dsbA

Summary

Gene Symbol: dsbA
Description: periplasmic protein disulfide isomerase I
Alias: ECK3852, JW3832, dsf, iarA, ppfA
Species: Escherichia coli str. K-12 substr. MG1655
Products:     dsbA

Top Publications

  1. Hiniker A, Bardwell J. In vivo substrate specificity of periplasmic disulfide oxidoreductases. J Biol Chem. 2004;279:12967-73 pubmed
    ..coli periplasmic disulfide oxidoreductases, including the well characterized oxidase DsbA, has not yet been performed...
  2. Kadokura H, Tian H, Zander T, Bardwell J, Beckwith J. Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science. 2004;303:534-7 pubmed
    b>DsbA, a thioredoxin superfamily member, introduces disulfide bonds into newly translocated proteins. This process is thought to occur via formation of mixed disulfide complexes between DsbA and its substrates...
  3. Bardwell J, McGovern K, Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell. 1991;67:581-9 pubmed
    We describe a mutation (dsbA) that renders Escherichia coli severely defective in disulfide bond formation. In dsbA mutant cells, pulse-labeled beta-lactamase, alkaline phosphatase, and OmpA are secreted but largely lack disulfide bonds...
  4. Bardwell J. Building bridges: disulphide bond formation in the cell. Mol Microbiol. 1994;14:199-205 pubmed
    ..Disulphide bond formation in Escherichia coli is catalysed by at least three 'Dsb' proteins; DsbA, -B and -C...
  5. Vertommen D, Depuydt M, Pan J, Leverrier P, Knoops L, Szikora J, et al. The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner. Mol Microbiol. 2008;67:336-49 pubmed
    In Escherichia coli, DsbA introduces disulphide bonds into secreted proteins. DsbA is recycled by DsbB, which generates disulphides from quinone reduction...
  6. Nelson J, Creighton T. Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry. 1994;33:5974-83 pubmed
    b>DsbA is a periplasmic protein of Escherichia coli that appears to be the immediate donor of disulfide bonds to proteins that are secreted...
  7. Danese P, Silhavy T. The sigma(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli. Genes Dev. 1997;11:1183-93 pubmed
    ..Similarly, the Cpx system controls transcription of the dsbA locus, which encodes a periplasmic enzyme required for efficient disulfide bond formation in several ..
  8. Bessette P, Qiu J, Bardwell J, Swartz J, Georgiou G. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. J Bacteriol. 2001;183:980-8 pubmed
    We have examined the role of the active-site CXXC central dipeptides of DsbA and DsbC in disulfide bond formation and isomerization in the Escherichia coli periplasm...
  9. Kadokura H, Nichols L, Beckwith J. Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily. J Bacteriol. 2005;187:1519-22 pubmed
    The DsbA-DsbB pathway introduces disulfide bonds into newly translocated proteins...

More Information

Publications90

  1. Tang M, Nesbitt A, Sperling L, Berthold D, Schwieters C, Gennis R, et al. Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer. J Mol Biol. 2013;425:1670-82 pubmed publisher
    The integral membrane protein DsbB in Escherichia coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins...
  2. Noiva R. Enzymatic catalysis of disulfide formation. Protein Expr Purif. 1994;5:1-13 pubmed
    ..bridges is facilitated by the thiol-disulfide oxidoreductases, protein disulfide isomerase (PDI) in eukaryotes and dsbA in prokaryotes...
  3. Guddat L, Bardwell J, Glockshuber R, Huber Wunderlich M, Zander T, Martin J. Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Protein Sci. 1997;6:1893-900 pubmed
    b>DsbA, a 21-kDa protein from Escherichia coli, is a potent oxidizing disulfide catalyst required for disulfide bond formation in secreted proteins...
  4. Sambongi Y, Ferguson S. 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. 1996;398:265-8 pubmed
    Absence through mutation of two proteins involved in periplasmic disulphide bond formation, DsbA and DsbB, results in failure of anaerobically grown Escherichia coli to synthesise the holo forms of either its endogenous c-type cytochrome ..
  5. Tian H, Boyd D, Beckwith J. A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery. Proc Natl Acad Sci U S A. 2000;97:4730-5 pubmed
    ..The mutants defective in disulfide bond formation include additional classes of dsbA and dsbB mutations...
  6. Bader M, Hiniker A, Regeimbal J, Goldstone D, Haebel P, Riemer J, et al. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. EMBO J. 2001;20:1555-62 pubmed
    There are two distinct pathways for disulfide formation in prokaryotes. The DsbA-DsbB pathway introduces disulfide bonds de novo, while the DsbC-DsbD pathway functions to isomerize disulfides...
  7. Hiniker A, Bardwell J. Disulfide bond isomerization in prokaryotes. Biochemistry. 2003;42:1179-85 pubmed
  8. Inaba K. Disulfide bond formation system in Escherichia coli. J Biochem. 2009;146:591-7 pubmed publisher
    ..Coexisting in the periplasm of Escherichia coli are the DsbA-DsbB disulfide-introducing and DsbC-DsbD disulfide-isomerizing pathways, which promote the oxidative folding of ..
  9. Wunderlich M, Glockshuber R. In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA). J Biol Chem. 1993;268:24547-50 pubmed
    The formation of disulfide bonds in Escherichia coli is catalyzed by periplasmic protein disulfide-isomerase (DsbA)...
  10. Huber D, Boyd D, Xia Y, Olma M, Gerstein M, Beckwith J. Use of thioredoxin as a reporter to identify a subset of Escherichia coli signal sequences that promote signal recognition particle-dependent translocation. J Bacteriol. 2005;187:2983-91 pubmed
    We have previously reported that the DsbA signal sequence promotes efficient, cotranslational translocation of the cytoplasmic protein thioredoxin-1 via the bacterial signal recognition particle (SRP) pathway...
  11. Ito K. Editing disulphide bonds: error correction using redox currencies. Mol Microbiol. 2010;75:1-5 pubmed publisher
    The disulphide bond-introducing enzyme of bacteria, DsbA, sometimes oxidizes non-native cysteine pairs. DsbC should rearrange the resulting incorrect disulphide bonds into those with correct connectivity...
  12. Zapun A, Bardwell J, Creighton T. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry. 1993;32:5083-92 pubmed
    The protein DsbA facilitates disulfide bond formation in the periplasm of Escherichia coli. It has only two cysteine residues that are separated in the sequence by two other residues and are shown to form a disulfide bond reversibly...
  13. Tan J, Lu Y, Bardwell J. Mutational analysis of the disulfide catalysts DsbA and DsbB. J Bacteriol. 2005;187:1504-10 pubmed
    In prokaryotes, disulfides are generated by the DsbA-DsbB system. DsbB functions to generate disulfides by quinone reduction. These disulfides are passed to the DsbA protein and then to folding proteins...
  14. Wunderlich M, Otto A, Seckler R, Glockshuber R. Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH. Biochemistry. 1993;32:12251-6 pubmed
    Periplasmic protein disulfide isomerase (DsbA) is essential for disulfide formation in Escherichia coli...
  15. Stafford S, Humphreys D, Lund P. Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+. FEMS Microbiol Lett. 1999;174:179-84 pubmed
    ..Mutations in dsbA or dsbB, but not dsbC, increase the proportion of proteins with free thiols in the periplasm compared to wild-type...
  16. Inaba K, Ito K. [Structural basis for disulfide bond generation in the cell]. Tanpakushitsu Kakusan Koso. 2007;52:853-61 pubmed
  17. Porat A, Cho S, Beckwith J. The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases. Res Microbiol. 2004;155:617-22 pubmed
    ..Its substrates include protein disulfide isomerases and a protein involved in cytochrome c assembly. Two membrane-embedded cysteines in DsbD alternate between the disulfide-bonded (oxidized) and reduced states in this process. ..
  18. Debarbieux L, Beckwith J. On the functional interchangeability, oxidant versus reductant, of members of the thioredoxin superfamily. J Bacteriol. 2000;182:723-7 pubmed
    ..where it can also act as an oxidant, replacing the normal periplasmic catalyst of disulfide bond formation, DsbA, in oxidizing cell envelope proteins (L. Debarbieux and J. Beckwith, Proc. Natl. Acad. Sci...
  19. Inaba K, Murakami S, Suzuki M, Nakagawa A, Yamashita E, Okada K, et al. Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell. 2006;127:789-801 pubmed
    ..DsbB is an E. coli membrane protein that oxidizes DsbA, a periplasmic dithiol oxidase...
  20. Pugsley A. A mutation in the dsbA gene coding for periplasmic disulfide oxidoreductase reduces transcription of the Escherichia coli ompF gene. Mol Gen Genet. 1993;237:407-11 pubmed
    An insertion mutation in the Escherichia coli dsbA gene, coding for periplasmic disulfide oxidoreductase, dramatically reduces the level of OmpF porin protein in the cell envelope...
  21. Martin J, Bardwell J, Kuriyan J. Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Nature. 1993;365:464-8 pubmed
    ..The folding of such proteins is greatly accelerated in Escherichia coli by DsbA, but the mechanism of this rate enhancement is not well understood...
  22. Martin J, Waksman G, Bardwell J, Beckwith J, Kuriyan J. Crystallization of DsbA, an Escherichia coli protein required for disulphide bond formation in vivo. J Mol Biol. 1993;230:1097-100 pubmed
    b>DsbA is a 21 kDa protein that facilitates disulphide bond formation and is required for the correct folding and stability of a number of exported proteins in Escherichia coli...
  23. Inaba K, Ito K. Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine. Biochim Biophys Acta. 2008;1783:520-9 pubmed
    ..membrane-integrated DsbB protein cooperates with ubiquinone to generate a disulfide bond, which is transferred to DsbA, a periplasmic dithiol oxido-reductase that serves as the direct disulfide bond donor to proteins folding ..
  24. Kadokura H, Beckwith J. Detecting folding intermediates of a protein as it passes through the bacterial translocation channel. Cell. 2009;138:1164-73 pubmed publisher
    ..cotranslational and posttranslational folding intermediates of a periplasmic protein in which the protein and DsbA, a periplasmic disulfide bond-forming enzyme, are covalently linked by a disulfide bond...
  25. Kamitani S, Akiyama Y, Ito K. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 1992;11:57-62 pubmed
    ..It was susceptible to degradation by proteases in vivo and in vitro. The wild-type counterpart of this gene (named ppfA) has been sequenced and shown to encode a periplasmic protein with a pair of potentially redox-active cysteine ..
  26. Regeimbal J, Gleiter S, Trumpower B, Yu C, Diwakar M, Ballou D, et al. Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc Natl Acad Sci U S A. 2003;100:13779-84 pubmed
    ..In prokaryotic organisms, it is known that DsbB delivers oxidizing equivalents through DsbA to secreted proteins...
  27. Sandee D, Tungpradabkul S, Kurokawa Y, Fukui K, Takagi M. Combination of Dsb coexpression and an addition of sorbitol markedly enhanced soluble expression of single-chain Fv in Escherichia coli. Biotechnol Bioeng. 2005;91:418-24 pubmed
    ..coli by the Dsb coexpression system with the addition of sorbitol medium additive. This method might be applicable for high-yield soluble expression of proteins with multiple disulfide bonds. ..
  28. Hiniker A, Collet J, Bardwell J. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J Biol Chem. 2005;280:33785-91 pubmed
    In Escherichia coli, the periplasmic disulfide oxidoreductase DsbA is thought to be a powerful but nonspecific oxidant, joining cysteines together the moment they enter the periplasm...
  29. Paxman J, Borg N, Horne J, Thompson P, Chin Y, Sharma P, et al. The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes. J Biol Chem. 2009;284:17835-45 pubmed publisher
    ..This is a multistep process in which the dithiol-disulfide oxidoreductase enzyme, DsbA, plays a central role...
  30. Messens J, Collet J. Pathways of disulfide bond formation in Escherichia coli. Int J Biochem Cell Biol. 2006;38:1050-62 pubmed
    ..This review focuses on the pathways of disulfide bond formation and isomerization in bacteria, taking Escherichia coli as a model. ..
  31. Choo K, Tong J, Ranganathan S. Modeling Escherichia coli signal peptidase complex with bound substrate: determinants in the mature peptide influencing signal peptide cleavage. BMC Bioinformatics. 2008;9 Suppl 1:S15 pubmed publisher
    ..We report here a structure-based model for Escherichia coli DsbA 13-25 in complex with its endogenous type I SPase...
  32. Philipps B, Glockshuber R. Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli. J Biol Chem. 2002;277:43050-7 pubmed
    b>DsbA from Escherichia coli is the most oxidizing member of the thiol-disulfide oxidoreductase family (E(o)' = -122 mV) and is required for efficient disulfide bond formation in the periplasm...
  33. Rozhkova A, Stirnimann C, Frei P, Grauschopf U, Brunisholz R, Grutter M, et al. Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD. EMBO J. 2004;23:1709-19 pubmed
    ..disulfide exchange reactions between redox-active, periplasmic proteins and protein domains from the oxidative DsbA/B and the reductive DsbC/D pathway...
  34. Inaba K, Ito K. Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade. EMBO J. 2002;21:2646-54 pubmed
    ..redox properties of the redox active sites in DsbB to gain further insights into the catalytic mechanisms of DsbA oxidation. The standard redox potential of DsbB was determined to be -0...
  35. Guilhot C, Jander G, Martin N, Beckwith J. 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. 1995;92:9895-9 pubmed
    ..This process involves at least two proteins: DsbA and DsbB...
  36. Guddat L, Bardwell J, Martin J. Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization. Structure. 1998;6:757-67 pubmed
    ..The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family...
  37. Manjasetty B, Hennecke J, Glockshuber R, Heinemann U. Structure of circularly permuted DsbA(Q100T99): preserved global fold and local structural adjustments. Acta Crystallogr D Biol Crystallogr. 2004;60:304-9 pubmed
    The thiol-disulfide oxidoreductase DsbA is required for efficient formation of disulfide bonds in the Escherichia coli periplasm...
  38. Jacob Dubuisson F, Pinkner J, Xu Z, Striker R, Padmanhaban A, Hultgren S. PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA. Proc Natl Acad Sci U S A. 1994;91:11552-6 pubmed
    ..of uropathogenic Escherichia coli were not assembled by a strain that lacks the periplasmic disulfide isomerase DsbA. This defect was mostly attributed to the immunoglobulin-like pilus chaperone PapD, which possesses an unusual ..
  39. Thie H, Schirrmann T, Paschke M, Dubel S, Hust M. SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. coli. N Biotechnol. 2008;25:49-54 pubmed publisher
    ..Four leader peptides using the Sec pathway (PelB, OmpA, PhoA and pIII) and three using the SRP pathway (DsbA, TorT and TolB) were compared...
  40. Inaba K, Murakami S, Nakagawa A, Iida H, Kinjo M, Ito K, et al. Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB. EMBO J. 2009;28:779-91 pubmed publisher
    ..bonds are generated by the cooperation of DsbB and ubiquinone and transferred to substrate proteins through DsbA. The structures solved so far for different forms of DsbB lack the Cys104-Cys130 initial-state disulphide that is ..
  41. Tapley T, Eichner T, Gleiter S, Ballou D, Bardwell J. Kinetic characterization of the disulfide bond-forming enzyme DsbB. J Biol Chem. 2007;282:10263-71 pubmed
    ..In the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition at approximately 510 nm...
  42. Takahashi Y, Inaba K, Ito K. Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli. J Biol Chem. 2004;279:47057-65 pubmed
    ..In the protein disulfide-introducing system of Escherichia coli, plasma membrane-integrated DsbB oxidizes periplasmic DsbA, the primary disulfide donor...
  43. Bardwell J, Lee J, Jander G, Martin N, Belin D, Beckwith J. A pathway for disulfide bond formation in vivo. Proc Natl Acad Sci U S A. 1993;90:1038-42 pubmed
    Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations in the gene for a second protein, DsbB, which is also necessary for disulfide bond formation...
  44. Pugsley A, Bayan N, Sauvonnet N. Disulfide bond formation in secreton component PulK provides a possible explanation for the role of DsbA in pullulanase secretion. J Bacteriol. 2001;183:1312-9 pubmed
    ..Besides these pul genes, efficient pullulanase secretion also requires the host dsbA gene, encoding a periplasmic disulfide oxidoreductase, independently of disulfide bond formation in pullulanase ..
  45. Wunderlich M, Jaenicke R, Glockshuber R. The redox properties of protein disulfide isomerase (DsbA) of Escherichia coli result from a tense conformation of its oxidized form. J Mol Biol. 1993;233:559-66 pubmed
    Periplasmic protein disulfide isomerase (DsbA) from Escherichia coli is a strongly oxidizing thiol reagent with one catalytic disulfide bridge and an intrinsic redox potential of -0.089 V...
  46. Malojcic G, Owen R, Glockshuber R. Structural and mechanistic insights into the PAPS-independent sulfotransfer catalyzed by bacterial aryl sulfotransferase and the role of the DsbL/Dsbl system in its folding. Biochemistry. 2014;53:1870-7 pubmed publisher
    ..coli CFT073, DsbA, and the ASST-specific enzyme DsbL, to introduce the single, conserved disulfide bond into ASST...
  47. Malojcic G, Owen R, Grimshaw J, Glockshuber R. Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB. FEBS Lett. 2008;582:3301-7 pubmed publisher
    ..In bacteria, disulfide bonds are introduced by the periplasmic dithiol oxidase DsbA, which transfers its catalytic disulfide bond to folding polypeptides...
  48. Allen J, Barker P, Ferguson S. A cytochrome b562 variant with a c-type cytochrome CXXCH heme-binding motif as a probe of the Escherichia coli cytochrome c maturation system. J Biol Chem. 2003;278:52075-83 pubmed
    ..coli strains deficient in the periplasmic reductant DsbD or oxidant DsbA. In the DsbA- strain under aerobic conditions, c-type cytochromes were made abundantly and correctly when the Ccm ..
  49. Kadokura H, Beckwith J. Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA. EMBO J. 2002;21:2354-63 pubmed
    Protein disulfide bond formation in Escherichia coli is catalyzed by the periplasmic protein DsbA. A cytoplasmic membrane protein DsbB maintains DsbA in the oxidized state by transferring electrons from DsbA to quinones in the respiratory ..
  50. Pogliano J, Lynch A, Belin D, Lin E, Beckwith J. Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev. 1997;11:1169-82 pubmed
    ..First, activation of the Cpx pathway induces 5- to 10-fold the synthesis of DsbA, required for disulfide bond formation, and DegP, a major periplasmic protease...
  51. Joly J, Swartz J. Protein folding activities of Escherichia coli protein disulfide isomerase. Biochemistry. 1994;33:4231-6 pubmed
    b>DsbA is an Escherichia coli periplasmic protein that mediates disulfide bond formation in newly secreted proteins in vivo...
  52. Zhang Y, Zhuang R, Xu Z, Jin B. Generation of monoclonal antibodies against Escherichia coli DsbA. Hybridoma (Larchmt). 2008;27:131-4 pubmed
    Disulfide oxidoreductase A (also known as disulfide bond formation protein A, or DsbA) is produced in Escherichia coli (E...
  53. Leichert L, Jakob U. Protein thiol modifications visualized in vivo. PLoS Biol. 2004;2:e333 pubmed
    ..thiols were periplasmic proteins and were found to be in vivo substrates of the disulfide-bond-forming protein DsbA. We discovered a substantial number of redox-sensitive cytoplasmic proteins, whose thiol groups were significantly ..
  54. Dartigalongue C, Nikaido H, Raina S. Protein folding in the periplasm in the absence of primary oxidant DsbA: modulation of redox potential in periplasmic space via OmpL porin. EMBO J. 2000;19:5980-8 pubmed
    Disulfide bond formation in Escherichia coli is a catalyzed reaction accomplished by DsbA. We found that null mutations in a new porin gene, ompL, allowed a total bypass of the DsbA requirement for protein oxidation...
  55. Grauschopf U, Fritz A, Glockshuber R. Mechanism of the electron transfer catalyst DsbB from Escherichia coli. EMBO J. 2003;22:3503-13 pubmed
    ..coli is essential for disulfide bond formation and catalyses the oxidation of the periplasmic dithiol oxidase DsbA by ubiquinone. DsbB contains two catalytic disulfide bonds, Cys41-Cys44 and Cys104-Cys130...
  56. Bader M, Bardwell J. Catalysis of disulfide bond formation and isomerization in Escherichia coli. Adv Protein Chem. 2001;59:283-301 pubmed
  57. Hennecke J, Sebbel P, Glockshuber R. Random circular permutation of DsbA reveals segments that are essential for protein folding and stability. J Mol Biol. 1999;286:1197-215 pubmed
    ..As a model system, we used the disulfide oxidoreductase DsbA from Escherichia coli, a monomeric protein of 189 amino acid residues...
  58. Inaba K, Takahashi Y, Fujieda N, Kano K, Miyoshi H, Ito K. DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation. J Biol Chem. 2004;279:6761-8 pubmed
    DsbB is an Escherichia coli plasma membrane protein that reoxidizes the Cys30-Pro-His-Cys33 active site of DsbA, the primary dithiol oxidant in the periplasm...
  59. Pan J, Sliskovic I, Bardwell J. Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway. J Mol Biol. 2008;377:1433-42 pubmed publisher
    Disulfide bond formation occurs in secreted proteins in Escherichia coli when the disulfide oxidoreductase DsbA, a soluble periplasmic protein, nonspecifically transfers a disulfide to a substrate protein...
  60. Belin P, Boquet P. The Escherichia coli dsbA gene is partly transcribed from the promoter of a weakly expressed upstream gene. Microbiology. 1994;140 ( Pt 12):3337-48 pubmed
    The dsbA gene of Escherichia coli encodes a periplasmic enzyme which catalyses disulfide bond formation. Analysis of its surrounding DNA region showed that it is preceded by an open reading frame, orfA, of 984 nucleotides...
  61. Ondo Mbele E, Vivès C, Kone A, Serre L. Intriguing conformation changes associated with the trans/cis isomerization of a prolyl residue in the active site of the DsbA C33A mutant. J Mol Biol. 2005;347:555-63 pubmed
    Escherichia coli DsbA belongs to the thioredoxin family and catalyzes the formation of disulfide bonds during the folding of proteins in the bacterial periplasm...
  62. Ize B, Stanley N, Buchanan G, Palmer T. Role of the Escherichia coli Tat pathway in outer membrane integrity. Mol Microbiol. 2003;48:1183-93 pubmed
    ..The presence of genes encoding amidases with twin-arginine signal sequences in the genomes of other Gram-negative bacteria suggests that a similar cell envelope defect may be a common feature of tat mutant strains. ..
  63. Strauch E, Georgiou G. A bacterial two-hybrid system based on the twin-arginine transporter pathway of E. coli. Protein Sci. 2007;16:1001-8 pubmed
    ..In addition, we introduce the use of the cysteine disulfide oxidase DsbA as a reporter...
  64. Landeta C, Meehan B, McPartland L, Ingendahl L, Hatahet F, Tran N, et al. Inhibition of virulence-promoting disulfide bond formation enzyme DsbB is blocked by mutating residues in two distinct regions. J Biol Chem. 2017;292:6529-6541 pubmed publisher
    ..In the Escherichia coli disulfide bond formation pathway, the periplasmic protein DsbA introduces disulfide bonds into substrates, and then the cytoplasmic membrane protein DsbB reoxidizes DsbA's ..
  65. Inaba K, Takahashi Y, Ito K. Reactivities of quinone-free DsbB from Escherichia coli. J Biol Chem. 2005;280:33035-44 pubmed
    ..and Cys104-Cys130, facing the periplasm, as well as the bound quinone molecules play crucial roles in oxidizing DsbA, the protein dithiol oxidant in the periplasm...
  66. Pugsley A. Translocation of a folded protein across the outer membrane in Escherichia coli. Proc Natl Acad Sci U S A. 1992;89:12058-62 pubmed
    A mutation in the Escherichia coli dsbA gene (coding for a periplasmic disulfide oxidoreductase) reduces the rate of disulfide bond formation in the enzyme pullulanase and also reduces the rate at which the enzyme is secreted to the cell ..
  67. Dailey F, Berg H. Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc Natl Acad Sci U S A. 1993;90:1043-7 pubmed
    ..Cystine suppresses this defect in dsbB strains. We also show that dsbA strains [Bardwell, J. C. A., McGovern, K. & Beckwith, J...
  68. Metheringham R, Griffiths L, Crooke H, Forsythe S, Cole J. An essential role for DsbA in cytochrome c synthesis and formate-dependent nitrite reduction by Escherichia coli K-12. Arch Microbiol. 1995;164:301-7 pubmed
    ..The mutation was localized by conjugation, transduction, and Southern blotting experiments to the dsbA gene at minute 87 on the E. coli chromosome and was complemented by the wild-type allele...
  69. Messens J, Collet J, Van Belle K, Brosens E, Loris R, Wyns L. The oxidase DsbA folds a protein with a nonconsecutive disulfide. J Biol Chem. 2007;282:31302-7 pubmed
    ..In contrast, our study with RNase I shows that DsbA is a sufficient catalyst for correct disulfide formation in vivo and in vitro...
  70. Narzi D, Siu S, Stirnimann C, Grimshaw J, Glockshuber R, Capitani G, et al. Evidence for proton shuffling in a thioredoxin-like protein during catalysis. J Mol Biol. 2008;382:978-86 pubmed publisher
    ..A consistent catalytic mechanism for DsbL, probably conferrable to other proteins of the same class, is presented. Our results suggest a functional role of hydration entropy of active-site groups. ..
  71. Belin P, Quemeneur E, Boquet P. A pleîotropic 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. 1994;242:23-32 pubmed
    ..A DNA fragment that complements the mutation was cloned and shown to carry the dsbA gene, which encodes a periplasmic disulphide bond-forming factor...
  72. Yamanaka H, Kameyama M, Baba T, Fujii Y, Okamoto K. Maturation pathway of Escherichia coli heat-stable enterotoxin I: requirement of DsbA for disulfide bond formation. J Bacteriol. 1994;176:2906-13 pubmed
    ..The involvement of DsbA in the formation of the disulfide bonds of STp was examined in this study...
  73. Ortenberg R, Beckwith J. Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities. Antioxid Redox Signal. 2003;5:403-11 pubmed
  74. Zander T, Phadke N, Bardwell J. Disulfide bond catalysts in Escherichia coli. Methods Enzymol. 1998;290:59-74 pubmed
  75. Missiakas D, Schwager F, Raina S. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 1995;14:3415-24 pubmed
    Previous studies have established that DsbA and DsbC, periplasmic proteins of Escherichia coli, are two key players involved in disulfide bond formation...
  76. Tan J, Bardwell J. Key players involved in bacterial disulfide-bond formation. Chembiochem. 2004;5:1479-87 pubmed
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    It was shown previously that the Escherichia coli gene ppfA (dsbA) encodes a periplasmic protein, and its inactivation leads to a deficiency in disulfide bond formation of envelope proteins (Kamitani, S., Akiyama, Y., and Ito, K...
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    ..Three adhesion mutants harbored the transposon in the dsbA gene, whose product, DsbA, catalyses folding of numerous extracytoplasmic disulfide bond-containing proteins...
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