dsbD

Summary

Gene Symbol: dsbD
Description: thiol:disulfide interchange protein and activator of DsbC
Alias: ECK4130, JW5734, cutA2, cycZ, dipZ, htrI
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Mavridou D, Stevens J, Ferguson S, Redfield C. Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy. J Mol Biol. 2007;370:643-58 pubmed
    The periplasmic C-terminal domain of the Escherichia coli DsbD protein (cDsbD) has a thioredoxin fold...
  2. Stirnimann C, Grutter M, Glockshuber R, Capitani G. nDsbD: a redox interaction hub in the Escherichia coli periplasm. Cell Mol Life Sci. 2006;63:1642-8 pubmed
    b>DsbD is a redox-active protein of the inner Escherichia coli membrane possessing an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain...
  3. Katzen F, Beckwith J. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell. 2000;103:769-79 pubmed
    The cytoplasmic membrane protein DsbD transfers electrons from the cytoplasm to the periplasm of E. coli, where its reducing power is used to maintain cysteines in certain proteins in the reduced state...
  4. Katzen F, Beckwith J. Role and location of the unusual redox-active cysteines in the hydrophobic domain of the transmembrane electron transporter DsbD. Proc Natl Acad Sci U S A. 2003;100:10471-6 pubmed
    The central hydrophobic domain of the membrane protein DsbD catalyzes the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli...
  5. Haebel P, Goldstone D, Katzen F, Beckwith J, Metcalf P. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex. EMBO J. 2002;21:4774-84 pubmed
    ..specifically activated by the periplasmic N-terminal domain (DsbDalpha) of the transmembrane electron transporter DsbD. An intermediate of the electron transport reaction was trapped, yielding a covalent DsbC-DsbDalpha complex. The 2...
  6. Gordon E, Page M, Willis A, Ferguson S. Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function. Mol Microbiol. 2000;35:1360-74 pubmed
    b>DipZ is a bacterial cytoplasmic membrane protein that transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment...
  7. Goulding C, Sawaya M, Parseghian A, Lim V, Eisenberg D, Missiakas D. Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD. Biochemistry. 2002;41:6920-7 pubmed
    Escherichia coli DsbD transports electrons across the plasma membrane, a pathway that leads to the reduction of protein disulfide bonds...
  8. Ito K, Inaba K. The disulfide bond formation (Dsb) system. Curr Opin Struct Biol. 2008;18:450-8 pubmed publisher
    ..respectively, that are transmitted across the cytoplasmic membrane through integral membrane components DsbB and DsbD. In both pathways, alternating interactions between a Cys-XX-Cys-containing thioredoxin domain and other regulatory ..
  9. Crooke H, Cole J. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain. Mol Microbiol. 1995;15:1139-50 pubmed
    ..The mutation in strain JCB606, dipZ, was mapped by P1 transduction close to the mel operon at co-ordinate 4425 on the E...

More Information

Publications60

  1. Collet J, Riemer J, Bader M, Bardwell J. Reconstitution of a disulfide isomerization system. J Biol Chem. 2002;277:26886-92 pubmed
    ..responsible for disulfide isomerization involves thioredoxin, thioredoxin reductase, and the DsbC, DsbG, and DsbD proteins. To be active as isomerases, DsbC and DsbG must be kept reduced...
  2. Chung J, Chen T, Missiakas D. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Mol Microbiol. 2000;35:1099-109 pubmed
    ..Cytoplasmic electrons donated by thioredoxin are thought to be transferred into the periplasm via the DsbD membrane protein...
  3. 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
    b>DsbD from Escherichia coli catalyzes the transport of electrons from cytoplasmic thioredoxin to the periplasmic disulfide isomerase DsbC...
  4. Hiniker A, Vertommen D, Bardwell J, Collet J. Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues. J Bacteriol. 2006;188:7317-20 pubmed
    The mechanism by which DsbD transports electrons across the cytoplasmic membrane is unknown. Here we provide evidence that DsbD's conformation depends on its oxidation state...
  5. Stirnimann C, Rozhkova A, Grauschopf U, Böckmann R, Glockshuber R, Capitani G, et al. High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallographic, biochemical and computational study. J Mol Biol. 2006;358:829-45 pubmed
    Escherichia coli DsbD transports electrons from cytoplasmic thioredoxin to periplasmic target proteins. DsbD is composed of an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain, connected by a central transmembrane domain...
  6. Kim J, Kim S, Jeong D, Son J, Ryu S. Crystal structure of DsbDgamma reveals the mechanism of redox potential shift and substrate specificity(1). FEBS Lett. 2003;543:164-9 pubmed
    The Escherichia coli transmembrane protein DsbD transfers electrons from the cytoplasm to the periplasm through a cascade of thiol-disulfide exchange reactions...
  7. Goldstone D, Haebel P, Katzen F, Bader M, Bardwell J, Beckwith J, et al. DsbC activation by the N-terminal domain of DsbD. Proc Natl Acad Sci U S A. 2001;98:9551-6 pubmed
    ..b>DsbD is a membrane protein required to maintain the functional oxidation state of DsbC and DsbG...
  8. Rietsch A, Bessette P, Georgiou G, Beckwith J. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol. 1997;179:6602-8 pubmed
    ..involving the cytoplasmic proteins thioredoxin reductase and thioredoxin and the cytoplasmic membrane protein DsbD is responsible for the reduction of these cysteines...
  9. Collet J, Bardwell J. Oxidative protein folding in bacteria. Mol Microbiol. 2002;44:1-8 pubmed
    ..Two isomerases exist in Escherichia coli, DsbC and DsbG. The membrane protein DsbD maintains these disulphide isomerases in their reduced and thereby active form...
  10. Kimball R, Martin L, Saier M. Reversing transmembrane electron flow: the DsbD and DsbB protein families. J Mol Microbiol Biotechnol. 2003;5:133-49 pubmed
    b>DsbD and DsbB are two proteins that in Escherichia coli catalyze transmembrane electron flow in opposite directions, thereby allowing reversible oxidoreduction of periplasmic dithiol/disulfide-containing proteins...
  11. Joly J, Swartz J. In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. Biochemistry. 1997;36:10067-72 pubmed
    ..On the other hand, in vivo DsbC has one pair of cysteines oxidized and one pair reduced. DsbD is required to maintain this reduced pair of cysteines, confirming previous genetic results...
  12. 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
    ..coli chromosome and was complemented by the wild-type allele. Both DsbA and the recently described DipZ protein were shown to be essential for cytochrome c synthesis, suggesting that they act sequentially in a pathway ..
  13. Hiniker A, Bardwell J. Disulfide bond isomerization in prokaryotes. Biochemistry. 2003;42:1179-85 pubmed
  14. Hemmis C, Berkmen M, Eser M, Schildbach J. TrbB from conjugative plasmid F is a structurally distinct disulfide isomerase that requires DsbD for redox state maintenance. J Bacteriol. 2011;193:4588-97 pubmed publisher
    ..Interestingly, although TrbB diverges structurally from other disulfide bond isomerases, we show that like those isomerases, TrbB relies on DsbD from E. coli for maintenance of its C-X-X-C redox active site motif.
  15. Stevens J, Gordon E, Ferguson S. Overproduction of CcmABCDEFGH restores cytochrome c maturation in a DsbD deletion strain of E. coli: another route for reductant?. FEBS Lett. 2004;576:81-5 pubmed
    The multidomain transmembrane protein DsbD is essential for cytochrome c maturation (Ccm) in Escherichia coli and transports reductant to the otherwise oxidising environment of the bacterial periplasm...
  16. Pittman M, Robinson H, Poole R. A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm. J Biol Chem. 2005;280:32254-61 pubmed
    ..Overexpression of the cydDC operon in dsbD mutants defective in disulfide bond formation restores dithiothreitol tolerance and periplasmic cytochrome b ..
  17. Kurokawa Y, Yanagi H, Yura T. Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli. J Biol Chem. 2001;276:14393-9 pubmed
    ..These results suggest synergistic roles of DsbC and DsbD in disulfide isomerization that appear to become limiting upon NGF production...
  18. Haebel P, Wichman S, Goldstone D, Metcalf P. Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the alpha domain of the electron transporter DsbD. J Struct Biol. 2001;136:162-6 pubmed
    ..active site cysteines of DsbC are maintained in the active reduced form by the transmembrane electron transporter DsbD. DsbD obtains electrons from the cytoplasm, transports them across the inner membrane, and passes them onto ..
  19. 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
    ..able to compensate for the lack of dsbA function in vivo led us to the identification of a new gene, designated dsbD. Lack of DsbD protein leads to some, but not all, of the phenotypic defects observed with other dsb mutations, such ..
  20. Bessette P, Cotto J, Gilbert H, Georgiou G. In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J Biol Chem. 1999;274:7784-92 pubmed
    ..As in DsbC, the putative active site thiols in DsbG are completely reduced in vivo in a dsbD-dependent fashion, as would be expected if DsbG is acting as a disulfide isomerase or reductase...
  21. Rozhkova A, Glockshuber R. Kinetics of the intramolecular disulfide exchange between the periplasmic domains of DsbD. J Mol Biol. 2007;367:1162-70 pubmed
    b>DsbD from Escherichia coli catalyzes the transport of electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG...
  22. Iobbi Nivol C, Crooke H, Griffiths L, Grove J, Hussain H, Pommier J, et al. A reassessment of the range of c-type cytochromes synthesized by Escherichia coli K-12. FEMS Microbiol Lett. 1994;119:89-94 pubmed
    ..No other c-type cytochrome was detected under any growth condition tested. ..
  23. Tan J, Bardwell J. Key players involved in bacterial disulfide-bond formation. Chembiochem. 2004;5:1479-87 pubmed
  24. 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
    The bacterial membrane protein DsbD transfers electrons across the cytoplasmic membrane to reduce protein disulfide bonds in extracytoplasmic proteins...
  25. 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
  26. Zander T, Phadke N, Bardwell J. Disulfide bond catalysts in Escherichia coli. Methods Enzymol. 1998;290:59-74 pubmed
  27. 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 secreted proteins...
  28. Krupp R, Chan C, Missiakas D. DsbD-catalyzed transport of electrons across the membrane of Escherichia coli. J Biol Chem. 2001;276:3696-701 pubmed
    ..at least three proteins, the cytoplasmic thioredoxin reductase (TrxB) and thioredoxin (TrxA) as well as the DsbD membrane protein...
  29. Rietsch A, Belin D, Martin N, Beckwith J. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc Natl Acad Sci U S A. 1996;93:13048-53 pubmed
    ..Mutations in the dipZ and trxA genes have similar phenotypes...
  30. 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. ..
  31. Sambongi Y, Ferguson S. Specific thiol compounds complement deficiency in c-type cytochrome biogenesis in Escherichia coli carrying a mutation in a membrane-bound disulphide isomerase-like protein. FEBS Lett. 1994;353:235-8 pubmed
    Escherichia coli JCB606 carries a mutation in the dipZ gene, known to code for a disulphide isomerase-like protein, with the consequence that holo forms of neither exogenous nor endogenous c-type cytochromes are synthesised...
  32. 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. ..
  33. Han K, Park J, Seo H, Ahn K, Lee J. Multiple stressor-induced proteome responses of Escherichia coli BL21(DE3). J Proteome Res. 2008;7:1891-903 pubmed publisher
    ..The quantitative and systematic proteome analyses that we have performed provide more detailed information on E. coli BL21(DE3), a widely used host strain for recombinant protein overexpression. ..
  34. Nakamoto H, Bardwell J. Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim Biophys Acta. 2004;1694:111-9 pubmed
    ..Proofreading of disulfide bond formation is performed by the DsbC/DsbD system, which has the ability to rearrange non-native disulfides to their native configuration...
  35. Fong S, Camakaris J, Lee B. Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12. Mol Microbiol. 1995;15:1127-37 pubmed
    ..Transcriptional fusions of cutA with the lux operon showed induction by copper, zinc, nickel, cobalt and, to a lesser extent, cadmium, manganese and silver salts. ..
  36. Cho S, Beckwith J. Mutations of the membrane-bound disulfide reductase DsbD that block electron transfer steps from cytoplasm to periplasm in Escherichia coli. J Bacteriol. 2006;188:5066-76 pubmed
    The cytoplasmic membrane protein DsbD keeps the periplasmic disulfide isomerase DsbC reduced, using the cytoplasmic reducing power of thioredoxin. DsbD contains three domains, each containing two reactive cysteines...
  37. 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
    ..to be corrected by a protein disulphide isomerase, DsbC, which is kept in the reduced and active configuration by DsbD. The DsbC/DsbD isomerization pathway is considered to be isolated from the DsbA/DsbB pathway...
  38. Skórko Glónekv J, Sobiecka A. [Periplasmatic disulfide oxidoreductases from bacterium Escherichia coli--their structure and function]. Postepy Biochem. 2005;51:459-67 pubmed
    ..separate pathways: (1) oxidizing (DsbA/DsbB system), responsible for introducing S-S bonds, and (2) reducing (DsbC/DsbD system, DsbG, CcmG and CcmH) which acts to isomerase wrongly formed disulfide bonds and participates in maturation ..
  39. Cho S, Beckwith J. Two snapshots of electron transport across the membrane: insights into the structure and function of DsbD. J Biol Chem. 2009;284:11416-24 pubmed publisher
    ..reduced by transfer of electrons from cytoplasmic thioredoxin-1 (Trx1) via the cytoplasmic membrane protein, DsbD. The transmembrane domain of DsbD (DsbDbeta), which comprises eight transmembrane segments (TMs), contains two ..
  40. Missiakas D, Raina S. Protein folding in the bacterial periplasm. J Bacteriol. 1997;179:2465-71 pubmed
  41. Fabianek R, Hennecke H, Thony Meyer L. Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli. FEMS Microbiol Rev. 2000;24:303-16 pubmed
    ..This review reflects the recently made efforts to elucidate the sources of oxidising and reducing power in the periplasm as well as the different properties of certain periplasmic protein thiol:disulfide oxidoreductases of E. coli. ..
  42. Katzen F, Deshmukh M, Daldal F, Beckwith J. Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J. 2002;21:3960-9 pubmed
    ..The multidomain transmembrane protein DsbD catalyzes the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli...
  43. Stewart P, D Ari R. Genetic and morphological characterization of an Escherichia coli chromosome segregation mutant. J Bacteriol. 1992;174:4513-6 pubmed
    ..Observation by fluorescence microscopy revealed the formation, at a nonpermissive temperature, of filaments containing one or two large nucleoids and of normal-size anucleate cells. There was also a significant loss of viability. ..
  44. Mavridou D, Stevens J, Goddard A, Willis A, Ferguson S, Redfield C. Control of periplasmic interdomain thiol:disulfide exchange in the transmembrane oxidoreductase DsbD. J Biol Chem. 2009;284:3219-26 pubmed publisher
    The bacterial protein DsbD transfers reductant from the cytoplasm to the otherwise oxidizing environment of the periplasm...
  45. Sambongi Y, Crooke H, Cole J, Ferguson S. A mutation blocking the formation of membrane or periplasmic endogenous and exogenous c-type cytochromes in Escherichia coli permits the cytoplasmic formation of Hydrogenobacter thermophilus holo cytochrome c552. FEBS Lett. 1994;344:207-10 pubmed
    ..thermophilus cytochrome c552 in E. coli does not involve the physiological pathway of c-type cytochrome biosynthesis in E. coli and that the haem insertion may be catalysed...
  46. Beck R, Crooke H, Jarsch M, Cole J, Burtscher H. Mutation in dipZ leads to reduced production of active human placental alkaline phosphatase in Escherichia coli. FEMS Microbiol Lett. 1994;124:209-14 pubmed
    We have tested the expression of alkaline phosphatases in a mutant strain of Escherichia coli deficient in dipZ, a gene coding for a protein involved in cytochrome c biogenesis, and the isogenic wild-type strain...
  47. Segatori L, Murphy L, Arredondo S, Kadokura H, Gilbert H, Beckwith J, et al. Conserved role of the linker alpha-helix of the bacterial disulfide isomerase DsbC in the avoidance of misoxidation by DsbB. J Biol Chem. 2006;281:4911-9 pubmed
    ..The kinetic partitioning of the DsbA/DsbB and DsbC/DsbD pathways partly depends on the ability of DsbB to oxidize DsbA at rates >1000 times greater than DsbC...
  48. Stewart E, Katzen F, Beckwith J. 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. 1999;18:5963-71 pubmed
    ..coli periplasmic protein disulfide bond isomerase (DsbC) are kept reduced by the cytoplasmic membrane protein, DsbD. DsbD, in turn, is reduced by cytoplasmic thioredoxin, indicating that DsbD transfers disulfidereducing potential ..
  49. Rozhkova A, Glockshuber R. Thermodynamic aspects of DsbD-mediated electron transport. J Mol Biol. 2008;380:783-8 pubmed publisher
    b>DsbD from Escherichia coli transports electrons from cytoplasmic thioredoxin across the inner membrane to the periplasmic substrate proteins DsbC, DsbG and CcmG...
  50. Stirnimann C, Rozhkova A, Grauschopf U, Grutter M, Glockshuber R, Capitani G. Structural basis and kinetics of DsbD-dependent cytochrome c maturation. Structure. 2005;13:985-93 pubmed
    b>DsbD from Escherichia coli transports two electrons from cytoplasmic thioredoxin to the periplasmic substrate proteins DsbC, DsbG and CcmG...
  51. Bader M, Bardwell J. Catalysis of disulfide bond formation and isomerization in Escherichia coli. Adv Protein Chem. 2001;59:283-301 pubmed