User menu

A new role for Escherichia coli DsbC protein in protection against oxidative stress

Bibliographic reference Denoncin, Katleen ; Vertommen, Didier ; Arts, Isabelle ; Goemans, Camille ; Collet, Jean-François. A new role for Escherichia coli DsbC protein in protection against oxidative stress. In: Journal of Biological Chemistry, Vol. 289, no. 18, p. 12356-12364
Permanent URL
  1. Goemans Camille, Denoncin Katleen, Collet Jean-François, Folding mechanisms of periplasmic proteins, 10.1016/j.bbamcr.2013.10.014
  2. Casadaban Malcolm J., Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu, 10.1016/0022-2836(76)90119-4
  3. Miller J. H. (1992) A Short Course in Bacterial Genetics: Laboratory Manual (Cold Spring Harbor Laboratory, ed), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
  4. Rietsch A, Bessette P, Georgiou G, Beckwith J, Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin., 10.1128/jb.179.21.6602-6608.1997
  5. Kawazu Shin-ichiro, Takemae Hitoshi, Komaki-Yasuda Kanako, Kano Shigeyuki, Target proteins of the cytosolic thioredoxin in Plasmodium falciparum, 10.1016/j.parint.2010.03.005
  6. Sturm Nicole, Jortzik Esther, Mailu Boniface M., Koncarevic Sasa, Deponte Marcel, Forchhammer Karl, Rahlfs Stefan, Becker Katja, Identification of Proteins Targeted by the Thioredoxin Superfamily in Plasmodium falciparum, 10.1371/journal.ppat.1000383
  7. Denoncin Katleen, Vertommen Didier, Paek Eunok, Collet Jean-François, The Protein-disulfide Isomerase DsbC Cooperates with SurA and DsbA in the Assembly of the Essential β-Barrel Protein LptD, 10.1074/jbc.m110.119321
  8. Newcomer, J. Biol. Chem, 254, 7529 (1979)
  9. Declerck Nathalie, Abelson John, Novel substrate specificity engineered in the arabinose binding protein, 10.1093/protein/7.8.997
  10. Horazdovsky B F, Hogg R W, Genetic reconstitution of the high-affinity L-arabinose transport system., 10.1128/jb.171.6.3053-3059.1989
  11. Newcomer, J. Biol. Chem, 256, 13213 (1981)
  12. Messens Joris, Collet Jean-François, Pathways of disulfide bond formation in Escherichia coli, 10.1016/j.biocel.2005.12.011
  13. Quiocho Florante A., Vyas Nand K., Novel stereospecificity of the L-arabinose-binding protein, 10.1038/310381a0
  14. Miller, J. Biol. Chem, 254, 7521 (1979)
  15. Hiniker Annie, Bardwell James C. A., In VivoSubstrate Specificity of Periplasmic Disulfide Oxidoreductases, 10.1074/jbc.m311391200
  16. 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
  17. Leverrier Pauline, Declercq Jean-Paul, Denoncin Katleen, Vertommen Didier, Hiniker Annie, Cho Seung-Hyun, Collet Jean-François, Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC, 10.1074/jbc.m111.224865
  18. Sun Xiu-xia, Wang Chih-chen, The N-terminal Sequence (Residues 1–65) Is Essential for Dimerization, Activities, and Peptide Binding ofEscherichia coliDsbC, 10.1074/jbc.m002406200
  19. Joly John C., Swartz James R., In Vitroandin VivoRedox States of theEscherichia coliPeriplasmic Oxidoreductases DsbA and DsbC, 10.1021/bi9707739
  20. Cho Seung-Hyun, Collet Jean-Francois, Many Roles of the Bacterial Envelope Reducing Pathways, 10.1089/ars.2012.4962
  21. Brot Nathan, Collet Jean-François, Johnson Lynnette C., Jönsson Thomas J., Weissbach Herbert, Lowther W. Todd, The Thioredoxin Domain ofNeisseria gonorrhoeaePilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases, 10.1074/jbc.m604971200
  22. Cho S.-H., Parsonage D., Thurston C., Dutton R. J., Poole L. B., Collet J.-F., Beckwith J., A New Family of Membrane Electron Transporters and Its Substrates, Including a New Cell Envelope Peroxiredoxin, Reveal a Broadened Reductive Capacity of the Oxidative Bacterial Cell Envelope, 10.1128/mbio.00291-11
  23. Dutton R. J., Boyd D., Berkmen M., Beckwith J., Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation, 10.1073/pnas.0804621105
  24. 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
  25. Vertommen, Mol. Microbiol, 67, 336 (2008)
  26. Vermersch, J. Biol. Chem, 265, 16592 (1990)
  27. Mao, J. Biol. Chem, 258, 12543 (1983)
  28. Schreier B., Stumpp C., Wiesner S., Hocker B., Computational design of ligand binding is not a solved problem, 10.1073/pnas.0907950106
  29. Guzman L M, Belin D, Carson M J, Beckwith J, Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter., 10.1128/jb.177.14.4121-4130.1995
  30. Reddie Khalilah G, Carroll Kate S, Expanding the functional diversity of proteins through cysteine oxidation, 10.1016/j.cbpa.2008.07.028
  31. Roos Goedele, Messens Joris, Protein sulfenic acid formation: From cellular damage to redox regulation, 10.1016/j.freeradbiomed.2011.04.031
  32. Depuydt M., Leonard S. E., Vertommen D., Denoncin K., Morsomme P., Wahni K., Messens J., Carroll K. S., Collet J.-F., A Periplasmic Reducing System Protects Single Cysteine Residues from Oxidation, 10.1126/science.1179557
  33. 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
  34. Shevchik, EMBO J, 13, 2007 (1994)
  35. Collet Jean-Francois, Messens Joris, Structure, Function, and Mechanism of Thioredoxin Proteins, 10.1089/ars.2010.3114