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The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner

Bibliographic reference Vertommen, Didier ; Depuydt, Matthieu ; Pan, Jonathan ; Leverrier, Pauline ; Knoops, Laurent ; et. al. The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner. In: Molecular Microbiology, Vol. 67, no. 2, p. 336-349 (2008)
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  1. Bardwell James C.A., McGovern Karen, Beckwith Jon, Identification of a protein required for disulfide bond formation in vivo, 10.1016/0092-8674(91)90532-4
  2. Bardwell J. C., Lee J. O., Jander G., Martin N., Belin D., Beckwith J., A pathway for disulfide bond formation in vivo., 10.1073/pnas.90.3.1038
  3. Inaba Kenji, Murakami Satoshi, Suzuki Mamoru, Nakagawa Atsushi, Yamashita Eiki, Okada Kengo, Ito Koreaki, Crystal Structure of the DsbB-DsbA Complex Reveals a Mechanism of Disulfide Bond Generation, 10.1016/j.cell.2006.10.034
  4. Bader Martin, Muse Wilson, Ballou David P, Gassner Christian, Bardwell James C.A, Oxidative Protein Folding Is Driven by the Electron Transport System, 10.1016/s0092-8674(00)81016-8
  5. Collet Jean-Francois, Bardwell James C. A., Oxidative protein folding in bacteria : Oxidative protein folding in bacteria, 10.1046/j.1365-2958.2002.02851.x
  6. Kadokura H., Snapshots of DsbA in Action: Detection of Proteins in the Process of Oxidative Folding, 10.1126/science.1091724
  7. Leichert Lars I, Jakob Ursula, Protein Thiol Modifications Visualized In Vivo, 10.1371/journal.pbio.0020333
  8. Hiniker Annie, Bardwell James C. A., In VivoSubstrate Specificity of Periplasmic Disulfide Oxidoreductases, 10.1074/jbc.m311391200
  9. Berkmen M., Boyd D., Beckwith J., The Nonconsecutive Disulfide Bond of Escherichia coli Phytase (AppA) Renders It Dependent on the Protein-disulfide Isomerase, DsbC, 10.1074/jbc.m411774200
  10. Messens J., J Biol Chem, 282, 31302 (2007)
  11. Zapun A., Biochemistry, 34, 5075 (1995)
  12. Bessette Paul H., Cotto José J., Gilbert Hiram F., Georgiou George, In Vivoandin VitroFunction of theEscherichia coliPeriplasmic Cysteine Oxidoreductase DsbG, 10.1074/jbc.274.12.7784
  13. Messens Joris, Collet Jean-François, Pathways of disulfide bond formation in Escherichia coli, 10.1016/j.biocel.2005.12.011
  14. Rietsch A., Belin D., Martin N., Beckwith J., An in vivo pathway for disulfide bond isomerization in Escherichia coli, 10.1073/pnas.93.23.13048
  15. Katzen F., Cell, 103, 769 (2000)
  16. Collet J.F., J Biol Chem, 277, 26886 (2002)
  17. Rozhkova A., EMBO J, 23, 1709 (2004)
  18. Cho S.H., J Bacteriol, 188, 5066 (2006)
  19. Hiniker A., J Bacteriol, 188, 7317 (2006)
  20. Hiniker A., J Biol Chem, 280, 33785 (2005)
  21. Andersen C.L., Mol Microbiol, 26, 121 (1997)
  22. Hiniker A., Proc Natl Acad Sci USA, 104, 11670 (2007)
  23. Heras B., Proc Natl Acad Sci USA, 101, 8876 (2004)
  24. Sevier Carolyn S., Kaiser Chris A., Conservation and Diversity of the Cellular Disulfide Bond Formation Pathways, 10.1089/ars.2006.8.797
  25. Gruber C.W., Trends Biochem Sci, 31, 455 (2006)
  26. Duguay A.R., J Bacteriol, 184, 6918 (2002)
  27. Ferenci T., FEMS Microbiol Lett, 52, 335 (1989)
  28. Bos C., J Bacteriol, 180, 605 (1998)
  29. Liu X., J Biol Chem, 276, 1146 (2001)
  30. Altermark B., Acta Crystallogr D Biol Crystallogr, 62, 1387 (2006)
  31. Liu Hongbin, Sadygov Rovshan G., Yates John R., A Model for Random Sampling and Estimation of Relative Protein Abundance in Shotgun Proteomics, 10.1021/ac0498563
  32. Old William M., Meyer-Arendt Karen, Aveline-Wolf Lauren, Pierce Kevin G., Mendoza Alex, Sevinsky Joel R., Resing Katheryn A., Ahn Natalie G., Comparison of Label-free Methods for Quantifying Human Proteins by Shotgun Proteomics, 10.1074/mcp.m500084-mcp200
  33. Pugsley A.P., Mol Gen Genet, 237, 407 (1993)
  34. Dailey F.E., Proc Natl Acad Sci USA, 90, 1043 (1993)
  35. Chilcott G. S., Hughes K. T., Coupling of Flagellar Gene Expression to Flagellar Assembly in Salmonella enterica Serovar Typhimurium and Escherichia coli, 10.1128/mmbr.64.4.694-708.2000
  36. Ruiz Natividad, Silhavy Thomas J, Sensing external stress: watchdogs of the Escherichia coli cell envelope, 10.1016/j.mib.2005.02.013
  37. Mecsas J, Rouviere P E, Erickson J W, Donohue T J, Gross C A, The activity of sigma E, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins., 10.1101/gad.7.12b.2618
  38. Bordes P., Bouvier J., Conter A., Kolb A., Gutierrez C., Transient repressor effect of Fis on the growth phase-regulated osmE promoter of Escherichia coli K12, 10.1007/s00438-002-0733-y
  39. Lange R., J Bacteriol, 175, 7910 (1993)
  40. Repoila F., Gutierrez C., Osmotic induction of the periplasmic trehalase in Escherichia coli K12: characterization of the treA gene promoter, 10.1111/j.1365-2958.1991.tb00745.x
  41. Hagenmaier S., J Bacteriol, 179, 2073 (1997)
  42. Bader M. W., Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA, 10.1093/emboj/20.7.1555