메뉴 건너뛰기




Volumn 1844, Issue 8, 2014, Pages 1402-1414

Disulfide bond formation in prokaryotes: History, diversity and design

Author keywords

Disulfide bond formation; DsbA; DsbB; Hyperthermophiles; PDI; VKOR

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; CYTOPLASM PROTEIN; DISULFIDE; DSBA PROTEIN; DSBB PROTEIN; DSBC PROTEIN; DSBD PROTEIN; GLUTATHIONE; PROTEIN; THIOL; THIOL OXIDASE; THIOREDOXIN; THIOSULFATE SULFURTRANSFERASE; UNCLASSIFIED DRUG; VITAMIN K EPOXIDE REDUCTASE;

EID: 84902270478     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.02.014     Document Type: Review
Times cited : (101)

References (155)
  • 1
    • 0000893108 scopus 로고
    • Studies on reduction and re-formation of protein disulfide bonds
    • C. Anfinsen, and E. Haber Studies on reduction and re-formation of protein disulfide bonds J. Biol. Chem. 236 1961 1361 1363
    • (1961) J. Biol. Chem. , vol.236 , pp. 1361-1363
    • Anfinsen, C.1    Haber, E.2
  • 2
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
    • R. Goldberger, C. Epstein, and C. Anfinsen Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver J. Biol. Chem. 238 1963 628 635
    • (1963) J. Biol. Chem. , vol.238 , pp. 628-635
    • Goldberger, R.1    Epstein, C.2    Anfinsen, C.3
  • 3
    • 0142019685 scopus 로고
    • Enzymic reactivation of reduced ribonuclease
    • P. Venetianer, and F. Straub Enzymic reactivation of reduced ribonuclease Biochim. Biophys. Acta 67 1963 166 168
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 166-168
    • Venetianer, P.1    Straub, F.2
  • 4
    • 0000870776 scopus 로고
    • Native disulfide band formation in protein-biosynthesis - Evidence for the role of protein disulfide isomerase
    • R. Freedman Native disulfide band formation in protein-biosynthesis - evidence for the role of protein disulfide isomerase Trends Biochem. Sci. 9 1984 438 441
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 438-441
    • Freedman, R.1
  • 5
    • 0017328226 scopus 로고
    • Protein disulfide bond synthesis: A possible intracellular mechanism
    • D. Ziegler, and L. Poulsen Protein disulfide bond synthesis - possible intracellular mechanism Trends Biochem. Sci. 2 1977 79 81 (Pubitemid 8063568)
    • (1977) Trends in Biochemical Sciences , vol.2 , Issue.4 , pp. 79-81
    • Ziegler, D.M.1    Poulsen, L.L.2
  • 6
    • 0017652974 scopus 로고
    • Microsomal mixed function oxidase dependent renaturation of reduced ribonuclease
    • DOI 10.1016/0003-9861(77)90391-5
    • L. Poulsen, and D. Ziegler Microsomal mixed-function oxidase-dependent renaturation of reduced ribonuclease Arch. Biochem. Biophys. 183 1977 563 570 (Pubitemid 8194573)
    • (1977) Archives of Biochemistry and Biophysics , vol.183 , Issue.2 , pp. 563-570
    • Poulsen, L.L.1    Ziegler, D.M.2
  • 7
    • 0017392539 scopus 로고
    • Stimulation of reduced lysozyme regeneration by transferrin and lactoferrin
    • DOI 10.1016/0003-9861(77)90552-5
    • W. Anderson, and T. Tomasi Stimulation of reduced lysozyme regeneration by transferrin and lactoferrin Arch. Biochem. Biophys. 182 1977 705 711 (Pubitemid 8161080)
    • (1977) Archives of Biochemistry and Biophysics , vol.182 , Issue.2 , pp. 705-711
    • Anderson, W.L.1    Tomasi Jr., T.B.2
  • 9
    • 0020570384 scopus 로고
    • Role of primary structure and disulfide bond formation in beta-lactamase secretion
    • S. Pollitt, and H. Zalkin Role of primary structure and disulfide bond formation in beta-lactamase secretion J. Bacteriol. 153 1983 27 32 (Pubitemid 13119837)
    • (1983) Journal of Bacteriology , vol.153 , Issue.1 , pp. 27-32
    • Pollitt, S.1    Zalkin, H.2
  • 10
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • J.C. Bardwell, K. McGovern, and J. Beckwith Identification of a protein required for disulfide bond formation in vivo Cell 67 1991 581 589 (Pubitemid 121001472)
    • (1991) Cell , vol.67 , Issue.3 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 11
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • DOI 10.1016/0092-8674(93)90469-7
    • M.L. LaMantia, and W.J. Lennarz The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity Cell 74 1993 899 908 (Pubitemid 23270609)
    • (1993) Cell , vol.74 , Issue.5 , pp. 899-908
    • LaMantia, M.1    Lennarz, W.J.2
  • 12
    • 0028953741 scopus 로고
    • Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
    • N.J. Darby, and T.E. Creighton Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase Biochemistry 34 1995 3576 3587
    • (1995) Biochemistry , vol.34 , pp. 3576-3587
    • Darby, N.J.1    Creighton, T.E.2
  • 13
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • A.R. Frand, and C.A. Kaiser The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum Mol. Cell 1 1998 161 170 (Pubitemid 128378657)
    • (1998) Molecular Cell , vol.1 , Issue.2 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 14
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • DOI 10.1016/j.cell.2005.04.011, PII S0092867405003570
    • N. Mesecke, N. Terziyska, C. Kozany, F. Baumann, W. Neupert, K. Hell, and J.M. Herrmann A disulfide relay system in the intermembrane space of mitochondria that mediates protein import Cell 121 2005 1059 1069 (Pubitemid 40884396)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 17
    • 0030671552 scopus 로고    scopus 로고
    • Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
    • T. Kobayashi, S. Kishigami, M. Sone, H. Inokuchi, T. Mogi, and K. Ito Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells Proc. Natl. Acad. Sci. U. S. A. 94 1997 11857 11862
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11857-11862
    • Kobayashi, T.1    Kishigami, S.2    Sone, M.3    Inokuchi, H.4    Mogi, T.5    Ito, K.6
  • 18
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • R.J. Dutton, D. Boyd, M. Berkmen, and J. Beckwith Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation Proc. Natl. Acad. Sci. U. S. A. 105 2008 11933 11938
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2    Berkmen, M.3    Beckwith, J.4
  • 19
    • 71549132149 scopus 로고    scopus 로고
    • Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
    • F. Hatahet, and L.W. Ruddock Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation Antioxid. Redox Signal. 11 2009 2807 2850
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2807-2850
    • Hatahet, F.1    Ruddock, L.W.2
  • 20
    • 0027062943 scopus 로고
    • Environment-specific amino acid substitution tables: Tertiary templates and prediction of protein folds
    • J. Overington, D. Donnelly, M.S. Johnson, A. Sali, and T.L. Blundell Environment-specific amino acid substitution tables: tertiary templates and prediction of protein folds Protein Sci. 1 1992 216 226 (Pubitemid 23007288)
    • (1992) Protein Science , vol.1 , Issue.2 , pp. 216-226
    • Overington, J.1    Donnelly, D.2    Johnson, M.S.3    Sali, A.4    Blundell, T.L.5
  • 21
    • 0141506109 scopus 로고    scopus 로고
    • Disulfide by Design™: A computational method for the rational design of disulfide bonds in proteins
    • DOI 10.1093/bioinformatics/btg231
    • A. Dombkowski Disulfide by Design (TM): a computational method for the rational design of disulfide bonds in proteins Bioinformatics 19 2003 1852 1853 (Pubitemid 37220480)
    • (2003) Bioinformatics , vol.19 , Issue.14 , pp. 1852-1853
    • Dombkowski, A.A.1
  • 22
    • 78649529306 scopus 로고    scopus 로고
    • Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces
    • S.M. Marino, and V.N. Gladyshev Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces J. Mol. Biol. 404 2010 902 916
    • (2010) J. Mol. Biol. , vol.404 , pp. 902-916
    • Marino, S.M.1    Gladyshev, V.N.2
  • 24
    • 24944449074 scopus 로고    scopus 로고
    • The genomics of disulfide bonding and protein stabilization in thermophiles
    • DOI 10.1371/journal.pbio.0030309, e309
    • M. Beeby, B. O'Connor, C. Ryttersgaard, D. Boutz, L. Perry, and T. Yeates The Genomics of disulfide bonding and protein stabilization in thermophiles PLoS Biol. 3 2005 1549 1558 (Pubitemid 41306438)
    • (2005) PLoS Biology , vol.3 , Issue.9 , pp. 1549-1558
    • Beeby, M.1    O'Connor, B.D.2    Ryttersgaard, C.3    Boutz, D.R.4    Perry, L.J.5    Yeates, T.O.6
  • 26
    • 45549122242 scopus 로고    scopus 로고
    • DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli
    • J.P.A. Grimshaw, C.U. Stirnimann, M.S. Brozzo, G. Malojcic, M.G. Gruetter, G. Capitani, and R. Glockshuber DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli J. Mol. Biol. 380 2008 667 680
    • (2008) J. Mol. Biol. , vol.380 , pp. 667-680
    • Grimshaw, J.P.A.1    Stirnimann, C.U.2    Brozzo, M.S.3    Malojcic, G.4    Gruetter, M.G.5    Capitani, G.6    Glockshuber, R.7
  • 27
    • 0023883641 scopus 로고
    • Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli
    • S. Froshauer, G.N. Green, D. Boyd, K. McGovern, and J. Beckwith Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli J. Mol. Biol. 200 1988 501 511
    • (1988) J. Mol. Biol. , vol.200 , pp. 501-511
    • Froshauer, S.1    Green, G.N.2    Boyd, D.3    McGovern, K.4    Beckwith, J.5
  • 28
    • 0032526690 scopus 로고    scopus 로고
    • Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization
    • L.W. Guddat, J.C.A. Bardwell, and J.L. Martin Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization Struct. Fold. Des. 6 1998 757 767 (Pubitemid 28301209)
    • (1998) Structure , vol.6 , Issue.6 , pp. 757-767
    • Guddat, L.W.1    Bardwell, J.C.A.2    Martin, J.L.3
  • 29
    • 0031776171 scopus 로고    scopus 로고
    • A single dipeptide sequence modulates the redox properties of a whole enzyme family
    • DOI 10.1016/S1359-0278(98)00024-8
    • M. Huber-Wunderlich, and R. Glockshuber A single dipeptide sequence modulates the redox properties of a whole enzyme family Fold. Des. 3 1998 161 171 (Pubitemid 28264393)
    • (1998) Folding and Design , vol.3 , Issue.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 30
    • 70149110001 scopus 로고    scopus 로고
    • Detecting folding intermediates of a protein as it passes through the bacterial translocation channel
    • H. Kadokura, and J. Beckwith Detecting folding intermediates of a protein as it passes through the bacterial translocation channel Cell 138 2009 1164 1173
    • (2009) Cell , vol.138 , pp. 1164-1173
    • Kadokura, H.1    Beckwith, J.2
  • 33
    • 33750813327 scopus 로고    scopus 로고
    • Crystal Structure of the DsbB-DsbA Complex Reveals a Mechanism of Disulfide Bond Generation
    • DOI 10.1016/j.cell.2006.10.034, PII S0092867406014127
    • K. Inaba, S. Murakami, M. Suzuki, A. Nakagawa, E. Yamashita, K. Okada, and K. Ito Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation Cell 127 2006 789 801 (Pubitemid 44716258)
    • (2006) Cell , vol.127 , Issue.4 , pp. 789-801
    • Inaba, K.1    Murakami, S.2    Suzuki, M.3    Nakagawa, A.4    Yamashita, E.5    Okada, K.6    Ito, K.7
  • 34
    • 0037093512 scopus 로고    scopus 로고
    • Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA
    • DOI 10.1093/emboj/21.10.2354
    • H. Kadokura, and J. Beckwith Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA EMBO J. 21 2002 2354 2363 (Pubitemid 34546708)
    • (2002) EMBO Journal , vol.21 , Issue.10 , pp. 2354-2363
    • Kadokura, H.1    Beckwith, J.2
  • 35
    • 0037031882 scopus 로고    scopus 로고
    • DsbB catalyzes disulfide bond formation de novo
    • DOI 10.1074/jbc.M205433200
    • J. Regeimbal, and J.C. Bardwell DsbB catalyzes disulfide bond formation de novo J. Biol. Chem. 277 2002 32706 32713 (Pubitemid 34984777)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 32706-32713
    • Regeimbal, J.1    Bardwell, J.C.A.2
  • 36
    • 62649151322 scopus 로고    scopus 로고
    • Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB
    • K. Inaba, S. Murakami, A. Nakagawa, H. Iida, M. Kinjo, K. Ito, and M. Suzuki Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB EMBO J. 28 2009 779 791
    • (2009) EMBO J. , vol.28 , pp. 779-791
    • Inaba, K.1    Murakami, S.2    Nakagawa, A.3    Iida, H.4    Kinjo, M.5    Ito, K.6    Suzuki, M.7
  • 37
    • 0033106153 scopus 로고    scopus 로고
    • Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
    • T. Kobayashi, and K. Ito Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway EMBO J. 18 1999 1192 1198 (Pubitemid 29110304)
    • (1999) EMBO Journal , vol.18 , Issue.5 , pp. 1192-1198
    • Kobayashi, T.1    Ito, K.2
  • 38
    • 0028971218 scopus 로고
    • Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
    • C. Guilhot, G. Jander, N.L. Martin, and J. Beckwith Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA Proc. Natl. Acad. Sci. U. S. A. 92 1995 9895 9899
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9895-9899
    • Guilhot, C.1    Jander, G.2    Martin, N.L.3    Beckwith, J.4
  • 39
    • 0029161150 scopus 로고
    • DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
    • S. Kishigami, E. Kanaya, M. Kikuchi, and K. Ito DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA J. Biol. Chem. 270 1995 17072 17074
    • (1995) J. Biol. Chem. , vol.270 , pp. 17072-17074
    • Kishigami, S.1    Kanaya, E.2    Kikuchi, M.3    Ito, K.4
  • 40
    • 1342304093 scopus 로고    scopus 로고
    • DsbB Elicits a Red-shift of Bound Ubiquinone during the Catalysis of DsbA Oxidation
    • DOI 10.1074/jbc.M310765200
    • K. Inaba, Y.H. Takahashi, N. Fujieda, K. Kano, H. Miyoshi, and K. Ito DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation J. Biol. Chem. 279 2004 6761 6768 (Pubitemid 38248817)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6761-6768
    • Inaba, K.1    Takahashi, Y.-H.2    Ito, K.3
  • 42
    • 54549124476 scopus 로고    scopus 로고
    • Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
    • G. Malojcic, R.L. Owen, J.P.A. Grimshaw, and R. Glockshuber Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB FEBS Lett. 582 2008 3301 3307
    • (2008) FEBS Lett. , vol.582 , pp. 3301-3307
    • Malojcic, G.1    Owen, R.L.2    Grimshaw, J.P.A.3    Glockshuber, R.4
  • 43
    • 0034718489 scopus 로고    scopus 로고
    • Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli
    • H. Kadokura, M. Bader, H. Tian, J.C. Bardwell, and J. Beckwith Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 97 2000 10884 10889
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10884-10889
    • Kadokura, H.1    Bader, M.2    Tian, H.3    Bardwell, J.C.4    Beckwith, J.5
  • 44
    • 3242786500 scopus 로고    scopus 로고
    • Vitamin K epoxide reductase: Homology, active site and catalytic mechanism
    • DOI 10.1016/j.tibs.2004.04.004, PII S0968000404000829
    • L. Goodstadt, and C.P. Ponting Vitamin K epoxide reductase: homology, active site and catalytic mechanism Trends Biochem. Sci. 29 2004 289 292 (Pubitemid 38968759)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.6 , pp. 289-292
    • Goodstadt, L.1    Ponting, C.P.2
  • 45
    • 40949088051 scopus 로고    scopus 로고
    • VKORC1 and the vitamin K cycle
    • A.A. Garcia, and P.H. Reitsma VKORC1 and the vitamin K cycle Vitam. Horm. 78 2008 23 33
    • (2008) Vitam. Horm. , vol.78 , pp. 23-33
    • Garcia, A.A.1    Reitsma, P.H.2
  • 47
    • 1142274548 scopus 로고    scopus 로고
    • Identification of the gene for vitamin K epoxide reductase
    • DOI 10.1038/nature02254
    • T. Li, C.Y. Chang, D.Y. Jin, P.J. Lin, A. Khvorova, and D.W. Stafford Identification of the gene for vitamin K epoxide reductase Nature 427 2004 541 544 (Pubitemid 38209111)
    • (2004) Nature , vol.427 , Issue.6974 , pp. 541-544
    • Li, T.1    Chang, C.-Y.2    Jin, D.-Y.3    Lin, P.-J.4    Khvorova, A.5    Stafford, D.W.6
  • 48
    • 77957007036 scopus 로고    scopus 로고
    • Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners
    • S. Schulman, B. Wang, W. Li, and T.A. Rapoport Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners Proc. Natl. Acad. Sci. U. S. A. 107 2010 15027 15032
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 15027-15032
    • Schulman, S.1    Wang, B.2    Li, W.3    Rapoport, T.A.4
  • 49
    • 79952821270 scopus 로고    scopus 로고
    • Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase
    • X. Wang, R.J. Dutton, J. Beckwith, and D. Boyd Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase Antioxid. Redox Signal. 14 2011 1413 1420
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1413-1420
    • Wang, X.1    Dutton, R.J.2    Beckwith, J.3    Boyd, D.4
  • 50
    • 79953218059 scopus 로고    scopus 로고
    • Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): Electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation
    • M.A. Rishavy, A. Usubalieva, K.W. Hallgren, and K.L. Berkner Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation J. Biol. Chem. 286 2011 7267 7278
    • (2011) J. Biol. Chem. , vol.286 , pp. 7267-7278
    • Rishavy, M.A.1    Usubalieva, A.2    Hallgren, K.W.3    Berkner, K.L.4
  • 51
    • 47049096139 scopus 로고    scopus 로고
    • Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms
    • A.K. Singh, M. Bhattacharyya-Pakrasi, and H.B. Pakrasi Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms J. Biol. Chem. 283 2008 15762 15770
    • (2008) J. Biol. Chem. , vol.283 , pp. 15762-15770
    • Singh, A.K.1    Bhattacharyya-Pakrasi, M.2    Pakrasi, H.B.3
  • 52
    • 23944489821 scopus 로고    scopus 로고
    • The vitamin K-dependent carboxylase
    • DOI 10.1146/annurev.nutr.25.050304.092713
    • K. Berkner The vitamin K-dependent carboxylase Annu. Rev. Nutr. 25 2005 127 149 (Pubitemid 41208997)
    • (2005) Annual Review of Nutrition , vol.25 , pp. 127-149
    • Berkner, K.L.1
  • 53
    • 84861662334 scopus 로고    scopus 로고
    • Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum
    • L.A. Rutkevich, and D.B. Williams Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum Mol. Biol. Cell 23 2012 2017 2027
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2017-2027
    • Rutkevich, L.A.1    Williams, D.B.2
  • 54
    • 18144423143 scopus 로고    scopus 로고
    • Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation
    • DOI 10.1074/jbc.M500765200
    • J.K. Tie, C. Nicchitta, G. von Heijne, and D.W. Stafford Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/ cotranslocation J. Biol. Chem. 280 2005 16410 16416 (Pubitemid 40616771)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16410-16416
    • Tie, J.-K.1    Nicchitta, C.2    Von Heijne, G.3    Stafford, D.W.4
  • 55
    • 84867240359 scopus 로고    scopus 로고
    • Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms
    • J. Tie, D. Jin, and D.W. Stafford Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms J. Biol. Chem. 287 2012 33945 33955
    • (2012) J. Biol. Chem. , vol.287 , pp. 33945-33955
    • Tie, J.1    Jin, D.2    Stafford, D.W.3
  • 56
    • 34250796202 scopus 로고    scopus 로고
    • The conversion of vitamin K epoxide to Vitamin K quinone and vitamin K quinone to vitamin K hydroquinone uses the same active site cysteines
    • DOI 10.1021/bi700527j
    • D.Y. Jin, J.K. Tie, and D.W. Stafford The conversion of vitamin K epoxide to vitamin K quinone and vitamin K quinone to vitamin K hydroquinone uses the same active site cysteines Biochemistry 46 2007 7279 7283 (Pubitemid 46974001)
    • (2007) Biochemistry , vol.46 , Issue.24 , pp. 7279-7283
    • Jin, D.-Y.1    Tie, J.-K.2    Stafford, D.W.3
  • 57
    • 22444432755 scopus 로고    scopus 로고
    • The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases
    • DOI 10.1110/ps.051355705
    • C.S. Sevier, H. Kadokura, V.C. Tam, J. Beckwith, D. Fass, and C.A. Kaiser The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases Protein Sci. 14 2005 1630 1642 (Pubitemid 41007924)
    • (2005) Protein Science , vol.14 , Issue.6 , pp. 1630-1642
    • Sevier, C.S.1    Kadokura, H.2    Tam, V.C.3    Beckwith, J.4    Fass, D.5    Kaiser, C.A.6
  • 58
    • 84855415686 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells
    • J.K. Tie, D.Y. Jin, and D.W. Stafford Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells Antioxid. Redox Signal. 16 2012 329 338
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 329-338
    • Tie, J.K.1    Jin, D.Y.2    Stafford, D.W.3
  • 59
    • 0030787850 scopus 로고    scopus 로고
    • In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC
    • DOI 10.1021/bi9707739
    • J.C. Joly, and J.R. Swartz In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC Biochemistry (N. Y) 36 1997 10067 10072 (Pubitemid 27357714)
    • (1997) Biochemistry , vol.36 , Issue.33 , pp. 10067-10072
    • Joly, J.C.1    Swartz, J.R.2
  • 60
    • 15744375548 scopus 로고    scopus 로고
    • The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC
    • DOI 10.1074/jbc.M411774200
    • M. Berkmen, D. Boyd, and J. Beckwith The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC J. Biol. Chem. 280 2005 11387 11394 (Pubitemid 40418447)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11387-11394
    • Berkmen, M.1    Boyd, D.2    Beckwith, J.3
  • 61
    • 0034048647 scopus 로고    scopus 로고
    • Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
    • DOI 10.1038/73295
    • A.A. McCarthy, P.W. Haebel, A. Torronen, V. Rybin, E.N. Baker, and P. Metcalf Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli Nat. Struct. Biol. 7 2000 196 199 (Pubitemid 30140763)
    • (2000) Nature Structural Biology , vol.7 , Issue.3 , pp. 196-199
    • McCarthy, A.A.1    Haebel, P.W.2    Torronen, A.3    Rybin, V.4    Baker, E.N.5    Metcalf, P.6
  • 62
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • A. Zapun, D. Missiakas, S. Raina, and T.E. Creighton Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli Biochemistry 34 1995 5075 5089
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4
  • 63
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • D. Missiakas, C. Georgopoulos, and S. Raina The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation EMBO J. 13 1994 2013 2020 (Pubitemid 24124535)
    • (1994) EMBO Journal , vol.13 , Issue.8 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 65
    • 1842477219 scopus 로고    scopus 로고
    • In vivo substrate specificity of periplasmic disulfide oxidoreductases
    • DOI 10.1074/jbc.M311391200
    • A. Hiniker, and J.C. Bardwell In vivo substrate specificity of periplasmic disulfide oxidoreductases J. Biol. Chem. 279 2004 12967 12973 (Pubitemid 38445872)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12967-12973
    • Hiniker, A.1    Bardwell, J.C.A.2
  • 66
    • 0031736826 scopus 로고    scopus 로고
    • Expression of active human tissue-type plasminogen activator in Escherichia coli
    • J. Qiu, J.R. Swartz, and G. Georgiou Expression of active human tissue-type plasminogen activator in Escherichia coli Appl. Environ. Microbiol. 64 1998 4891 4896 (Pubitemid 28557856)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.12 , pp. 4891-4896
    • Qiu, J.1    Swartz, J.R.2    Georgiou, G.3
  • 68
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • A. Rietsch, P. Bessette, G. Georgiou, and J. Beckwith Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin J. Bacteriol. 179 1997 6602 6608 (Pubitemid 27465291)
    • (1997) Journal of Bacteriology , vol.179 , Issue.21 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 70
    • 0030898705 scopus 로고    scopus 로고
    • Scanning and escape during protein-disulfide isomerase-assisted protein folding
    • DOI 10.1074/jbc.272.14.8845
    • K.W. Walker, and H.F. Gilbert Scanning and escape during protein-disulfide isomerase-assisted protein folding J. Biol. Chem. 272 1997 8845 8848 (Pubitemid 27154874)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 8845-8848
    • Walker, K.W.1    Gilbert, H.F.2
  • 71
    • 0037470064 scopus 로고    scopus 로고
    • Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase
    • DOI 10.1074/jbc.M211036200
    • M. Schwaller, B. Wilkinson, and H.F. Gilbert Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase J. Biol. Chem. 278 2003 7154 7159 (Pubitemid 36800714)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 7154-7159
    • Schwaller, M.1    Wilkinson, B.2    Gilbert, H.F.3
  • 72
    • 0033230589 scopus 로고    scopus 로고
    • Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
    • DOI 10.1093/emboj/18.21.5963
    • E.J. Stewart, F. Katzen, and J. Beckwith Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli EMBO J. 18 1999 5963 5971 (Pubitemid 29515673)
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 73
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • F. Katzen, and J. Beckwith Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade Cell 103 2000 769 779
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 74
    • 84860534459 scopus 로고    scopus 로고
    • A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope
    • 10.1128/mBio.00291-11 (Print 2012)
    • S.H. Cho, D. Parsonage, C. Thurston, R.J. Dutton, L.B. Poole, J.F. Collet, and J. Beckwith A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope MBio 3 2012 10.1128/mBio.00291-11 (Print 2012)
    • (2012) MBio , vol.3
    • Cho, S.H.1    Parsonage, D.2    Thurston, C.3    Dutton, R.J.4    Poole, L.B.5    Collet, J.F.6    Beckwith, J.7
  • 76
    • 0030830073 scopus 로고    scopus 로고
    • A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins
    • C.L. Andersen, A. Matthey-Dupraz, D. Missiakas, and S. Raina A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins Mol. Microbiol. 26 1997 121 132 (Pubitemid 27438243)
    • (1997) Molecular Microbiology , vol.26 , Issue.1 , pp. 121-132
    • Andersen, C.L.1    Matthey-Dupraz, A.2    Missiakas, D.3    Raina, S.4
  • 77
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • P.H. Bessette, J.J. Cotto, H.F. Gilbert, and G. Georgiou In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG J. Biol. Chem. 274 1999 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
  • 79
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • K.G. Reddie, and K.S. Carroll Expanding the functional diversity of proteins through cysteine oxidation Curr. Opin. Chem. Biol. 12 2008 746 754
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 80
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • DOI 10.1128/JB.183.24.7173-7181.2001
    • L.C. Seaver, and J.A. Imlay Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli J. Bacteriol. 183 2001 7173 7181 (Pubitemid 33121851)
    • (2001) Journal of Bacteriology , vol.183 , Issue.24 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 81
    • 84858279884 scopus 로고    scopus 로고
    • Overview of peroxiredoxins in oxidant defense and redox regulation
    • (Chapter 7, Unit7.9)
    • L.B. Poole, A. Hall, and K.J. Nelson Overview of peroxiredoxins in oxidant defense and redox regulation Curr. Protoc. Toxicol. 49 2011 7.9.1 7.9.15 (Chapter 7, Unit7.9)
    • (2011) Curr. Protoc. Toxicol. , vol.49 , pp. 791-7915
    • Poole, L.B.1    Hall, A.2    Nelson, K.J.3
  • 82
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • H.Z. Chae, S.J. Chung, and S.G. Rhee Thioredoxin-dependent peroxide reductase from yeast J. Biol. Chem. 269 1994 27670 27678 (Pubitemid 24346604)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.44 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 83
    • 84857602613 scopus 로고    scopus 로고
    • Peroxides and peroxidases in the endoplasmic reticulum: Integrating redox homeostasis and oxidative folding
    • T. Kakihana, K. Nagata, and R. Sitia Peroxides and peroxidases in the endoplasmic reticulum: integrating redox homeostasis and oxidative folding Antioxid. Redox Signal. 16 2012 763 771
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 763-771
    • Kakihana, T.1    Nagata, K.2    Sitia, R.3
  • 84
    • 78649918283 scopus 로고    scopus 로고
    • Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
    • E. Zito, E.P. Melo, Y. Yang, A. Wahlander, T.A. Neubert, and D. Ron Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin Mol. Cell 40 2010 787 797
    • (2010) Mol. Cell , vol.40 , pp. 787-797
    • Zito, E.1    Melo, E.P.2    Yang, Y.3    Wahlander, A.4    Neubert, T.A.5    Ron, D.6
  • 85
    • 57649138449 scopus 로고    scopus 로고
    • De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC
    • S. Arredondo, L. Segatori, H.F. Gilbert, and G. Georgiou De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC J. Biol. Chem. 283 2008 31469 31476
    • (2008) J. Biol. Chem. , vol.283 , pp. 31469-31476
    • Arredondo, S.1    Segatori, L.2    Gilbert, H.F.3    Georgiou, G.4
  • 87
    • 33646205345 scopus 로고    scopus 로고
    • Conserved role of the linker α-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB
    • DOI 10.1074/jbc.M505453200
    • L. Segatori, L. Murphy, S. Arredondo, H. Kadokura, H. Gilbert, J. Beckwith, and G. Georgiou Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB J. Biol. Chem. 281 2006 4911 4919 (Pubitemid 43847753)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 4911-4919
    • Segatori, L.1    Murphy, L.2    Arredondo, S.3    Kadokura, H.4    Gilbert, H.5    Beckwith, J.6    Georgiou, G.7
  • 88
    • 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
    • P.W. Haebel, D. Goldstone, F. Katzen, J. Beckwith, and P. Metcalf The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex EMBO J. 21 2002 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
  • 92
    • 77952311188 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
    • A. Holmgren, and J. Lu Thioredoxin and thioredoxin reductase: current research with special reference to human disease Biochem. Biophys. Res. Commun. 396 2010 120 124
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 120-124
    • Holmgren, A.1    Lu, J.2
  • 93
    • 0034770083 scopus 로고    scopus 로고
    • Roles of thiol-redox pathways in bacteria
    • DOI 10.1146/annurev.micro.55.1.21
    • D. Ritz, and J. Beckwith Roles of thiol-redox pathways in bacteria Annu. Rev. Microbiol. 55 2001 21 48 (Pubitemid 32978099)
    • (2001) Annual Review of Microbiology , vol.55 , pp. 21-48
    • Ritz, D.1    Beckwith, J.2
  • 94
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • DOI 10.1074/jbc.272.25.15661
    • W.A. Prinz, F. Aslund, A. Holmgren, and J. Beckwith The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm J. Biol. Chem. 272 1997 15661 15667 (Pubitemid 27265536)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 96
    • 0022036755 scopus 로고
    • Examination of calf prochymosin accumulation in Escherichia coli: Disulphide linkages are a structural component of prochymosin-containing inclusion bodies
    • J.M. Schoemaker, A.H. Brasnett, and F.A. Marston Examination of calf prochymosin accumulation in Escherichia coli: disulphide linkages are a structural component of prochymosin-containing inclusion bodies EMBO J. 4 1985 775 780
    • (1985) EMBO J. , vol.4 , pp. 775-780
    • Schoemaker, J.M.1    Brasnett, A.H.2    Marston, F.A.3
  • 98
    • 0037022796 scopus 로고    scopus 로고
    • A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond
    • DOI 10.1021/bi015981m
    • J. Meyer, M.D. Clay, M.K. Johnson, A. Stubna, E. Munck, C. Higgins, and P. Wittung-Stafshede A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond Biochemistry (N. Y.) 41 2002 3096 3108 (Pubitemid 34184641)
    • (2002) Biochemistry , vol.41 , Issue.9 , pp. 3096-3108
    • Meyer, J.1    Clay, M.D.2    Johnson, M.K.3    Stubna, A.4    Munck, E.5    Higgins, C.6    Wittung-Stafshede, P.7
  • 100
    • 0034710899 scopus 로고    scopus 로고
    • A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation
    • T. Senkevich, C. White, E. Koonin, and B. Moss A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation Proc. Natl. Acad. Sci. U. S. A. 97 2000 12068 12073
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12068-12073
    • Senkevich, T.1    White, C.2    Koonin, E.3    Moss, B.4
  • 102
    • 0036140130 scopus 로고    scopus 로고
    • Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly
    • DOI 10.1128/JVI.76.2.467-472.2002
    • C. White, T. Senkevich, and B. Moss Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly J. Virol. 76 2002 467 472 (Pubitemid 34033344)
    • (2002) Journal of Virology , vol.76 , Issue.2 , pp. 467-472
    • White, C.L.1    Senkevich, T.G.2    Moss, B.3
  • 103
    • 68149178656 scopus 로고    scopus 로고
    • Dimer interface migration in a viral sulfhydryl oxidase
    • M. Hakim, and D. Fass Dimer interface migration in a viral sulfhydryl oxidase J. Mol. Biol. 391 2009 758 768
    • (2009) J. Mol. Biol. , vol.391 , pp. 758-768
    • Hakim, M.1    Fass, D.2
  • 104
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • (1-+)
    • C. Vieille, and G.J. Zeikus Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability Microbiol. Mol. Biol. Rev. 65 2001 (1 - +)
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65
    • Vieille, C.1    Zeikus, G.J.2
  • 105
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • DOI 10.1016/S0959-440X(98)80094-8
    • R. Jaenicke, and G. Bohm The stability of proteins in extreme environments Curr. Opin. Struct. Biol. 8 1998 738 748 (Pubitemid 29004672)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.6 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 106
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • A.I. Derman, W.A. Prinz, D. Belin, and J. Beckwith Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli Science 262 1993 1744 1747 (Pubitemid 24030100)
    • (1993) Science , vol.262 , Issue.5140 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 107
    • 78651484550 scopus 로고    scopus 로고
    • Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. Coli
    • F. Hatahet, V.D. Nguyen, K.E.H. Salo, and L.W. Ruddock Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli Microb. Cell Factories 9 2010 67
    • (2010) Microb. Cell Factories , vol.9 , pp. 67
    • Hatahet, F.1    Nguyen, V.D.2    Salo, K.E.H.3    Ruddock, L.W.4
  • 108
    • 84883292418 scopus 로고    scopus 로고
    • Topological plasticity of enzymes involved in disulfide bond formation allows catalysis in either the periplasm or the cytoplasm
    • F. Hatahet, and L.W. Ruddock Topological plasticity of enzymes involved in disulfide bond formation allows catalysis in either the periplasm or the cytoplasm J. Mol. Biol. 425 2013 3268 3276
    • (2013) J. Mol. Biol. , vol.425 , pp. 3268-3276
    • Hatahet, F.1    Ruddock, L.W.2
  • 109
    • 33748331151 scopus 로고    scopus 로고
    • A Novel Member of the Protein Disulfide Oxidoreductase Family from Aeropyrum pernix K1: Structure, Function and Electrostatics
    • DOI 10.1016/j.jmb.2006.07.038, PII S0022283606009077
    • K. D'Ambrosio, E. Pedone, E. Langella, G. De Simone, M. Rossi, C. Pedone, and S. Bartolucci A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: Structure, function and electrostatics J. Mol. Biol. 362 2006 743 752 (Pubitemid 44332421)
    • (2006) Journal of Molecular Biology , vol.362 , Issue.4 , pp. 743-752
    • D'Ambrosio, K.1    Pedone, E.2    Langella, E.3    De Simone, G.4    Rossi, M.5    Pedone, C.6    Bartolucci, S.7
  • 110
    • 0031816805 scopus 로고    scopus 로고
    • A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
    • B. Ren, G. Tibbelin, D. de Pascale, M. Rossi, S. Bartolucci, and R. Ladenstein A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units Nat. Struct. Biol. 5 1998 602 611
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 602-611
    • Ren, B.1    Tibbelin, G.2    De Pascale, D.3    Rossi, M.4    Bartolucci, S.5    Ladenstein, R.6
  • 111
    • 0034989118 scopus 로고    scopus 로고
    • Protein disulfide oxidoreductase from Pyrococcus furiosus: Biochemical properties
    • DOI 10.1016/S0076-6879(01)34459-2
    • S. Bartolucci, D. De Pascale, and M. Rossi Protein disulfide oxidoreductase from Pyrococcus furiosus: biochemical properties Hyperthermophilic Enzymes C 334 2001 62 73 (Pubitemid 32507264)
    • (2001) Methods in Enzymology , vol.334 , pp. 62-73
    • Bartolucci, S.1    De Pascale, D.2    Rossi, M.3
  • 113
    • 0034615794 scopus 로고    scopus 로고
    • The universal ancestor lived in a thermophilic or hyperthermophilic environment
    • M. Di Giulio The universal ancestor lived in a thermophilic or hyperthermophilic environment J. Theor. Biol. 203 2000 203 213
    • (2000) J. Theor. Biol. , vol.203 , pp. 203-213
    • Di Giulio, M.1
  • 114
    • 0037424668 scopus 로고    scopus 로고
    • The universal ancestor was a thermophile or a hyperthermophile: Tests and further evidence
    • DOI 10.1006/jtbi.2003.3197
    • M. Di Giulio The universal ancestor was a thermophile or a hyperthermophile: Tests and further evidence J. Theor. Biol. 221 2003 425 436 (Pubitemid 36299264)
    • (2003) Journal of Theoretical Biology , vol.221 , Issue.3 , pp. 425-436
    • Di Giulio, M.1
  • 120
    • 0033972054 scopus 로고    scopus 로고
    • On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily
    • DOI 10.1128/JB.182.3.723-727.2000
    • L. Debarbieux, and J. Beckwith On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily J. Bacteriol. 182 2000 723 727 (Pubitemid 30054003)
    • (2000) Journal of Bacteriology , vol.182 , Issue.3 , pp. 723-727
    • Debarbieux, L.1    Beckwith, J.2
  • 121
    • 0033564233 scopus 로고    scopus 로고
    • Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm
    • DOI 10.1093/emboj/18.12.3271
    • S. Jonda, M. Huber-Wunderlich, R. Glockshuber, and E. Mossner Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm EMBO J. 18 1999 3271 3281 (Pubitemid 29276574)
    • (1999) EMBO Journal , vol.18 , Issue.12 , pp. 3271-3281
    • Jonda, S.1    Huber-Wunderlich, M.2    Glockshuber, R.3    Mossner, E.4
  • 122
    • 15844371986 scopus 로고    scopus 로고
    • Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds
    • DOI 10.1074/jbc.271.18.10616
    • M. Ostermeier, K. De Sutter, and G. Georgiou Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds J. Biol. Chem. 271 1996 10616 10622 (Pubitemid 26145795)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.18 , pp. 10616-10622
    • Ostermeier, M.1    De Sutter, K.2    Georgiou, G.3
  • 123
    • 60849121135 scopus 로고    scopus 로고
    • Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. Coli periplasm
    • M. Eser, L. Masip, H. Kadokura, G. Georgiou, and J. Beckwith Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm Proc. Natl. Acad. Sci. U. S. A. 106 2009 1572 1577
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 1572-1577
    • Eser, M.1    Masip, L.2    Kadokura, H.3    Georgiou, G.4    Beckwith, J.5
  • 124
    • 40849141969 scopus 로고    scopus 로고
    • Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway
    • J.L. Pan, I. Sliskovic, and J.C. Bardwell Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway J. Mol. Biol. 377 2008 1433 1442
    • (2008) J. Mol. Biol. , vol.377 , pp. 1433-1442
    • Pan, J.L.1    Sliskovic, I.2    Bardwell, J.C.3
  • 126
    • 25444517605 scopus 로고    scopus 로고
    • A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm
    • DOI 10.1074/jbc.M503075200
    • M.S. Pittman, H.C. Robinson, and R.K. Poole A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm J. Biol. Chem. 280 2005 32254 32261 (Pubitemid 41361833)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32254-32261
    • Pittman, M.S.1    Robinson, H.C.2    Poole, R.K.3
  • 127
    • 84865559539 scopus 로고    scopus 로고
    • Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA
    • S.S. Chng, R.J. Dutton, K. Denoncin, D. Vertommen, J.F. Collet, H. Kadokura, and J. Beckwith Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA Mol. Microbiol. 85 2012 996 1006
    • (2012) Mol. Microbiol. , vol.85 , pp. 996-1006
    • Chng, S.S.1    Dutton, R.J.2    Denoncin, K.3    Vertommen, D.4    Collet, J.F.5    Kadokura, H.6    Beckwith, J.7
  • 128
    • 34047225116 scopus 로고    scopus 로고
    • Common themes and variations in the rhodanese superfamily
    • DOI 10.1080/15216540701206859, PII 776197113
    • R. Cipollone, P. Ascenzi, and P. Visca Common themes and variations in the rhodanese superfamily IUBMB Life 59 2007 51 59 (Pubitemid 46535402)
    • (2007) IUBMB Life , vol.59 , Issue.2 , pp. 51-59
    • Cipollone, R.1    Ascenzi, P.2    Visca, P.3
  • 130
    • 33646349748 scopus 로고    scopus 로고
    • Trafficking in persulfides: Delivering sulfur in biosynthetic pathways
    • E. Mueller Trafficking in persulfides: delivering sulfur in biosynthetic pathways Nat. Chem. Biol. 2 2006 185 194
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 185-194
    • Mueller, E.1
  • 131
    • 85056072751 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of PspE and GlpE, two single-domain sulfurtransferases of Escherichia coli
    • H. Cheng, J.L. Donahue, S.E. Battle, W.K. Ray, and T.J. Larson Biochemical and genetic characterization of PspE and GlpE, two single-domain sulfurtransferases of Escherichia coli Open Microbiol. J. 2 2008 18 28
    • (2008) Open Microbiol. J. , vol.2 , pp. 18-28
    • Cheng, H.1    Donahue, J.L.2    Battle, S.E.3    Ray, W.K.4    Larson, T.J.5
  • 132
    • 42049089494 scopus 로고    scopus 로고
    • Solution structures and backbone dynamics of Escherichia coli rhodanese PspE in its sulfur-free and persulfide-intermediate forms: Implications for the catalytic mechanism of rhodanese
    • DOI 10.1021/bi800039n
    • H. Li, F. Yang, X. Kang, B. Xia, and C. Jin Solution structures and backbone dynamics of Escherichia coli rhodanese PspE in its sulfur-free and persulfide-intermediate forms: Implications for the catalytic mechanism of rhodanese Biochemistry (N. Y.) 47 2008 4377 4385 (Pubitemid 351522086)
    • (2008) Biochemistry , vol.47 , Issue.15 , pp. 4377-4385
    • Li, H.1    Yang, F.2    Kang, X.3    Xia, B.4    Jin, C.5
  • 133
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • DOI 10.1016/j.cell.2005.10.044, PII S0092867405014121
    • G. Tian, S. Xiang, R. Noiva, W. Lennarz, and H. Schindelin The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites Cell 124 2006 61 73 (Pubitemid 43069310)
    • (2006) Cell , vol.124 , Issue.1 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3    Lennarz, W.J.4    Schindelin, H.5
  • 135
    • 79957530554 scopus 로고    scopus 로고
    • Engineered pathways for correct disulfide bond oxidation
    • G. Ren, and J.C.A. Bardwell Engineered pathways for correct disulfide bond oxidation Antioxid. Redox Signal. 14 2011 2399 2412
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2399-2412
    • Ren, G.1    Bardwell, J.C.A.2
  • 137
    • 0032189925 scopus 로고    scopus 로고
    • Disulfide bond formation in the Escherichia coli cytoplasm: An in vivo role reversal for the thioredoxins
    • DOI 10.1093/emboj/17.19.5543
    • E.J. Stewart, F. Aslund, and J. Beckwith Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins EMBO J. 17 1998 5543 5550 (Pubitemid 28445966)
    • (1998) EMBO Journal , vol.17 , Issue.19 , pp. 5543-5550
    • Stewart, E.J.1    Aslund, F.2    Beckwith, J.3
  • 138
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • DOI 10.1016/S0092-8674(01)00300-2
    • H.J. Choi, S.J. Kim, P. Mukhopadhyay, S. Cho, J.R. Woo, G. Storz, and S.E. Ryu Structural basis of the redox switch in the OxyR transcription factor Cell 105 2001 103 113 (Pubitemid 32323920)
    • (2001) Cell , vol.105 , Issue.1 , pp. 103-113
    • Choi, H.-J.1    Kim, S.-J.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.-R.5    Storz, G.6    Ryu, S.-E.7
  • 139
    • 0033767925 scopus 로고    scopus 로고
    • Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress
    • O. Carmel-Harel, and G. Storz Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress Annu. Rev. Microbiol. 54 2000 439 461
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 439-461
    • Carmel-Harel, O.1    Storz, G.2
  • 140
    • 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
  • 141
    • 0035812702 scopus 로고    scopus 로고
    • Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion
    • DOI 10.1126/science.1063143
    • D. Ritz, J. Lim, C.M. Reynolds, L.B. Poole, and J. Beckwith Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion Science 294 2001 158 160 (Pubitemid 32952968)
    • (2001) Science , vol.294 , Issue.5540 , pp. 158-160
    • Ritz, D.1    Lim, J.2    Reynolds, C.M.3    Poole, L.B.4    Beckwith, J.5
  • 142
    • 84857364837 scopus 로고    scopus 로고
    • Production of disulfide-bonded proteins in Escherichia coli
    • M. Berkmen Production of disulfide-bonded proteins in Escherichia coli Protein Expr. Purif. 82 2012 240 251
    • (2012) Protein Expr. Purif. , vol.82 , pp. 240-251
    • Berkmen, M.1
  • 143
    • 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
    • (1-2859-10-1)
    • V.D. Nguyen, F. Hatahet, K.E. Salo, E. Enlund, C. Zhang, and L.W. Ruddock 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 Factories 10 2011 (1-2859-10-1)
    • (2011) Microb. Cell Factories , vol.10
    • Nguyen, V.D.1    Hatahet, F.2    Salo, K.E.3    Enlund, E.4    Zhang, C.5    Ruddock, L.W.6
  • 144
    • 84860601037 scopus 로고    scopus 로고
    • SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm
    • J. Lobstein, C.A. Emrich, C. Jeans, M. Faulkner, P. Riggs, and M. Berkmen SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm Microb. Cell Factories 11 2012 56
    • (2012) Microb. Cell Factories , vol.11 , pp. 56
    • Lobstein, J.1    Emrich, C.A.2    Jeans, C.3    Faulkner, M.4    Riggs, P.5    Berkmen, M.6
  • 145
    • 84873208973 scopus 로고    scopus 로고
    • The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-alpha or mFIZZ1) in a wheat germ cell-free extract
    • W. Gad, M.G. Nair, K. Van Belle, K. Wahni, H. De Greve, J.A. Van Ginderachter, G. Vandenbussche, Y. Endo, D. Artis, and J. Messens The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-alpha or mFIZZ1) in a wheat germ cell-free extract PLoS ONE 8 2013 e55621
    • (2013) PLoS ONE , vol.8 , pp. 55621
    • Gad, W.1    Nair, M.G.2    Van Belle, K.3    Wahni, K.4    De Greve, H.5    Van Ginderachter, J.A.6    Vandenbussche, G.7    Endo, Y.8    Artis, D.9    Messens, J.10
  • 146
    • 0037372822 scopus 로고    scopus 로고
    • DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors
    • DOI 10.1128/IAI.71.3.1590-1595.2003
    • U. Ha, Y. Wang, and S. Jin DsbA of Pseudomonas aeruginosa is essential for multiple virulence factors Infect. Immun. 71 2003 1590 1595 (Pubitemid 36254353)
    • (2003) Infection and Immunity , vol.71 , Issue.3 , pp. 1590-1595
    • Ha, U.-H.1    Wang, Y.2    Jin, S.3
  • 147
    • 37249007770 scopus 로고    scopus 로고
    • The role of disulfide bond isomerase A (DsbA) of Escherichia coli O157:H7 in biofilm formation and virulence
    • DOI 10.1111/j.1574-6968.2007.00993.x
    • Y. Lee, Y. Kim, S. Yeom, S. Kim, S. Park, C.O. Jeon, and W. Park The role of disulfide bond isomerase A (DsbA) of Escherichia coli O157: H7 in biofilm formation and virulence FEMS Microbiol. Lett. 278 2008 213 222 (Pubitemid 350264579)
    • (2008) FEMS Microbiology Letters , vol.278 , Issue.2 , pp. 213-222
    • Lee, Y.1    Kim, Y.2    Yeom, S.3    Kim, S.4    Park, S.5    Jeon, C.O.6    Park, W.7
  • 149
    • 77949599606 scopus 로고    scopus 로고
    • Characterization of the DsbA oxidative folding catalyst from Pseudomonas aeruginosa reveals a highly oxidizing protein that binds small molecules
    • S.R. Shouldice, B. Heras, R. Jarrott, P. Sharma, M.J. Scanlon, and J.L. Martin Characterization of the DsbA oxidative folding catalyst from Pseudomonas aeruginosa reveals a highly oxidizing protein that binds small molecules Antioxid. Redox Signal. 12 2010 921 931
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 921-931
    • Shouldice, S.R.1    Heras, B.2    Jarrott, R.3    Sharma, P.4    Scanlon, M.J.5    Martin, J.L.6
  • 150
    • 77956015631 scopus 로고    scopus 로고
    • Application of fragment-based drug discovery to membrane proteins: Identification of ligands of the integral membrane enzyme DsbB
    • V. Fruh, Y. Zhou, D. Chen, C. Loch, E. AB, Y.N. Grinkova, H. Verheij, S.G. Sligar, J.H. Bushweller, and G. Siegal Application of fragment-based drug discovery to membrane proteins: identification of ligands of the integral membrane enzyme DsbB Chem. Biol. 17 2010 881 891
    • (2010) Chem. Biol. , vol.17 , pp. 881-891
    • Fruh, V.1    Zhou, Y.2    Chen, D.3    Loch, C.4    Ab, E.5    Grinkova, Y.N.6    Verheij, H.7    Sligar, S.G.8    Bushweller, J.H.9    Siegal, G.10
  • 152
    • 80055082271 scopus 로고    scopus 로고
    • Accelerated profile HMM searches
    • S.R. Eddy Accelerated profile HMM searches PLoS Comput. Biol. 7 2011 e1002195
    • (2011) PLoS Comput. Biol. , vol.7 , pp. 1002195
    • Eddy, S.R.1
  • 153
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • DOI 10.1093/nar/gkh340
    • R. Edgar MUSCLE: multiple sequence alignment with high accuracy and high throughput Nucleic Acids Res. 32 2004 1792 1797 (Pubitemid 38832724)
    • (2004) Nucleic Acids Research , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 154
    • 34547489084 scopus 로고    scopus 로고
    • Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments
    • DOI 10.1080/10635150701472164, PII 780704285
    • G. Talavera, and J. Castresana Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments Syst. Biol. 56 2007 564 577 (Pubitemid 47171631)
    • (2007) Systematic Biology , vol.56 , Issue.4 , pp. 564-577
    • Talavera, G.1    Castresana, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.