메뉴 건너뛰기




Volumn 30, Issue 2, 2014, Pages 281-290

Efficient export of prefolded, disulfide-bonded recombinant proteins to the periplasm by the Tat pathway in Escherichia coli CyDisCo strains

Author keywords

Cell engineering; E. coli; Fermentation; Protein export; Tat pathway

Indexed keywords

CELL ENGINEERING; CELL MEMBRANES; COVALENT BONDS; CYTOLOGY; ESCHERICHIA COLI; FERMENTATION; INTERNATIONAL TRADE; MASS SPECTROMETRY; PHOSPHATASES; RECOMBINANT PROTEINS;

EID: 84898543333     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1858     Document Type: Article
Times cited : (41)

References (23)
  • 2
    • 77956458110 scopus 로고    scopus 로고
    • Post-translational modifications of protein biopharmaceuticals
    • Walsh G. Post-translational modifications of protein biopharmaceuticals. Drug Discov Today. 2010;15:773-780.
    • (2010) Drug Discov Today , vol.15 , pp. 773-780
    • Walsh, G.1
  • 3
    • 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. Factors determining more efficient large-scale release of a periplasmic enzyme from E. coli using lysozyme. J Biotechnol. 1997;58:1-11.
    • (1997) J Biotechnol , vol.58 , pp. 1-11
    • Pierce, J.J.1    Turner, C.2    Keshavarz-Moore, E.3    Dunnill, P.4
  • 4
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: status report and future prospects
    • Georgiou G, Segatori L. Preparative expression of secreted proteins in bacteria: status report and future prospects. Curr Opin Biotechnol. 2005;16:538-545.
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 5
    • 84898546880 scopus 로고    scopus 로고
    • The Tat system of Gram-positive bacteria. Biochim Biophys Acta. In press.
    • Goosens VJ, Monteferrante CG, van Dijl J-M. The Tat system of Gram-positive bacteria. Biochim Biophys Acta. In press.
    • Goosens, V.J.1    Monteferrante, C.G.2    van Dijl, J.-M.3
  • 6
    • 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. Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Mol Microbiol. 2001;39:47-53.
    • (2001) Mol Microbiol , vol.39 , pp. 47-53
    • Thomas, J.D.1    Daniel, R.A.2    Errington, J.3    Robinson, C.4
  • 8
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • Delisa MP, Tullman D and Georgiou, G. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway. Proc Natl Acad Sci USA. 2003;100, 6115-20.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6115-6120
    • Delisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 9
    • 84864835788 scopus 로고    scopus 로고
    • Coexpression of molecular chaperone enhances activity and export of organophosphorus hydrolase in Escherichia coli
    • Kang DG, Kim CS, Seo JH, Kim IG, Choi SS, Ha JH, Nam SW, Lim G, Cha HJ. Coexpression of molecular chaperone enhances activity and export of organophosphorus hydrolase in Escherichia coli. Biotechnol Prog. 2012;28:925-930.
    • (2012) Biotechnol Prog , vol.28 , pp. 925-930
    • Kang, D.G.1    Kim, C.S.2    Seo, J.H.3    Kim, I.G.4    Choi, S.S.5    Ha, J.H.6    Nam, S.W.7    Lim, G.8    Cha, H.J.9
  • 11
    • 84857445113 scopus 로고    scopus 로고
    • Investigation of the impact of Tat export pathway enhancement on E. coli culture, protein production and early stage recovery
    • Branston SD, Matos CFRO, Freedman RB, Robinson C, Keshavarz-Moore E. Investigation of the impact of Tat export pathway enhancement on E. coli culture, protein production and early stage recovery. Biotechnol Bioeng. 2012;109:983-991.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 983-991
    • Branston, S.D.1    Matos, C.F.R.O.2    Freedman, R.B.3    Robinson, C.4    Keshavarz-Moore, E.5
  • 13
    • 0035812702 scopus 로고    scopus 로고
    • Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion
    • Ritz D, Lim J, Reynolds CM, Poole LB, Beckwith J. Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion. Science. 2001;294:158-160.
    • (2001) Science , vol.294 , pp. 158-160
    • Ritz, D.1    Lim, J.2    Reynolds, C.M.3    Poole, L.B.4    Beckwith, J.5
  • 14
    • 44349171036 scopus 로고    scopus 로고
    • Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways
    • Faulkner MJ, Veeravalli K, Gon S, Georgiou G, Beckwith J. Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways. Proc Natl Acad Sci USA. 2008, 105:6735-6740.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6735-6740
    • Faulkner, M.J.1    Veeravalli, K.2    Gon, S.3    Georgiou, G.4    Beckwith, J.5
  • 16
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz WA, Åslund F, Holmgren A, Beckwith J. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J Biol Chem. 1997;272:15661-15667.
    • (1997) J Biol Chem , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Åslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 17
    • 78651484550 scopus 로고    scopus 로고
    • Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli
    • Hatahet F, Nguyen VD, Salo KEH, Ruddock LW. Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli. Microb Cell Fact. 2010;9:67.
    • (2010) Microb Cell Fact , vol.9 , pp. 67
    • Hatahet, F.1    Nguyen, V.D.2    Salo, K.E.H.3    Ruddock, L.W.4
  • 18
    • 78650965365 scopus 로고    scopus 로고
    • Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E. coli
    • Nguyen VD, Hatahet F, Salo KEH, Enlund E, Zhang C, Ruddock LW. Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E. coli. Microb Cell Fact. 2011;10:1.
    • (2011) Microb Cell Fact , vol.10 , pp. 1
    • Nguyen, V.D.1    Hatahet, F.2    Salo, K.E.H.3    Enlund, E.4    Zhang, C.5    Ruddock, L.W.6
  • 19
    • 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. 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. 1986;46:921-928.
    • (1986) Cell , vol.46 , pp. 921-928
    • Randall, L.L.1    Hardy, S.J.S.2
  • 20
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm M, Shevchenko A, Houthaeve T, Breit S, Schweigerer L, Fotsis T, Mann M. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature. 1996;379:466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 21
    • 15744375548 scopus 로고    scopus 로고
    • The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein disulfide isomerase DsbC
    • Berkmen M, Boyd D, Beckwith J. The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein disulfide isomerase DsbC. J Biol Chem. 2005;280:11387-11394.
    • (2005) J Biol Chem , vol.280 , pp. 11387-11394
    • Berkmen, M.1    Boyd, D.2    Beckwith, J.3
  • 23
    • 77956318615 scopus 로고    scopus 로고
    • Mechanisms of oxidative protein folding in the bacterial cell envelope
    • Kadokura H, Beckwith J. Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid Redox Signal. 2010;13:1231-1246.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1231-1246
    • Kadokura, H.1    Beckwith, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.