifuge operations using an ultra scale-down device
    • Zhang H, Kong S, Booth A, Boushaba R, Levy MS, Hoare M. 2007. Prediction of shear damage of plasmid DNA in pump and centrifuge operations using an ultra scale-down device. Biotechnol Prog 23(4):858-865.
    • (2007) Biotechnol Prog , vol.23 , Issue.4 , pp. 858-865
    • Zhang, H.1    Kong, S.2    Booth, A.3    Boushaba, R.4    Levy, M.S.5    Hoare, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.