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Volumn 75, Issue 1, 2010, Pages 13-28

In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; PERIPLASMIC PROTEIN; PROTEIN TRXP; THIOREDOXIN; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

EID: 72949101778     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06952.x     Document Type: Article
Times cited : (38)

References (80)
  • 2
    • 0028835464 scopus 로고
    • A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli
    • Alksne, L.E., Keeney, D. Rasmussen, B.A. (1995) A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli. J Bacteriol 177 : 462 464.
    • (1995) J Bacteriol , vol.177 , pp. 462-464
    • Alksne, L.E.1    Keeney, D.2    Rasmussen, B.A.3
  • 3
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld, D.S. (2001) Zinc coordination sphere in biochemical zinc sites. Biometals 14 : 271 313.
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 4
    • 0035794534 scopus 로고    scopus 로고
    • Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA
    • Bader, M.W., Hiniker, A., Regeimbal, J., Goldstone, D., Haebel, P.W., Riemer, J., et al. (2001) Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. EMBO J 20 : 1555 1562.
    • (2001) EMBO J , vol.20 , pp. 1555-1562
    • Bader, M.W.1    Hiniker, A.2    Regeimbal, J.3    Goldstone, D.4    Haebel, P.W.5    Riemer, J.6
  • 5
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C., McGovern, K. Beckwith, J. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67 : 581 589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 7
    • 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. (2005) The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. J Biol Chem 280 : 11387 11394.
    • (2005) J Biol Chem , vol.280 , pp. 11387-11394
    • Berkmen, M.1    Boyd, D.2    Beckwith, J.3
  • 8
    • 72949102433 scopus 로고    scopus 로고
    • Disulfide bond formation in the periplasm
    • In. Ehrmann, M. (ed.). Washington, DC. American Society for Microbiology Press. pp.
    • Berkmen, M., Boyd, D. Beckwith J. (2006) Disulfide bond formation in the periplasm. In The Periplasm. Ehrmann, M. (ed.). Washington, DC : American Society for Microbiology Press, pp. 122 140.
    • (2006) The Periplasm. , pp. 122-140
    • Berkmen, M.1    Boyd, D.2    Beckwith, J.3
  • 9
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • Bessette, P.H., Cotto, J.J., Gilbert, H.F. Georgiou, G. (1999) In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J Biol Chem 274 : 7784 7792.
    • (1999) J Biol Chem , vol.274 , pp. 7784-7792
    • Bessette, P.H.1    Cotto, J.J.2    Gilbert, H.F.3    Georgiou, G.4
  • 11
    • 2942570076 scopus 로고    scopus 로고
    • A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region
    • Buddelmeijer, N. Beckwith, J. (2004) A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region. Mol Microbiol 52 : 1315 1327.
    • (2004) Mol Microbiol , vol.52 , pp. 1315-1327
    • Buddelmeijer, N.1    Beckwith, J.2
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50 : 760 763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 14
    • 0037178798 scopus 로고    scopus 로고
    • Reconstitution of a disulfide isomerization system
    • Collet, J.F., Riemer, J., Bader, M.W. Bardwell, J.C. (2002) Reconstitution of a disulfide isomerization system. J Biol Chem 277 : 26886 26892.
    • (2002) J Biol Chem , vol.277 , pp. 26886-26892
    • Collet, J.F.1    Riemer, J.2    Bader, M.W.3    Bardwell, J.C.4
  • 15
    • 0032548471 scopus 로고    scopus 로고
    • Contributions of substrate binding to the catalytic activity of DsbC
    • Darby, N.J., Raina, S. Creighton, T.E. (1998) Contributions of substrate binding to the catalytic activity of DsbC. Biochemistry 37 : 783 791.
    • (1998) Biochemistry , vol.37 , pp. 783-791
    • Darby, N.J.1    Raina, S.2    Creighton, T.E.3
  • 16
    • 0032167852 scopus 로고    scopus 로고
    • The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm
    • Debarbieux, L. Beckwith, J. (1998) The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm. Proc Natl Acad Sci USA 95 : 10751 10756.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10751-10756
    • Debarbieux, L.1    Beckwith, J.2
  • 17
    • 32344441879 scopus 로고    scopus 로고
    • Disulfide formation and stability of a cysteine-rich repeat protein from Helicobacter pylori
    • Devi, V.S., Sprecher, C.B., Hunziker, P., Mittl, P.R., Bosshard, H.R. Jelesarov, I. (2006) Disulfide formation and stability of a cysteine-rich repeat protein from Helicobacter pylori. Biochemistry 45 : 1599 1607.
    • (2006) Biochemistry , vol.45 , pp. 1599-1607
    • Devi, V.S.1    Sprecher, C.B.2    Hunziker, P.3    Mittl, P.R.4    Bosshard, H.R.5    Jelesarov, I.6
  • 18
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • Dutton, R.J., Boyd, D., Berkmen, M. Beckwith, J. (2008) Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc Natl Acad Sci USA 105 : 11933 11938.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2    Berkmen, M.3    Beckwith, J.4
  • 19
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60 : 2126 2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 20
    • 60849121135 scopus 로고    scopus 로고
    • Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm
    • Eser, M., Masip, L., Kadokura, H., Georgiou, G. Beckwith, J. (2009) Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm. Proc Natl Acad Sci USA 106 : 1572 1577.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1572-1577
    • Eser, M.1    Masip, L.2    Kadokura, H.3    Georgiou, G.4    Beckwith, J.5
  • 21
    • 0004245772 scopus 로고
    • Mechanisms of protein folding
    • In. Pain, R.H. (ed.). Oxford. Oxford University Press. pp.
    • Gilbert, H.F. (1994) Mechanisms of protein folding. In Overview of Protein Folding. Pain, R.H. (ed.). Oxford : Oxford University Press, pp. 104 135.
    • (1994) Overview of Protein Folding. , pp. 104-135
    • Gilbert, H.F.1
  • 22
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • Gilbert, H.F. (1995) Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol 251 : 8 28.
    • (1995) Methods Enzymol , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 23
    • 41449093101 scopus 로고    scopus 로고
    • Disulfide bond isomerization in prokaryotes
    • Gleiter, S. Bardwell, J.C. (2008) Disulfide bond isomerization in prokaryotes. Biochim Biophys Acta 1783 : 530 534.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 530-534
    • Gleiter, S.1    Bardwell, J.C.2
  • 24
    • 33745195461 scopus 로고    scopus 로고
    • Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly
    • Goehring, N.W., Gonzalez, M.D. Beckwith, J. (2006) Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly. Mol Microbiol 61 : 33 45.
    • (2006) Mol Microbiol , vol.61 , pp. 33-45
    • Goehring, N.W.1    Gonzalez, M.D.2    Beckwith, J.3
  • 25
    • 0020652683 scopus 로고
    • Isolation of iron-containing superoxide dismutase from Bacteroides fragilis: Reconstitution as a Mn-containing enzyme
    • Gregory, E.M. Dapper, C.H. (1983) Isolation of iron-containing superoxide dismutase from Bacteroides fragilis: reconstitution as a Mn-containing enzyme. Arch Biochem Biophys 220 : 293 300.
    • (1983) Arch Biochem Biophys , vol.220 , pp. 293-300
    • Gregory, E.M.1    Dapper, C.H.2
  • 26
    • 0028971218 scopus 로고
    • Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
    • Guilhot, C., Jander, G., Martin, N.L. Beckwith, J. (1995) Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc Natl Acad Sci USA 92 : 9895 9899.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9895-9899
    • Guilhot, C.1    Jander, G.2    Martin, N.L.3    Beckwith, J.4
  • 27
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J. Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177 : 4121 4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 28
    • 0035782685 scopus 로고    scopus 로고
    • Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the alpha domain of the electron transporter DsbD
    • Haebel, P.W., Wichman, S., Goldstone, D. Metcalf, P. (2001) Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the alpha domain of the electron transporter DsbD. J Struct Biol 136 : 162 166.
    • (2001) J Struct Biol , vol.136 , pp. 162-166
    • Haebel, P.W.1    Wichman, S.2    Goldstone, D.3    Metcalf, P.4
  • 29
    • 0037119945 scopus 로고    scopus 로고
    • The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDalpha complex
    • Haebel, P.W., Goldstone, D., Katzen, F., Beckwith, J. Metcalf, P. (2002) The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex. EMBO J 21 : 4774 4784.
    • (2002) EMBO J , vol.21 , pp. 4774-4784
    • Haebel, P.W.1    Goldstone, D.2    Katzen, F.3    Beckwith, J.4    Metcalf, P.5
  • 30
    • 32944467057 scopus 로고    scopus 로고
    • Post-crystallization treatments for improving diffraction quality of protein crystals
    • Heras, B. Martin, J.L. (2005) Post-crystallization treatments for improving diffraction quality of protein crystals. Acta Crystallogr D Biol Crystallogr 61 : 1173 1180.
    • (2005) Acta Crystallogr D Biol Crystallogr , vol.61 , pp. 1173-1180
    • Heras, B.1    Martin, J.L.2
  • 32
    • 0021152329 scopus 로고
    • Formation and isomerization of disulfide bonds in proteins: Protein disulfide-isomerase
    • Hillson, D.A., Lambert, N. Freedman, R.B. (1984) Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase. Methods Enzymol 107 : 281 294.
    • (1984) Methods Enzymol , vol.107 , pp. 281-294
    • Hillson, D.A.1    Lambert, N.2    Freedman, R.B.3
  • 33
    • 1842477219 scopus 로고    scopus 로고
    • In vivo substrate specificity of periplasmic disulfide oxidoreductases
    • Hiniker, A. Bardwell, J.C. (2004) In vivo substrate specificity of periplasmic disulfide oxidoreductases. J Biol Chem 279 : 12967 12973.
    • (2004) J Biol Chem , vol.279 , pp. 12967-12973
    • Hiniker, A.1    Bardwell, J.C.2
  • 34
    • 26644437700 scopus 로고    scopus 로고
    • Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC
    • Hiniker, A., Collet, J.F. Bardwell, J.C. (2005) Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J Biol Chem 280 : 33785 33791.
    • (2005) J Biol Chem , vol.280 , pp. 33785-33791
    • Hiniker, A.1    Collet, J.F.2    Bardwell, J.C.3
  • 35
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren, A. (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254 : 9627 9632.
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 36
    • 41449118757 scopus 로고    scopus 로고
    • Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine
    • Inaba, K. Ito, K. (2008) Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine. Biochim Biophys Acta 1783 : 520 529.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 520-529
    • Inaba, K.1    Ito, K.2
  • 37
    • 33750813327 scopus 로고    scopus 로고
    • Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    • Inaba, K., Murakami, S., Suzuki, M., Nakagawa, A., Yamashita, E., Okada, K. Ito, K. (2006) Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell 127 : 789 801.
    • (2006) Cell , vol.127 , pp. 789-801
    • Inaba, K.1    Murakami, S.2    Suzuki, M.3    Nakagawa, A.4    Yamashita, E.5    Okada, K.6    Ito, K.7
  • 38
    • 0028154918 scopus 로고
    • Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation
    • Jander, G., Martin, N.L. Beckwith, J. (1994) Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. EMBO J 13 : 5121 5127.
    • (1994) EMBO J , vol.13 , pp. 5121-5127
    • Jander, G.1    Martin, N.L.2    Beckwith, J.3
  • 39
    • 64549161166 scopus 로고    scopus 로고
    • Kinetic and thermodynamic aspects of cellular thiol-disulfide redox regulation
    • Jensen, K.S., Hansen, R.E. Winther, J.R. (2008) Kinetic and thermodynamic aspects of cellular thiol-disulfide redox regulation. Antioxid Redox Signal 11 : 1047 1058.
    • (2008) Antioxid Redox Signal , vol.11 , pp. 1047-1058
    • Jensen, K.S.1    Hansen, R.E.2    Winther, J.R.3
  • 40
    • 0030787850 scopus 로고    scopus 로고
    • In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC
    • Joly, J.C. Swartz, J.R. (1997) In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. Biochemistry 36 : 10067 10072.
    • (1997) Biochemistry , vol.36 , pp. 10067-10072
    • Joly, J.C.1    Swartz, J.R.2
  • 41
    • 0042011224 scopus 로고    scopus 로고
    • Matthews coefficient probabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals
    • Kantardjieff, K.A. Rupp, B. (2003) Matthews coefficient probabilities: improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals. Protein Sci 12 : 1865 1871.
    • (2003) Protein Sci , vol.12 , pp. 1865-1871
    • Kantardjieff, K.A.1    Rupp, B.2
  • 42
    • 0028948780 scopus 로고
    • Redox states of DsbA in the periplasm of Escherichia coli
    • Kishigami, S., Akiyama, Y. Ito, K. (1995) Redox states of DsbA in the periplasm of Escherichia coli. FEBS Lett 364 : 55 58.
    • (1995) FEBS Lett , vol.364 , pp. 55-58
    • Kishigami, S.1    Akiyama, Y.2    Ito, K.3
  • 43
    • 38149027753 scopus 로고    scopus 로고
    • Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase
    • Mac, T.T., von Hacht, A., Hung, K.C., Dutton, R.J., Boyd, D., Bardwell, J.C. Ulmer, T.S. (2008) Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase. J Biol Chem 283 : 824 832.
    • (2008) J Biol Chem , vol.283 , pp. 824-832
    • Mac, T.T.1    Von Hacht, A.2    Hung, K.C.3    Dutton, R.J.4    Boyd, D.5    Bardwell, J.C.6    Ulmer, T.S.7
  • 44
  • 45
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A.J. (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D Biol Crystallogr 63 : 32 41.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 46
    • 33947364844 scopus 로고    scopus 로고
    • Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli
    • Macomber, L., Rensing, C. Imlay, J.A. (2007) Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli. J Bacteriol 189 : 1616 1626.
    • (2007) J Bacteriol , vol.189 , pp. 1616-1626
    • MacOmber, L.1    Rensing, C.2    Imlay, J.A.3
  • 47
    • 0036849859 scopus 로고    scopus 로고
    • Blu-Ice and the distributed control system: Software for data acquisition and instrument control at macromolecular crystallography beamlines
    • McPhillips, T.M., McPhillips, S.E., Chiu, H.J., Cohen, A.E., Deacon, A.M., Ellis, P.J., et al. (2002) Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines. J Synchrotron Radiat 9 : 401 406.
    • (2002) J Synchrotron Radiat , vol.9 , pp. 401-406
    • McPhillips, T.M.1    McPhillips, S.E.2    Chiu, H.J.3    Cohen, A.E.4    Deacon, A.M.5    Ellis, P.J.6
  • 49
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin, J.L. (1995) Thioredoxin - a fold for all reasons. Structure 3 : 245 250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 50
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation in vivo
    • Martin, J.L., Bardwell, J.C. Kuriyan, J. (1993) Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature 365 : 464 468.
    • (1993) Nature , vol.365 , pp. 464-468
    • Martin, J.L.1    Bardwell, J.C.2    Kuriyan, J.3
  • 51
    • 38149044281 scopus 로고    scopus 로고
    • Laboratory evolution of escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant
    • Masip, L., Klein-Marcuschamer, D., Quan, S., Bardwell, J.C. Georgiou, G. (2008) Laboratory Evolution of Escherichia coli Thioredoxin for Enhanced Catalysis of Protein Oxidation in the Periplasm Reveals a Phylogenetically Conserved Substrate Specificity Determinant. J Biol Chem 283 : 840 848.
    • (2008) J Biol Chem , vol.283 , pp. 840-848
    • Masip, L.1    Klein-Marcuschamer, D.2    Quan, S.3    Bardwell, J.C.4    Georgiou, G.5
  • 52
    • 0037229810 scopus 로고    scopus 로고
    • DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo
    • Maskos, K., Huber-Wunderlich, M. Glockshuber, R. (2003) DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo. J Mol Biol 325 : 495 513.
    • (2003) J Mol Biol , vol.325 , pp. 495-513
    • Maskos, K.1    Huber-Wunderlich, M.2    Glockshuber, R.3
  • 53
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968) Solvent content of protein crystals. J Mol Biol 33 : 491 497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 55
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas, D., Georgopoulos, C. Raina, S. (1994) The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J 13 : 2013 2020.
    • (1994) EMBO J , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 56
    • 4344594427 scopus 로고    scopus 로고
    • Coupling of the pathway of sulphur oxidation to dioxygen reduction: Characterization of a novel membrane-bound thiosulphate: Quinone oxidoreductase
    • Muller, F.H., Bandeiras, T.M., Urich, T., Teixeira, M., Gomes, C.M. Kletzin, A. (2004) Coupling of the pathway of sulphur oxidation to dioxygen reduction: characterization of a novel membrane-bound thiosulphate: quinone oxidoreductase. Mol Microbiol 53 : 1147 1160.
    • (2004) Mol Microbiol , vol.53 , pp. 1147-1160
    • Muller, F.H.1    Bandeiras, T.M.2    Urich, T.3    Teixeira, M.4    Gomes, C.M.5    Kletzin, A.6
  • 57
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol A 276 : 307 326.
    • (1997) Methods Enzymol A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 59
    • 0031039161 scopus 로고    scopus 로고
    • The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization
    • Purschke, W.G., Schmidt, C.L., Petersen, A. Schafer, G. (1997) The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization. J Bacteriol 179 : 1344 1353.
    • (1997) J Bacteriol , vol.179 , pp. 1344-1353
    • Purschke, W.G.1    Schmidt, C.L.2    Petersen, A.3    Schafer, G.4
  • 60
    • 0035311005 scopus 로고    scopus 로고
    • The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly
    • Reid, E., Cole, J. Eaves, D.J. (2001) The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly. Biochem J 355 : 51 58.
    • (2001) Biochem J , vol.355 , pp. 51-58
    • Reid, E.1    Cole, J.2    Eaves, D.J.3
  • 61
    • 65549115487 scopus 로고    scopus 로고
    • Thioredoxins in redox maintenance and survival during oxidative stress of Bacteroides fragilis
    • Reott, M.A., Parker, A.C., Rocha, E.R. Smith, C.J. (2009) Thioredoxins in redox maintenance and survival during oxidative stress of Bacteroides fragilis. J Bacteriol 191 : 3384 3391.
    • (2009) J Bacteriol , vol.191 , pp. 3384-3391
    • Reott, M.A.1    Parker, A.C.2    Rocha, E.R.3    Smith, C.J.4
  • 62
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch, A., Bessette, P., Georgiou, G. Beckwith, J. (1997) Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol 179 : 6602 6608.
    • (1997) J Bacteriol , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 63
    • 0029019571 scopus 로고
    • Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis
    • Rocha, E.R. Smith, C.J. (1995) Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis. J Bacteriol 177 : 3111 3119.
    • (1995) J Bacteriol , vol.177 , pp. 3111-3119
    • Rocha, E.R.1    Smith, C.J.2
  • 64
    • 0029848194 scopus 로고    scopus 로고
    • Oxidative stress response in an anaerobe, Bacteroides fragilis: A role for catalase in protection against hydrogen peroxide
    • Rocha, E.R., Selby, T., Coleman, J.P. Smith, C.J. (1996) Oxidative stress response in an anaerobe, Bacteroides fragilis: a role for catalase in protection against hydrogen peroxide. J Bacteriol 178 : 6895 6903.
    • (1996) J Bacteriol , vol.178 , pp. 6895-6903
    • Rocha, E.R.1    Selby, T.2    Coleman, J.P.3    Smith, C.J.4
  • 66
    • 36649016031 scopus 로고    scopus 로고
    • Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds
    • Rzhepishevska, O.I., Valdes, J., Marcinkeviciene, L., Gallardo, C.A., Meskys, R., Bonnefoy, V., et al. (2007) Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds. Appl Environ Microbiol 73 : 7367 7372.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 7367-7372
    • Rzhepishevska, O.I.1    Valdes, J.2    Marcinkeviciene, L.3    Gallardo, C.A.4    Meskys, R.5    Bonnefoy, V.6
  • 68
    • 0035458303 scopus 로고    scopus 로고
    • Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins
    • Schaffner, J., Winter, J., Rudolph, R. Schwarz, E. (2001) Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins. Appl Environ Microbiol 67 : 3994 4000.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3994-4000
    • Schaffner, J.1    Winter, J.2    Rudolph, R.3    Schwarz, E.4
  • 69
    • 0141727632 scopus 로고    scopus 로고
    • The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway
    • Schierle, C.F., Berkmen, M., Huber, D., Kumamoto, C., Boyd, D. Beckwith, J. (2003) The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. J Bacteriol 185 : 5706 5713.
    • (2003) J Bacteriol , vol.185 , pp. 5706-5713
    • Schierle, C.F.1    Berkmen, M.2    Huber, D.3    Kumamoto, C.4    Boyd, D.5    Beckwith, J.6
  • 70
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
    • Sedlak, J. Lindsay, R.H. (1968) Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal Biochem 25 : 192 205.
    • (1968) Anal Biochem , vol.25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 71
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • Shevchik, V.E., Condemine, G. Robert-Baudouy, J. (1994) Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J 13 : 2007 2012.
    • (1994) EMBO J , vol.13 , pp. 2007-2012
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3
  • 73
    • 0032589120 scopus 로고    scopus 로고
    • Characterization of the Batl (Bacteroides aerotolerance) operon in Bacteroides fragilis: Isolation of a B. fragilis mutant with reduced aerotolerance and impaired growth in in vivo model systems
    • Tang, Y.P., Dallas, M.M. Malamy, M.H. (1999) Characterization of the Batl (Bacteroides aerotolerance) operon in Bacteroides fragilis: isolation of a B. fragilis mutant with reduced aerotolerance and impaired growth in in vivo model systems. Mol Microbiol 32 : 139 149.
    • (1999) Mol Microbiol , vol.32 , pp. 139-149
    • Tang, Y.P.1    Dallas, M.M.2    Malamy, M.H.3
  • 74
    • 0034712727 scopus 로고    scopus 로고
    • A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery
    • Tian, H., Boyd, D. Beckwith, J. (2000) A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery. Proc Natl Acad Sci USA 97 : 4730 4735.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4730-4735
    • Tian, H.1    Boyd, D.2    Beckwith, J.3
  • 75
    • 0030006212 scopus 로고    scopus 로고
    • Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
    • Todd, M.J., Lorimer, G.H. Thirumalai, D. (1996) Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc Natl Acad Sci USA 93 : 4030 4035.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4030-4035
    • Todd, M.J.1    Lorimer, G.H.2    Thirumalai, D.3
  • 76
    • 0030898705 scopus 로고    scopus 로고
    • Scanning and escape during protein-disulfide isomerase-assisted protein folding
    • Walker, K.W. Gilbert, H.F. (1997) Scanning and escape during protein-disulfide isomerase-assisted protein folding. J Biol Chem 272 : 8845 8848.
    • (1997) J Biol Chem , vol.272 , pp. 8845-8848
    • Walker, K.W.1    Gilbert, H.F.2
  • 77
    • 0030061006 scopus 로고    scopus 로고
    • Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine
    • Walker, K.W., Lyles, M.M. Gilbert, H.F. (1996) Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry 35 : 1972 1980.
    • (1996) Biochemistry , vol.35 , pp. 1972-1980
    • Walker, K.W.1    Lyles, M.M.2    Gilbert, H.F.3
  • 78
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich, M. Glockshuber, R. (1993) Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci 2 : 717 726.
    • (1993) Protein Sci , vol.2 , pp. 717-726
    • Wunderlich, M.1    Glockshuber, R.2
  • 79
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun, A., Missiakas, D., Raina, S. Creighton, T.E. (1995) Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34 : 5075 5089.
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4
  • 80
    • 0242353305 scopus 로고    scopus 로고
    • Dimerization by domain hybridization bestows chaperone and isomerase activities
    • Zhao, Z., Peng, Y., Hao, S.F., Zeng, Z.H. Wang, C.C. (2003) Dimerization by domain hybridization bestows chaperone and isomerase activities. J Biol Chem 278 : 43292 43298.
    • (2003) J Biol Chem , vol.278 , pp. 43292-43298
    • Zhao, Z.1    Peng, Y.2    Hao, S.F.3    Zeng, Z.H.4    Wang, C.C.5


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