Gene Symbol: dsbC
Description: protein disulfide isomerase II
Alias: ECK2888, JW2861, xprA
Species: Escherichia coli str. K-12 substr. MG1655
Products:     dsbC

Top Publications

  1. Denoncin K, Vertommen D, Arts I, Goemans C, Rahuel Clermont S, Messens J, et al. A new role for Escherichia coli DsbC protein in protection against oxidative stress. J Biol Chem. 2014;289:12356-64 pubmed publisher
    We report a new function for Escherichia coli DsbC, a protein best known for disulfide bond isomerization in the periplasm. We found that DsbC regulates the redox state of the single cysteine of the L-arabinose-binding protein AraF...
  2. Yeh S, Koon N, Squire C, Metcalf P. Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG. Acta Crystallogr D Biol Crystallogr. 2007;63:465-71 pubmed
    b>DsbC and DsbG are periplasmic disulfide-bond isomerases, enzymes that facilitate the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement. Both enzymes also have in vitro chaperone activity...
  3. 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...
  4. Ito K, Inaba K. The disulfide bond formation (Dsb) system. Curr Opin Struct Biol. 2008;18:450-8 pubmed publisher
    ..of oxidized and reduced states of the specific terminal enzymes, DsbA that oxidizes target cysteines and DsbC that reduces an incorrect disulfide to allow its isomerization into the physiological one...
  5. Lovett S, Kolodner R. Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of recJ-overexpression plasmids. J Bacteriol. 1991;173:353-64 pubmed
    ..The addition of a ribosome-binding sequence fused to the initiator GTG of recJ in this construction was necessary to promote expression of high levels of RecJ protein. ..
  6. Hiniker A, Ren G, Heras B, Zheng Y, Laurinec S, Jobson R, et al. Laboratory evolution of one disulfide isomerase to resemble another. Proc Natl Acad Sci U S A. 2007;104:11670-5 pubmed
    ..to determine functionally important structural differences between two distantly related disulfide isomerases, DsbC and DsbG from Escherichia coli...
  7. 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
    ..Together, unusually fast disulfide interchange reactions and a preference for folding polypeptides appear to be responsible for the catalytic efficiency of DsbA and for disulfide formation in vivo at acidic pH. ..
  8. Metheringham R, Tyson K, Crooke H, Missiakas D, Raina S, Cole J. Effects of mutations in genes for proteins involved in disulphide bond formation in the periplasm on the activities of anaerobically induced electron transfer chains in Escherichia coli K12. Mol Gen Genet. 1996;253:95-102 pubmed
    ..The Nrf+ activity and cytochrome c content of mutants defective in DsbC, DsbE or DsbF were similar to those of the parental, wild-type strain...
  9. Zhang Z, Huang H. [Escherichia coli disulfide-forming related proteins: structures, functions and their application in gene engineering for expressing heterologous proteins in Escherichia coli]. Sheng Wu Gong Cheng Xue Bao. 2002;18:261-6 pubmed
    ..coli is a synergetic process depending on a series of Dsb proteins containing DsbA, DsbB, DsbC, DsbD, DsbE and DsbG...

More Information


  1. Leverrier P, Declercq J, Denoncin K, Vertommen D, Hiniker A, Cho S, et al. Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC. J Biol Chem. 2011;286:16734-42 pubmed publisher
    ..we show that formation of the nonconsecutive disulfides of RcsF depends on the periplasmic disulfide isomerase DsbC. We trapped RcsF in a mixed disulfide complex with DsbC, and we show that deletion of dsbC prevents the activation ..
  2. 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
    ..These incorrect disulphides are thought to be corrected by a protein disulphide isomerase, DsbC, which is kept in the reduced and active configuration by DsbD...
  3. Maskos K, Huber Wunderlich M, Glockshuber R. DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo. J Mol Biol. 2003;325:495-513 pubmed
    ..protein folding in the periplasm of Escherichia coli is catalyzed by the thiol-disulfide oxidoreductases DsbA and DsbC. We investigated the catalytic efficiency of these enzymes during folding of proteins with a very complex disulfide ..
  4. 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
    b>DsbC is a periplasmic protein of Escherichia coli that was previously identified by a genetic selection that rescued sensitivity to dithiothreitol in Tn10 mutagenized cells...
  5. 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
    In Escherichia coli, the periplasmic protein disulfide isomerase, DsbC, is maintained reduced by transfer of electrons from cytoplasmic thioredoxin-1 (Trx1) via the cytoplasmic membrane protein, DsbD...
  6. 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
    ..The results are discussed in terms of a general principle underlying the oxidizing properties of protein disulfide isomerases. ..
  7. Carrington P, Chivers P, Al Mjeni F, Sauer R, Maroney M. Nickel coordination is regulated by the DNA-bound state of NikR. Nat Struct Biol. 2003;10:126-30 pubmed publisher
  8. Noiva R. Enzymatic catalysis of disulfide formation. Protein Expr Purif. 1994;5:1-13 pubmed
    ..Systems for the expression of PDI in Escherichia coli and Spodoptera frugiperda cells have been developed which may prove useful in the expression of recombinant proteins. ..
  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. Chng S, Dutton R, Denoncin K, Vertommen D, Collet J, Kadokura H, et al. Overexpression of the rhodanese PspE, a single cysteine-containing protein, restores disulphide bond formation to an Escherichia coli strain lacking DsbA. Mol Microbiol. 2012;85:996-1006 pubmed publisher
    ..This activity depends on DsbC, the bacterial disulphide bond isomerase, but not on DsbB...
  11. Skórko Glónekv J, Sobiecka A. [Periplasmatic disulfide oxidoreductases from bacterium Escherichia coli--their structure and function]. Postepy Biochem. 2005;51:459-67 pubmed
    ..two 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 ..
  12. Arredondo S, Chen T, Riggs A, Gilbert H, Georgiou G. Role of dimerization in the catalytic properties of the Escherichia coli disulfide isomerase DsbC. J Biol Chem. 2009;284:23972-9 pubmed publisher
    The bacterial protein-disulfide isomerase DsbC is a homodimeric V-shaped enzyme that consists of a dimerization domain, two alpha-helical linkers, and two opposing thioredoxin fold catalytic domains...
  13. 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
    ..The ionization properties of the DsbA thiol groups can explain, at least partly, the high reactivity of its disulfide bonds and thiol groups at both neutral and acidic pH values. ..
  14. 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
    ..coli catalyzes the transport of electrons from cytoplasmic thioredoxin to the periplasmic disulfide isomerase DsbC. DsbD contains two periplasmically oriented domains at the N- and C-terminus (nDsbD and cDsbD) that are connected ..
  15. Mavridou D, Braun M, Thöny Meyer L, Stevens J, Ferguson S. Avoidance of the cytochrome c biogenesis system by periplasmic CXXCH motifs. Biochem Soc Trans. 2008;36:1124-8 pubmed publisher
    ..We also demonstrate covalent haem attachment at a low level in vivo to the periplasmic disulfide isomerase DsbC, which contains a native CXXCH motif...
  16. 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
    ..in an oxidized state and of a reduced enzyme that catalyzes the rearrangement of mispaired cysteine residues (DsbC) is important for the folding of proteins containing multiple disulfide bonds...
  17. 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. ..
  18. Hiniker A, Bardwell J. In vivo substrate specificity of periplasmic disulfide oxidoreductases. J Biol Chem. 2004;279:12967-73 pubmed
    ..extract and two-dimensional gel electrophoresis to identify substrates of the periplasmic oxidoreductases DsbA, DsbC, and DsbG...
  19. Premkumar L, Kurth F, Neyer S, Schembri M, Martin J. The multidrug resistance IncA/C transferable plasmid encodes a novel domain-swapped dimeric protein-disulfide isomerase. J Biol Chem. 2014;289:2563-76 pubmed publisher
    ..integrative and conjugative elements (ICE) from commensal and pathogenic bacteria identified a conserved DsbC/DsbG homolog (DsbP)...
  20. Banaszak K, Mechin I, Frost G, Rypniewski W. Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2004;60:1747-52 pubmed publisher
    Disufide-bond isomerase (DsbC) plays a crucial role in folding periplasmically excreted bacterial proteins. The crystal structure of the reduced form of DsbC is presented...
  21. Kohda J, Kawahara N, Fukuda H, Kondo A. Effect of oxidized and reduced forms of Escherichia coli DsbC on protein refolding. J Biosci Bioeng. 2002;94:130-4 pubmed
    b>DsbC, which catalyzes disulfide isomerization, was overproduced in the periplasm of Escherichia coli and purified from the periplasmic fraction by osmotic shock and anion-exchange chromatography...
  22. 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
    ..The DsbA-DsbB pathway introduces disulfide bonds de novo, while the DsbC-DsbD pathway functions to isomerize disulfides...
  23. Lovett S, Clark A. Cloning of the Escherichia coli recJ chromosomal region and identification of its encoded proteins. J Bacteriol. 1985;162:280-5 pubmed
    ..A 9.6-kilobase BamHI-SalI fragment carrying the temperature-sensitive mutation recJ147 was also cloned and used for complementation studies to identify other recJ mutations. ..
  24. 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
    ..These results suggest that a productive folding pathway for subunits requires sequential interactions with DsbA and the PapD chaperone. ..
  25. 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. ..
  26. 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
    The protein disulfide bond isomerase DsbC catalyzes the rearrangement of incorrect disulfide bonds during oxidative protein folding in the periplasm of Escherichia coli...
  27. Missiakas D, Georgopoulos C, Raina S. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 1994;13:2013-20 pubmed
    We have identified and functionally characterized a new Escherichia coli gene, dsbC, whose product is involved in disulfide bond formation in the periplasmic space...
  28. 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
    ..The DsbB mutants were dependent on the disulfide oxidoreductase DsbC, a soluble periplasmic thiol-disulfide isomerase, for complementation...
  29. 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. ..
  30. 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...
  31. 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
    ..b>DsbC, the primary disulfide isomerase, likely resolves incorrect disulfides...
  32. 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...
  33. Chen J, Song J, Zhang S, Wang Y, Cui D, Wang C. Chaperone activity of DsbC. J Biol Chem. 1999;274:19601-5 pubmed
    b>DsbC, a periplasmic disulfide isomerase of Gram-negative bacteria, displays about 30% of the activities of eukaryotic protein disulfide isomerase (PDI) as isomerase and as thiol-protein oxidoreductase...
  34. 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...
  35. 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
    ..These features suggest that DsbA might act by binding to partially folded polypeptide chains before oxidation of cysteine residues. ..
  36. Berkmen M, Boyd D, Beckwith J. The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. J Biol Chem. 2005;280:11387-94 pubmed
    ..coli require an additional protein for proper folding, the disulfide bond isomerase DsbC. Here we report studies on a native E...
  37. 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. ..
  38. Zander T, Phadke N, Bardwell J. Disulfide bond catalysts in Escherichia coli. Methods Enzymol. 1998;290:59-74 pubmed
  39. 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
    ..This suppression was not dependent on DsbC and DsbG, since the oxidation status of these proteins was unaltered in ompL dsbA strains...
  40. Stafford S, Lund P. Mutagenic studies on human protein disulfide isomerase by complementation of Escherichia coli dsbA and dsbC mutants. FEBS Lett. 2000;466:317-22 pubmed
    ..assays for these activities of PDI, based on the demonstration that PDI can complement both a dsbA mutation and a dsbC mutation when expressed to the periplasm of Escherichia coli...
  41. Zapun A, Cooper L, Creighton T. Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo. Biochemistry. 1994;33:1907-14 pubmed
    ..This suggests that the thiol groups are involved in interactions that stabilize the folded conformation, which would cause any disulfide bonds, either inter- or intramolecular, that involve these groups to be unstable...
  42. Li H, Ke H, Ren G, Qiu X, Weng Y, Wang C. Thermal-induced dissociation and unfolding of homodimeric DsbC revealed by temperature-jump time-resolved infrared spectra. Biophys J. 2009;97:2811-9 pubmed publisher
    The thermal stability of DsbC, a homodimeric protein disulfide isomerase in prokaryotic periplasm, has been studied by using temperature-dependent Fourier transformation infrared and time-resolved infrared spectroscopy coupled with ..
  43. Bader M, Bardwell J. Catalysis of disulfide bond formation and isomerization in Escherichia coli. Adv Protein Chem. 2001;59:283-301 pubmed
  44. Denoncin K, Vertommen D, Paek E, Collet J. The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential ?-barrel protein LptD. J Biol Chem. 2010;285:29425-33 pubmed publisher
    ..We found that the periplasmic disulfide isomerase DsbC cooperates with SurA and the thiol oxidase DsbA in the folding of the essential ?-barrel protein LptD...
  45. Depuydt M, Leonard S, Vertommen D, Denoncin K, Morsomme P, Wahni K, et al. A periplasmic reducing system protects single cysteine residues from oxidation. Science. 2009;326:1109-11 pubmed publisher
    ..We discovered that DsbG and DsbC, two thioredoxin-related proteins, control the global sulfenic acid content of the periplasm and protect single ..
  46. 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
    ..The resulting crystals diffract to 2 A and belong to the monoclinic space group C2 with cell dimensions a = 117.5 A, b = 65.0 A, c76.3 A, beta = 126.3 degrees with two molecules in the asymmetric unit. ..
  47. Zapun A, Missiakas D, Raina S, Creighton T. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry. 1995;34:5075-89 pubmed
    b>DsbC is a soluble protein of the bacterial periplasm that was identified genetically as being involved in protein disulfide formation...
  48. Collet J, Riemer J, Bader M, Bardwell J. Reconstitution of a disulfide isomerization system. J Biol Chem. 2002;277:26886-92 pubmed
    ..the catalytic pathway 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...
  49. Tan J, Bardwell J. Key players involved in bacterial disulfide-bond formation. Chembiochem. 2004;5:1479-87 pubmed
  50. 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
  51. 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
    The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding...
  52. Segatori L, Paukstelis P, Gilbert H, Georgiou G. Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways. Proc Natl Acad Sci U S A. 2004;101:10018-23 pubmed
    In the Escherichia coli periplasm, the formation of protein disulfide bonds is catalyzed by DsbA and DsbC. DsbA is a monomer that is maintained in a fully oxidized state by the membrane enzyme DsbB, whereas DsbC is a dimer that is kept ..
  53. Hiniker A, Bardwell J. Disulfide bond isomerization in prokaryotes. Biochemistry. 2003;42:1179-85 pubmed
  54. Frishman D. DSBC protein: a new member of the thioredoxin fold-containing family. Biochem Biophys Res Commun. 1996;219:686-9 pubmed
    Prediction of the DsbC protein secondary structure has been performed using a novel prediction technique which is based on consideration of both local and long-range interactions between amino acid residues...
  55. 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
    ..periplasm of Escherichia coli involves Dsb proteins, including two related periplasmic disulfide-bond isomerases, DsbC and DsbG. DsbD is a membrane protein required to maintain the functional oxidation state of DsbC and DsbG...
  56. Bardwell J. Building bridges: disulphide bond formation in the cell. Mol Microbiol. 1994;14:199-205 pubmed
    ..DsbB is required for the reoxidation of DsbA. DsbC is active in disulphide rearrangements and appears to work synergistically with DsbA...
  57. Shevchik V, Condemine G, Robert Baudouy J. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 1994;13:2007-12 pubmed
    ..This gene, dsbC, codes for a 24 kDa periplasmic protein that contains a characteristic active site sequence of disulfide isomerases,..
  58. Schlapschy M, Grimm S, Skerra A. A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli. Protein Eng Des Sel. 2006;19:385-90 pubmed
    ..of four established periplasmic chaperones and folding catalysts: the thiol-disulfide oxidoreductases DsbA and DsbC that catalyze the formation and isomerization of disulfide bridges and the peptidyl-prolyl cis/trans-isomerases ..
  59. Stepanenko O, Kuznetsova I, Turoverov K, Huang C, Wang C. Conformational change of the dimeric DsbC molecule induced by GdnHCl. A study by intrinsic fluorescence. Biochemistry. 2004;43:5296-303 pubmed
    Unfolding-refolding of Escherichia coli DsbC, a homodimeric molecule, induced by GdnHCl was studied by intrinsic fluorescence. Interpretation of experimental fluorescence data was done together with the analysis of protein 3D structure...
  60. 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...
  61. Kurokawa Y, Yanagi H, Yura T. Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli. Appl Environ Microbiol. 2000;66:3960-5 pubmed
    Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli...
  62. Lee K, Zhan X, Gao J, Qiu J, Feng Y, Meganathan R, et al. RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli. Cell. 2003;114:623-34 pubmed
    ..Our results reveal a possible mechanism for the dynamic regulation of RNA decay and processing by inhibitory RNase binding proteins...
  63. Zhan X, Gao J, Jain C, Cieslewicz M, Swartz J, Georgiou G. Genetic analysis of disulfide isomerization in Escherichia coli: expression of DsbC is modulated by RNase E-dependent mRNA processing. J Bacteriol. 2004;186:654-60 pubmed
    ..This phenotype resulted from significantly increased expression of the bacterial disulfide isomerase DsbC. In seven of the eight mutants, the upregulation of DsbC was found to be related to defects in RNA processing by ..
  64. Ke H, Zhang S, Li J, Howlett G, Wang C. Folding of Escherichia coli DsbC: characterization of a monomeric folding intermediate. Biochemistry. 2006;45:15100-10 pubmed
    The homodimeric protein DsbC is a disulfide isomerase and a chaperone located in the periplasm of Escherichia coli...
  65. 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...
  66. Joly J, Swartz J. Protein folding activities of Escherichia coli protein disulfide isomerase. Biochemistry. 1994;33:4231-6 pubmed
    ..The reduced form of the protein is a disulfide isomerase while the oxidized protein can assist formation of disulfide bonds in reduced substrates under physiological conditions. ..
  67. Bessette P, Aslund F, Beckwith J, Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc Natl Acad Sci U S A. 1999;96:13703-8 pubmed
    ..of TrxA (thioredoxin 1) mutants with different redox potentials, or 20-fold by the protein disulfide isomerase, DsbC. Remarkably, higher yields of oxidized, biologically active proteins were obtained by expression in the cytoplasm ..