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Volumn 26, Issue 1, 1997, Pages 121-132

A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0030830073     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.5581925.x     Document Type: Article
Times cited : (94)

References (38)
  • 1
    • 0028028387 scopus 로고
    • Building bridges: Disulfide bond formation in the cell
    • Bardwell, J.C.A. (1994) Building bridges: disulfide bond formation in the cell. Mol Microbiol 14: 199-205.
    • (1994) Mol Microbiol , vol.14 , pp. 199-205
    • Bardwell, J.C.A.1
  • 4
    • 0026799490 scopus 로고
    • Structural and functional characterization of the mutant Escherichia coli glutaredoxine (C14-S) and its mixed disulfide with glutathione
    • Bushweller, J.H., Åslund, F., Wütrich, K., and Holmgren, A. (1992) Structural and functional characterization of the mutant Escherichia coli glutaredoxine (C14-S) and its mixed disulfide with glutathione. Biochemistry 31: 9288-9293.
    • (1992) Biochemistry , vol.31 , pp. 9288-9293
    • Bushweller, J.H.1    Åslund, F.2    Wütrich, K.3    Holmgren, A.4
  • 5
    • 0027139018 scopus 로고
    • A model catalyst of protein disulphide bond formation
    • Creighton, T.E., and Freedman, R.B. (1993) A model catalyst of protein disulphide bond formation. Curr Biol 3: 790-793.
    • (1993) Curr Biol , vol.3 , pp. 790-793
    • Creighton, T.E.1    Freedman, R.B.2
  • 6
    • 0027446271 scopus 로고
    • Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
    • Dailey, F.E., and Berg, H.C. (1993) Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc Natl Acad Sci USA 90: 1043-1047.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1043-1047
    • Dailey, F.E.1    Berg, H.C.2
  • 7
    • 0023272340 scopus 로고
    • Interposon mutagenesis of soil and water bacteria: A family of DNA fragments designed for in vitro insertional mutagenesis of Gram-negative bacteria
    • Fellay, R., Frey, J., and Krisch, H. (1987) Interposon mutagenesis of soil and water bacteria: a family of DNA fragments designed for in vitro insertional mutagenesis of Gram-negative bacteria. Gene 52: 147-154.
    • (1987) Gene , vol.52 , pp. 147-154
    • Fellay, R.1    Frey, J.2    Krisch, H.3
  • 9
    • 0022533631 scopus 로고
    • Cloning of genes from members of the family Enterobacteriaceae with mini-Mu bacteriophage containing plasmid replicons
    • Groisman, E., and Casadaban, M.J. (1986) Cloning of genes from members of the family Enterobacteriaceae with mini-Mu bacteriophage containing plasmid replicons. J Bacteriol 168: 357-364.
    • (1986) J Bacteriol , vol.168 , pp. 357-364
    • Groisman, E.1    Casadaban, M.J.2
  • 10
    • 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., and 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
  • 11
    • 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
  • 13
    • 0019163962 scopus 로고
    • Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli
    • Kallis, G.B., and Holmgren, A. (1980) Differential reactivity of the functional sulfhydryl groups of cysteine-32 and cysteine-35 present in the reduced form of thioredoxin from Escherichia coli. J Biol Chem 255: 10261-10265.
    • (1980) J Biol Chem , vol.255 , pp. 10261-10265
    • Kallis, G.B.1    Holmgren, A.2
  • 14
    • 0029161150 scopus 로고
    • DsbA-DsbB interactions through their active cysteines
    • Kishigami, S., Kanaya, E., Kikuchi, M., and Ito, K. (1995) DsbA-DsbB interactions through their active cysteines. J Biol Chem 270: 17072-17074.
    • (1995) J Biol Chem , vol.270 , pp. 17072-17074
    • Kishigami, S.1    Kanaya, E.2    Kikuchi, M.3    Ito, K.4
  • 15
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., Akiyama, K., and Isono, K. (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50: 495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 16
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil, C., and Beckwith, J. (1985) TnphoA: a transposon probe for protein export signals. Proc Natl Acad Sci USA 82: 8129-8133.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 18
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas, D., and Raina, S. (1997) Protein folding in the bacterial periplasm. J Bacteriol 179: 2465-2471.
    • (1997) J Bacteriol , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 19
    • 0027291239 scopus 로고
    • Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo
    • Missiakas, D., Georgopoulos, C., and Raina, S. (1993) Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc Natl Acad Sci USA 90: 7084-7088.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7084-7088
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 20
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas, D., Georgopoulos, C., and Raina, S. (1994) The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J 13: 2013-20.
    • (1994) EMBO J , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 21
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide-isomerase like protein (DsbD) in Escherichia coli
    • Missiakas, D., Schwager, F., and Raina, S. (1995) Identification and characterization of a new disulfide-isomerase like protein (DsbD) in Escherichia coli. EMBO J 14: 3415-3424.
    • (1995) EMBO J , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 22
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in the extra-cytoplasmic compartments of Escherichia coli: SurA, FkpA and Skp/ OmpH
    • Missiakas, D., Betton, J.-M., and Raina, S. (1996) New components of protein folding in the extra-cytoplasmic compartments of Escherichia coli: SurA, FkpA and Skp/ OmpH. Mol Microbiol 21: 871-884.
    • (1996) Mol Microbiol , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.-M.2    Raina, S.3
  • 24
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of sphaeroplasts
    • Neu, H.C., and Heppel, L.A. (1965) The release of enzymes from Escherichia coli by osmotic shock and during the formation of sphaeroplasts. J Biol Chem 240: 3685-3692.
    • (1965) J Biol Chem , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 25
    • 0020570384 scopus 로고
    • Role of primary structure and disulfide bond formation
    • Pollitt, S., and Zalkin, H. (1983) Role of primary structure and disulfide bond formation. J Bacteriol 153: 27-32.
    • (1983) J Bacteriol , vol.153 , pp. 27-32
    • Pollitt, S.1    Zalkin, H.2
  • 26
    • 0027085709 scopus 로고
    • Translocation of folded protein across the outer membrane in Escherichia coli
    • Pugsley, A.P. (1992) Translocation of folded protein across the outer membrane in Escherichia coli. Proc Natl Acad Sci USA 89: 12058-12062.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12058-12062
    • Pugsley, A.P.1
  • 27
    • 0030765627 scopus 로고    scopus 로고
    • Making and breaking of disulfide bonds
    • Raina, S., and Missiakas, D. (1997) Making and breaking of disulfide bonds. Annu Rev Microbiol 51: 179-202.
    • (1997) Annu Rev Microbiol , vol.51 , pp. 179-202
    • Raina, S.1    Missiakas, D.2
  • 30
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • Shevchik, V.E., Condemine, G., and 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
  • 32
    • 0023974826 scopus 로고
    • An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins
    • Strauch, K.L., and Beckwith, J. (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc Natl Acad Sci USA 85: 1576-1580.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1576-1580
    • Strauch, K.L.1    Beckwith, J.2
  • 34
    • 0025809486 scopus 로고
    • New pUC-derived cloning vectors with different selectable markers and DNA replication origins
    • Vieira, J., and Messing, J. (1991) New pUC-derived cloning vectors with different selectable markers and DNA replication origins. Gene 100: 189-194.
    • (1991) Gene , vol.100 , pp. 189-194
    • Vieira, J.1    Messing, J.2
  • 35
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich, M., and 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
  • 36
    • 0027254133 scopus 로고
    • The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
    • Zapun, A., Bardwell, J.C.A., and Creighton, T.E. (1993) The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry 32: 5083-5092.
    • (1993) Biochemistry , vol.32 , pp. 5083-5092
    • Zapun, A.1    Bardwell, J.C.A.2    Creighton, T.E.3
  • 37
    • 0028355571 scopus 로고
    • Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • Zapun, A., Cooper, L., and Creighton, T.E. (1994) Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry 33: 1907-1914.
    • (1994) Biochemistry , vol.33 , pp. 1907-1914
    • Zapun, A.1    Cooper, L.2    Creighton, T.E.3
  • 38
    • 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., and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.