메뉴 건너뛰기




Volumn 122, Issue 4, 2006, Pages 412-421

Coexpression of TorD enhances the transport of GFP via the TAT pathway

Author keywords

Green fluorescence protein; Secretion; TorD; Twin arginine pathway

Indexed keywords

BACTERIA; FLUORESCENCE; GENETIC ENGINEERING; PROTEINS;

EID: 33645365498     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2005.09.011     Document Type: Article
Times cited : (36)

References (37)
  • 2
    • 0037414423 scopus 로고    scopus 로고
    • Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli
    • C.M. Barrett, N. Ray, J.D. Thomas, C. Robinson, and A. Bolhuis Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli Biochem. Biophys. Res. Commun. 304 2003 279 284
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 279-284
    • Barrett, C.M.1    Ray, N.2    Thomas, J.D.3    Robinson, C.4    Bolhuis, A.5
  • 3
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • B.C. Berks A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 22 1996 393 404
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 5
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • P.H. Bessette, F. Aslund, J. Beckwith, and G. Georgiou Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm Proc. Natl. Acad. Sci. U.S.A. 96 1999 13703 13708
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 6
    • 0037274388 scopus 로고    scopus 로고
    • An alternative model of the twin arginine translocation system
    • T. Bruser, and C. Sanders An alternative model of the twin arginine translocation system Microbiol. Res. 158 2003 7 17
    • (2003) Microbiol. Res. , vol.158 , pp. 7-17
    • Bruser, T.1    Sanders, C.2
  • 7
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • M.J. Casadaban Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu J. Mol. Biol. 104 1976 541 555
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 8
    • 0037470623 scopus 로고    scopus 로고
    • Specific inhibition of the translocation of a subset of Escherichia coli TAT substrates by the TorA signal peptide
    • A. Chanal, C.L. Santini, and L.F. Wu Specific inhibition of the translocation of a subset of Escherichia coli TAT substrates by the TorA signal peptide J. Mol. Biol. 327 2003 563 570
    • (2003) J. Mol. Biol. , vol.327 , pp. 563-570
    • Chanal, A.1    Santini, C.L.2    Wu, L.F.3
  • 9
    • 0035014528 scopus 로고    scopus 로고
    • Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS)
    • G. Chen, A. Hayhurst, J.G. Thomas, B.R. Harvey, B.L. Iverson, and G. Georgiou Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS) Nat. Biotechnol. 19 2001 537 542
    • (2001) Nat. Biotechnol. , vol.19 , pp. 537-542
    • Chen, G.1    Hayhurst, A.2    Thomas, J.G.3    Harvey, B.R.4    Iverson, B.L.5    Georgiou, G.6
  • 10
    • 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
    • K. Cline, W.F. Ettinger, and S.M. Theg 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. 267 1992 2688 2696
    • (1992) J. Biol. Chem. , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettinger, W.F.2    Theg, S.M.3
  • 11
    • 0015385368 scopus 로고
    • Nonchromosomal antibiotic resistance in bacteria: Genetic transformation of Escherichia coli by R-factor DNA
    • S.N. Cohen, A.C. Chang, and L. Hsu Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA Proc. Natl. Acad. Sci. U.S.A. 69 1972 2110 2114
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.2    Hsu, L.3
  • 12
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • B.P. Cormack, R.H. Valdivia, and S. Falkow FACS-optimized mutants of the green fluorescent protein (GFP) Gene 173 1996 33 38
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 13
    • 0346655242 scopus 로고    scopus 로고
    • Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway
    • M.P. DeLisa, P. Lee, T. Palmer, and G. Georgiou Phage shock protein PspA of Escherichia coli relieves saturation of protein export via the Tat pathway J. Bacteriol. 186 2004 366 373
    • (2004) J. Bacteriol. , vol.186 , pp. 366-373
    • Delisa, M.P.1    Lee, P.2    Palmer, T.3    Georgiou, G.4
  • 14
    • 0037119435 scopus 로고    scopus 로고
    • Genetic analysis of the twin arginine translocator secretion pathway in bacteria
    • M.P. DeLisa, P. Samuelson, T. Palmer, and G. Georgiou Genetic analysis of the twin arginine translocator secretion pathway in bacteria J. Biol. Chem. 277 2002 29825 29831
    • (2002) J. Biol. Chem. , vol.277 , pp. 29825-29831
    • Delisa, M.P.1    Samuelson, P.2    Palmer, T.3    Georgiou, G.4
  • 15
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
    • M.P. DeLisa, D. Tullman, and G. Georgiou Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway Proc. Natl. Acad. Sci. U.S.A. 100 2003 6115 6120
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6115-6120
    • Delisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 16
    • 0042564757 scopus 로고    scopus 로고
    • Assembly of Tat-dependent [NiFe] hydrogenases: Identification of precursor-binding accessory proteins
    • A. Dubini, and F. Sargent Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins FEBS Lett. 549 2003 141 146
    • (2003) FEBS Lett. , vol.549 , pp. 141-146
    • Dubini, A.1    Sargent, F.2
  • 17
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • L.M. Guzman, D. Belin, M.J. Carson, and J. Beckwith Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter J. Bacteriol. 177 1995 4121 4130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 20
    • 77957010716 scopus 로고
    • Bacterial membranes
    • H.R. Kaback Bacterial membranes Methods Enzymol. 22 1971 99 120
    • (1971) Methods Enzymol. , vol.22 , pp. 99-120
    • Kaback, H.R.1
  • 21
    • 0034046020 scopus 로고    scopus 로고
    • The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue
    • A.W. Karzai, E.D. Roche, and R.T. Sauer The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue Nat. Struct. Biol. 7 2000 449 455
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 449-455
    • Karzai, A.W.1    Roche, E.D.2    Sauer, R.T.3
  • 22
    • 0035996719 scopus 로고    scopus 로고
    • Using secretion to solve a solubility problem: High-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGase F
    • T. Loo, M.L. Patchett, G.E. Norris, and J.S. Lott Using secretion to solve a solubility problem: high-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGase F Protein Expr. Purif. 24 2002 90 98
    • (2002) Protein Expr. Purif. , vol.24 , pp. 90-98
    • Loo, T.1    Patchett, M.L.2    Norris, G.E.3    Lott, J.S.4
  • 23
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • S.C. Makrides 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
  • 24
    • 0033407138 scopus 로고    scopus 로고
    • Requirement for phospholipids of the translocation of the trimethylamine N-oxide reductase through the Tat pathway in Escherichia coli
    • N.I. Mikhaleva, C.L. Santini, G. Giordano, M.A. Nesmeyanova, and L.F. Wu Requirement for phospholipids of the translocation of the trimethylamine N-oxide reductase through the Tat pathway in Escherichia coli FEBS Lett. 463 1999 331 335
    • (1999) FEBS Lett. , vol.463 , pp. 331-335
    • Mikhaleva, N.I.1    Santini, C.L.2    Giordano, G.3    Nesmeyanova, M.A.4    Wu, L.F.5
  • 25
    • 0035038589 scopus 로고    scopus 로고
    • Identification of a twin-arginine leader-binding protein
    • I.J. Oresnik, C.L. Ladner, and R.J. Turner Identification of a twin-arginine leader-binding protein Mol. Microbiol. 40 2001 323 331
    • (2001) Mol. Microbiol. , vol.40 , pp. 323-331
    • Oresnik, I.J.1    Ladner, C.L.2    Turner, R.J.3
  • 26
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor
    • M. Paetzel, R.E. Dalbey, and N.C. Strynadka Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor Nature 396 1998 186 190
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 27
    • 16244380460 scopus 로고    scopus 로고
    • Export of complex cofactor-containing proteins by the bacterial Tat pathway
    • T. Palmer, F. Sargent, and B.C. Berks Export of complex cofactor-containing proteins by the bacterial Tat pathway Trends Microbiol. 13 2005 175 180
    • (2005) Trends Microbiol. , vol.13 , pp. 175-180
    • Palmer, T.1    Sargent, F.2    Berks, B.C.3
  • 28
    • 0025008174 scopus 로고
    • Translocation of proteins with signal sequences across membranes
    • A.P. Pugsley Translocation of proteins with signal sequences across membranes Curr. Opin. Cell. Biol. 2 1990 609 616
    • (1990) Curr. Opin. Cell. Biol. , vol.2 , pp. 609-616
    • Pugsley, A.P.1
  • 29
    • 0037448423 scopus 로고    scopus 로고
    • DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus
    • N. Ray, J. Oates, R.J. Turner, and C. Robinson DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus FEBS Lett. 534 2003 156 160
    • (2003) FEBS Lett. , vol.534 , pp. 156-160
    • Ray, N.1    Oates, J.2    Turner, R.J.3    Robinson, C.4
  • 30
    • 8844280791 scopus 로고    scopus 로고
    • Tat-dependent protein targeting in prokaryotes and chloroplasts
    • C. Robinson, and A. Bolhuis Tat-dependent protein targeting in prokaryotes and chloroplasts Biochim. Biophys. Acta 1694 2004 135 147
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 135-147
    • Robinson, C.1    Bolhuis, A.2
  • 31
    • 0035896573 scopus 로고    scopus 로고
    • Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock
    • C.L. Santini, A. Bernadac, M. Zhang, A. Chanal, B. Ize, C. Blanco, and L.F. Wu Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock J. Biol. Chem. 276 2001 8159 8164
    • (2001) J. Biol. Chem. , vol.276 , pp. 8159-8164
    • Santini, C.L.1    Bernadac, A.2    Zhang, M.3    Chanal, A.4    Ize, B.5    Blanco, C.6    Wu, L.F.7
  • 32
    • 0032472381 scopus 로고    scopus 로고
    • A novel sec-independent periplasmic protein translocation pathway in Escherichia coli
    • C.L. Santini, B. Ize, A. Chanal, M. Muller, G. Giordano, and L.F. Wu A novel sec-independent periplasmic protein translocation pathway in Escherichia coli EMBO J. 17 1998 101 112
    • (1998) EMBO J. , vol.17 , pp. 101-112
    • Santini, C.L.1    Ize, B.2    Chanal, A.3    Muller, M.4    Giordano, G.5    Wu, L.F.6
  • 33
    • 0036311769 scopus 로고    scopus 로고
    • Assembly of membrane-bound respiratory complexes by the Tat protein-transport system
    • F. Sargent, B.C. Berks, and T. Palmer Assembly of membrane-bound respiratory complexes by the Tat protein-transport system Arch. Microbiol. 178 2002 77 84
    • (2002) Arch. Microbiol. , vol.178 , pp. 77-84
    • Sargent, F.1    Berks, B.C.2    Palmer, T.3
  • 35
    • 0013564318 scopus 로고
    • Cellular location affects protein stability in Escherichia coli
    • K. Talmadge, and W. Gilbert 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
  • 36
    • 0035181362 scopus 로고    scopus 로고
    • Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli
    • J.D. Thomas, R.A. Daniel, J. Errington, and C. Robinson Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli Mol. Microbiol. 39 2001 47 53
    • (2001) Mol. Microbiol. , vol.39 , pp. 47-53
    • Thomas, J.D.1    Daniel, R.A.2    Errington, J.3    Robinson, C.4
  • 37
    • 0037143790 scopus 로고    scopus 로고
    • Anchorage of cyclodextrin glucanotransferase on the outer membrane of Escherichia coli
    • H.M. Wan, B.Y. Chang, and S.C. Lin Anchorage of cyclodextrin glucanotransferase on the outer membrane of Escherichia coli Biotechnol. Bioeng. 79 2002 457 464
    • (2002) Biotechnol. Bioeng. , vol.79 , pp. 457-464
    • Wan, H.M.1    Chang, B.Y.2    Lin, S.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.