The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

dsbC  -  protein disulfide isomerase II

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK2888, JW2861, xprA
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of dsbC

  • We have identified and functionally characterized a new Escherichia coli gene, dsbC, whose product is involved in disulfide bond formation in the periplasmic space [1].
  • In contrast, dsbC and dsbD mutants showed no hypersensitivity [2].
  • Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi [3].

High impact information on dsbC

  • This gene, dsbC, codes for a 24 kDa periplasmic protein that contains a characteristic active site sequence of disulfide isomerases, Phe-X-X-X-X-Cys-X-X-Cys [4].
  • Null mutations in dsbC were obtained using a screen for dithiothreitol (DTT)-sensitive mutants and were shown to result in the accumulation of reduced forms of a variety of disulfide bond-containing periplasmic proteins [1].
  • Given the reliance of protein function on correct disulfide bonds, it is surprising that no phenotype has been established for null mutations in dsbC [5].
  • Our data suggest that the copper sensitivity of dsbC- strains arises from the inability of the cell to rearrange copper-catalyzed non-native disulfides in the absence of functional DsbC [5].
  • The dsbC gene introduced on a multicopy plasmid in a dsbA mutant was only partially able to restore EGZ secretion, indicating that even if DsbA and DsbC possess disulphide oxydoreductase activity, they are not completely interchangeable [3].

Chemical compound and disease context of dsbC


Biological context of dsbC

  • The importance of mRNA stability on the expression of DsbC is underscored by the short half-life of the dsbC transcript, which was found to be only 0.8 min at 37 degrees C in wild-type cells but was two- to threefold longer in some of the stronger mutants [7].
  • Although the coexpression of dsbC had furthermore a stabilizing effect on the cell viability, the relative yield of the solubly produced RBP was not much better [6].

Anatomical context of dsbC

  • Mutations in genes dsbC and dsbD did not affect kdp expression, suggesting that the trx effects on kdp are not mediated by alterations in protein disulfide bond status in the periplasm [8].


  1. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. Missiakas, D., Georgopoulos, C., Raina, S. EMBO J. (1994) [Pubmed]
  2. Tellurite-mediated thiol oxidation in Escherichia coli. Turner, R.J., Weiner, J.H., Taylor, D.E. Microbiology (Reading, Engl.) (1999) [Pubmed]
  3. Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi. Shevchik, V.E., Bortoli-German, I., Robert-Baudouy, J., Robinet, S., Barras, F., Condemine, G. Mol. Microbiol. (1995) [Pubmed]
  4. Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. Shevchik, V.E., Condemine, G., Robert-Baudouy, J. EMBO J. (1994) [Pubmed]
  5. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. Hiniker, A., Collet, J.F., Bardwell, J.C. J. Biol. Chem. (2005) [Pubmed]
  6. Improved folding of apo-retinol-binding protein in the periplasm of Escherichia coli: positive influences of dsbC coexpression and of an amino acid exchange in the vitamin A binding site. Schmidt, A.M., Bloss, I., Skerra, A. Protein Eng. (1998) [Pubmed]
  7. Genetic analysis of disulfide isomerization in Escherichia coli: expression of DsbC is modulated by RNase E-dependent mRNA processing. Zhan, X., Gao, J., Jain, C., Cieslewicz, M.J., Swartz, J.R., Georgiou, G. J. Bacteriol. (2004) [Pubmed]
  8. trans-acting mutations in loci other than kdpDE that affect kdp operon regulation in Escherichia coli: effects of cytoplasmic thiol oxidation status and nucleoid protein H-NS on kdp expression. Sardesai, A.A., Gowrishankar, J. J. Bacteriol. (2001) [Pubmed]
WikiGenes - Universities