메뉴 건너뛰기




Volumn 187, Issue 4, 2005, Pages 1504-1510

Mutational analysis of the disulfide catalysts DsbA and DsbB

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; DSBA PROTEIN; DSBB PROTEIN; GLUTAMINE; PROTEIN; QUINONE DERIVATIVE; TYROSINE; UNCLASSIFIED DRUG;

EID: 14544306637     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.4.1504-1510.2005     Document Type: Article
Times cited : (10)

References (39)
  • 1
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader, M., W. Muse, D. P. Ballou, C. Gassner, and J. C. Bardwell. 1999. Oxidative protein folding is driven by the electron transport system. Cell 98:217-227.
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.5
  • 2
    • 0032562757 scopus 로고    scopus 로고
    • Reconstitution of a protein disulfide catalytic system
    • Bader, M., W. Muse, T. Zander, and J. Bardwell. 1998. Reconstitution of a protein disulfide catalytic system. J. Biol. Chem. 273:10302-10307.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10302-10307
    • Bader, M.1    Muse, W.2    Zander, T.3    Bardwell, J.4
  • 3
    • 0034714289 scopus 로고    scopus 로고
    • Disulfide bonds are generated by quinone reduction
    • Bader, M. W., T. Xie, C. A. Yu, and J. C. Bardwell. 2000. Disulfide bonds are generated by quinone reduction. J. Biol. Chem. 275:26082-26088.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26082-26088
    • Bader, M.W.1    Xie, T.2    Yu, C.A.3    Bardwell, J.C.4
  • 5
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J. C., K. McGovern, and J. Beckwith. 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
  • 6
    • 0028593831 scopus 로고
    • The Escherichia coli dsbA gene is partly transcribed from the promoter of a weakly expressed upstream gene
    • Belin, P., and P. L. Boquet. 1994. The Escherichia coli dsbA gene is partly transcribed from the promoter of a weakly expressed upstream gene. Microbiology 140:3337-3348.
    • (1994) Microbiology , vol.140 , pp. 3337-3348
    • Belin, P.1    Boquet, P.L.2
  • 7
    • 0028167593 scopus 로고
    • A pleiotropic acid phosphatase-deficient mutant of Escherichia coli shows premature termination in the dsbA gene. Use of dsbA::phoA fusions to localize a structurally important domain in DsbA
    • Belin, P., E. Quemeneur, and P. L. Boquet. 1994. A pleiotropic acid phosphatase-deficient mutant of Escherichia coli shows premature termination in the dsbA gene. Use of dsbA::phoA fusions to localize a structurally important domain in DsbA. Mol. Gen. Genet. 242:23-32.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 23-32
    • Belin, P.1    Quemeneur, E.2    Boquet, P.L.3
  • 8
    • 0035151833 scopus 로고    scopus 로고
    • Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli
    • Bessette, P. H., J. Qiu, J. C. Bardwell, J. R. Swartz, and G. Georgiou. 2001. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. J. Bacteriol. 183:980-988.
    • (2001) J. Bacteriol. , vol.183 , pp. 980-988
    • Bessette, P.H.1    Qiu, J.2    Bardwell, J.C.3    Swartz, J.R.4    Georgiou, G.5
  • 9
    • 0027446271 scopus 로고
    • Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
    • Dailey, F. E., and H. C. Berg. 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
  • 10
    • 0026026342 scopus 로고
    • Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability
    • Doig, A. J., and D. H. Williams. 1991. Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. J. Mol. Biol. 217:389-398.
    • (1991) J. Mol. Biol. , vol.217 , pp. 389-398
    • Doig, A.J.1    Williams, D.H.2
  • 11
    • 0030724094 scopus 로고    scopus 로고
    • Protein disulfide isomerase and assisted protein folding
    • Gilbert, H. F. 1997. Protein disulfide isomerase and assisted protein folding. J. Biol. Chem. 272:29399-29402.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29399-29402
    • Gilbert, H.F.1
  • 12
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and P. H. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 14
    • 0030880594 scopus 로고    scopus 로고
    • Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His32 in DsbA stability
    • Guddat, L. W., J. C. Bardwell, R. Glockshuber, M. Huber-Wunderlich, T. Zander, and J. L. Martin. 1997. Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Protein Sci. 6:1893-1900.
    • (1997) Protein Sci. , vol.6 , pp. 1893-1900
    • Guddat, L.W.1    Bardwell, J.C.2    Glockshuber, R.3    Huber-Wunderlich, M.4    Zander, T.5    Martin, J.L.6
  • 15
    • 0031010755 scopus 로고    scopus 로고
    • The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding
    • Guddat, L. W., J. C. Bardwell, T. Zander, and J. L. Martin. 1997. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding. Protein Sci. 6:1148-1156.
    • (1997) Protein Sci. , vol.6 , pp. 1148-1156
    • Guddat, L.W.1    Bardwell, J.C.2    Zander, T.3    Martin, J.L.4
  • 16
    • 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., G. Jander, N. L. Martin, and J. Beckwith. 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
  • 17
    • 0031776171 scopus 로고    scopus 로고
    • A single dipeptide sequence modulates the redox properties of a whole enzyme family
    • Huber-Wunderlich, M., and R. Glockshuber. 1998. A single dipeptide sequence modulates the redox properties of a whole enzyme family. Fold. Des. 3:161-171.
    • (1998) Fold. Des. , vol.3 , pp. 161-171
    • Huber-Wunderlich, M.1    Glockshuber, R.2
  • 18
    • 0022374336 scopus 로고
    • Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli
    • Hussain, M., A. Carlino, M. J. Madonna, and J. O. Lampen. 1985. Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli. J. Bacteriol. 164:223-229.
    • (1985) J. Bacteriol. , vol.164 , pp. 223-229
    • Hussain, M.1    Carlino, A.2    Madonna, M.J.3    Lampen, J.O.4
  • 19
    • 1342304093 scopus 로고    scopus 로고
    • DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation
    • Inaba, K., Y. H. Takahashi, and K. Ito. 2004. DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. J. Biol. Chem. 279:6761-6768.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6761-6768
    • Inaba, K.1    Takahashi, Y.H.2    Ito, K.3
  • 20
    • 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., N. L. Martin, and J. Beckwith. 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
  • 21
    • 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
    • Kadokura, H., M. Bader, H. Tian, J. C. Bardwell, and J. Beckwith. 2000. 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. USA 97:10884-10889.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10884-10889
    • Kadokura, H.1    Bader, M.2    Tian, H.3    Bardwell, J.C.4    Beckwith, J.5
  • 22
    • 0026567097 scopus 로고
    • Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
    • Kamitani, S., Y. Akiyama, and K. Ito. 1992. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11:57-62.
    • (1992) EMBO J. , vol.11 , pp. 57-62
    • Kamitani, S.1    Akiyama, Y.2    Ito, K.3
  • 23
    • 0030072669 scopus 로고    scopus 로고
    • Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli
    • Kishigami, S., and K. Ito. 1996. Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli. Genes Cells 1:201-208.
    • (1996) Genes Cells , vol.1 , pp. 201-208
    • Kishigami, S.1    Ito, K.2
  • 24
    • 0029161150 scopus 로고
    • DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
    • Kishigami, S., E. Kanaya, M. Kikuchi, and K. Ito. 1995. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. 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
  • 25
    • 0028886558 scopus 로고
    • Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family
    • Kortemme, T., and T. E. Creighton. 1995. Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family. J. Mol. Biol. 253:799-812.
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 26
    • 0027223571 scopus 로고
    • Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo
    • Martin, J. L., G. Waksman, J. C. Bardwell, J. Beckwith, and J. Kuriyan. 1993. Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J. Mol. Biol. 230:1097-1100.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1097-1100
    • Martin, J.L.1    Waksman, G.2    Bardwell, J.C.3    Beckwith, J.4    Kuriyan, J.5
  • 27
  • 28
    • 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., C. Georgopoulos, and S. Raina. 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
  • 29
    • 0025897176 scopus 로고
    • Escherichia coli chromosomal mutations that permit direct cloning of the Bacteroides fragilis metallo-beta-lactamase gene, ccrA
    • Rasmussen, B. A., Y. Gluzman, and F. P. Tally. 1991. Escherichia coli chromosomal mutations that permit direct cloning of the Bacteroides fragilis metallo-beta-lactamase gene, ccrA. Mol. Microbiol. 5:1211-1219.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1211-1219
    • Rasmussen, B.A.1    Gluzman, Y.2    Tally, F.P.3
  • 30
    • 0030969326 scopus 로고    scopus 로고
    • Insertional inactivation of dsbA produces sensitivity to cadmium and zinc in Escherichia coli
    • Rensing, C., B. Mitra, and B. P. Rosen. 1997. Insertional inactivation of dsbA produces sensitivity to cadmium and zinc in Escherichia coli. J. Bacteriol. 179:2769-2771.
    • (1997) J. Bacteriol. , vol.179 , pp. 2769-2771
    • Rensing, C.1    Mitra, B.2    Rosen, B.P.3
  • 32
    • 0013865825 scopus 로고
    • Zinc as a cofactor for cephalosporinase from Bacillus cereus 569
    • Sabath, L. D., and E. P. Abraham. 1966. Zinc as a cofactor for cephalosporinase from Bacillus cereus 569. Biochem. J. 98:11C-13C.
    • (1966) Biochem. J. , vol.98
    • Sabath, L.D.1    Abraham, E.P.2
  • 34
    • 0025806533 scopus 로고
    • Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme
    • Taniyama, Y., R. Kuroki, F. Omura, C. Seko, and M. Kikuchi. 1991. Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme. J. Biol. Chem. 266:6456-6461.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6456-6461
    • Taniyama, Y.1    Kuroki, R.2    Omura, F.3    Seko, C.4    Kikuchi, M.5
  • 35
    • 0029885303 scopus 로고    scopus 로고
    • Calculation of Cys 30 delta pKa's and oxidising power for DsbA mutants
    • Warwicker, J., and P. J. Gane. 1996. Calculation of Cys 30 delta pKa's and oxidising power for DsbA mutants. FEBS Lett. 385:105-108.
    • (1996) FEBS Lett. , vol.385 , pp. 105-108
    • Warwicker, J.1    Gane, P.J.2
  • 36
    • 0027481123 scopus 로고
    • Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
    • Wunderlich, M., and R. Glockshuber. 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
  • 37
    • 0037127202 scopus 로고    scopus 로고
    • Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B
    • Xie, T., L. Yu, M. W. Bader, J. C. Bardwell, and C. A. Yu. 2002. Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. J. Biol. Chem. 277:1649-1652.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1649-1652
    • Xie, T.1    Yu, L.2    Bader, M.W.3    Bardwell, J.C.4    Yu, C.A.5
  • 38
    • 0027467430 scopus 로고
    • Cloning and active site mutagenesis of Vibrio cholerae DsbA, a periplasmic enzyme that catalyzes disulfide bond formation
    • Yu, J., S. McLaughlin, R. B. Freedman, and T. R. Hirst. 1993. Cloning and active site mutagenesis of Vibrio cholerae DsbA, a periplasmic enzyme that catalyzes disulfide bond formation. J. Biol. Chem. 268:4326-4330.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4326-4330
    • Yu, J.1    McLaughlin, S.2    Freedman, R.B.3    Hirst, T.R.4
  • 39
    • 0028355571 scopus 로고
    • Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
    • Zapun, A., L. Cooper, and T. E. Creighton. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.