Site dsbA
- Name: dsbA
- Type: Gene
- Synonyms
b3860 MG1655 locus tag iarA increased ampicillin resistance, Alksne et al. ppfA - Mnemonic: disulfide bond
- Left End Point: 87.11
- Right End Point: 87.12
- Products:
disulfide oxidoreductase, periplasmic protein disulfide-isomerase - Direction: >
- Priority: 0
- 3 Alleles of This Gene
dsbA1::kan dsbA723(del)::kan dsbA791-YFP(::cat) - External Database Links:
Host Site Page Links EcoGene.org EG11297 EcoliWiki dsbA - Comment:
- essential role in cytochrome c synthesis and formate-dependent nitrite reduction. See Metheringham et al. Direct donor of disulfides to newly synth. periplasmic proteins
- References:
- Bardwell, J.C., K. McGovern, J.R. Beckwith 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67:581-589
- Pugsley, A.P. 1992. Translocation of a folded protein across the outer membrane in Escherichia coli. Proc.Natl.Acad.Sci.USA 89:12058-12062
- Akiyama, Y., S. Kamitani, N. Kusukawa, K. Ito 1992. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product. J.Biol.Chem. 267:22440-22445
- Bardwell, J.C., J.O. Lee, G. Jander, N. Martin, D. Belin, J.R. Beckwith 1993. A pathway for disulfide bond formation in vivo. Proc.Natl.Acad.Sci.USA 90:1038-1042
- Pugsley, A.P. 1993. A mutation in the dsbA gene coding for periplasmic disulfide oxidoreductase reduces transcription of the Escherichia coli ompF gene. Mol.Gen.Genet. 237:407-411
- Wunderlich, M., R. Glockshuber 1993. In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA). J.Biol.Chem. 268:24547-24550
- Dailey, F.E., H.C. Berg 1993. Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc.Natl.Acad.Sci.USA 90:1043-1047
- Belin, P., E. Quemeneur, 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. 2
- Yamanaka, H., M. Kameyama, T. Baba, Y. Fujii, K. Okamoto 1994. Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation. J.Bacteriol. 176:2906-2913
- Kishigami, S., E. Kanaya, M. Kikuchi, 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
- Guilhot, C., G. Jander, N.L. Martin, J.R. 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
- Metheringham, R., L. Griffiths, H. Crooke, S. Forsythe, J.A. Cole 1995. An essential role for DsbA in cytochrome c synthesis and formate-dependent nitrite reduction by Escherichia coli K-12. Arch.Microbiol. 164:301-307
- Alksne, L.E., D. Keeney, B.A. Rasmussen 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, Cc
- Sambongi, Y., S.J. Ferguson 1996. Mutants of Escherichia coli lacking disulphide oxidoreductases DsbA and DsbB cannot synthesise an exogenous monohaem c-type cytochrome except in the presence of disulphide compounds. FEBS Lett. 398:265-268
- Bader, M., W. Muse, T. Zander, J. Bardwell 1998. Reconstitution of a protein disulfide catalytic system. J.Biol.Chem. 273:10302-10307