Oxidative protein folding in bacteria

Ten years ago it was thought that disulphide bond formation in prokaryotes occurred spontaneously. Now two pathways involved in disulphide bond formation have been well characterized, the oxidative pathway, which is responsible for the formation of disulphides, and the isomerization pathway, which shuffles incorrectly formed disulphides. Disulphide bonds are donated directly to unfolded polypeptides by the DsbA protein; DsbA is reoxidized by DsbB. DsbB generates disulphides de novo from oxidized quinones. These quinones are reoxidized by the electron transport chain, showing that disulphide bond formation is actually driven by electron transport. Disulphide isomerization requires that incorrect disulphides be attacked using a reduced catalyst, followed by the redonation of the disulphide, allowing alternative disulphide pairing. Two isomerases exist in Escherichia coli, DsbC and DsbG. The membrane protein DsbD maintains these disulphide isomerases in their reduced and thereby active form. DsbD is kept reduced by cytosolic thioredoxin in an NADPH‐dependent reaction.

[1]  M. Bader,et al.  Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA , 2001, The EMBO journal.

[2]  N. Sauvonnet,et al.  Disulfide Bond Formation in Secreton Component PulK Provides a Possible Explanation for the Role of DsbA in Pullulanase Secretion , 2001, Journal of bacteriology.

[3]  R. Krupp,et al.  DsbD-catalyzed Transport of Electrons across the Membrane ofEscherichia coli * , 2001, The Journal of Biological Chemistry.

[4]  T. Kobayashi,et al.  Identification of a segment of DsbB essential for its respiration‐coupled oxidation , 2001, Molecular microbiology.

[5]  J. Beckwith,et al.  Transmembrane Electron Transfer by the Membrane Protein DsbD Occurs via a Disulfide Bond Cascade , 2000, Cell.

[6]  J. Beckwith,et al.  Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[7]  M. Bader,et al.  Disulfide Bonds Are Generated by Quinone Reduction* , 2000, The Journal of Biological Chemistry.

[8]  C. Wang,et al.  The N-terminal Sequence (Residues 1–65) Is Essential for Dimerization, Activities, and Peptide Binding of Escherichia coli DsbC* , 2000, The Journal of Biological Chemistry.

[9]  F. Vinci,et al.  Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex. , 2000, Biochemistry.

[10]  M. Bader,et al.  DsbG, a Protein Disulfide Isomerase with Chaperone Activity* , 2000, The Journal of Biological Chemistry.

[11]  D. Missiakas,et al.  Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol–disulphide exchange and protein folding in the bacterial periplasm , 2000, Molecular microbiology.

[12]  M. D. Page,et al.  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 , 2000, Molecular microbiology.

[13]  V. Rybin,et al.  Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli , 2000, Nature Structural Biology.

[14]  F. Daldal,et al.  Novel Rhodobacter capsulatus genes required for the biogenesis of various c‐type cytochromes , 2000, Molecular microbiology.

[15]  J. Beckwith,et al.  Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli , 1999, The EMBO journal.

[16]  M. Bader,et al.  Oxidative Protein Folding Is Driven by the Electron Transport System , 1999, Cell.

[17]  Yan Wang,et al.  Chaperone Activity of DsbC* , 1999, The Journal of Biological Chemistry.

[18]  P. Lund,et al.  Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+. , 1999, FEMS microbiology letters.

[19]  Paul H. Bessette,et al.  In Vivo and in Vitro Function of theEscherichia coli Periplasmic Cysteine Oxidoreductase DsbG* , 1999, The Journal of Biological Chemistry.

[20]  Koreaki Ito,et al.  Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway , 1999, The EMBO journal.

[21]  L. Guddat,et al.  Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization. , 1998, Structure.

[22]  M. Bader,et al.  Reconstitution of a Protein Disulfide Catalytic System* , 1998, The Journal of Biological Chemistry.

[23]  N. Sauvonnet,et al.  The requirement for DsbA in pullulanase secretion is independent of disulphide bond formation in the enzyme , 1998, Molecular microbiology.

[24]  Paul H. Bessette,et al.  Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin , 1997, Journal of bacteriology.

[25]  H. Inokuchi,et al.  Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[26]  D. Missiakas,et al.  A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins , 1997, Molecular microbiology.

[27]  L. Guddat,et al.  The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding , 1997, Protein science : a publication of the Protein Society.

[28]  J. Song,et al.  Does DsbA have chaperone-like activity? , 1997, Archives of biochemistry and biophysics.

[29]  D. Missiakas,et al.  Making and breaking disulfide bonds. , 1997, Annual review of microbiology.

[30]  D. Belin,et al.  An in vivo pathway for disulfide bond isomerization in Escherichia coli. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[31]  Koreaki Ito,et al.  Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli , 1996, Genes to cells : devoted to molecular & cellular mechanisms.

[32]  J. Winther,et al.  Why is DsbA such an oxidizing disulfide catalyst? , 1995, Cell.

[33]  J. Beckwith,et al.  Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[34]  Koreaki Ito,et al.  DsbA-DsbB Interaction through Their Active Site Cysteines , 1995, The Journal of Biological Chemistry.

[35]  D. Missiakas,et al.  Identification and characterization of a new disulfide isomerase‐like protein (DsbD) in Escherichia coli. , 1995, The EMBO journal.

[36]  T. Creighton,et al.  Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. , 1995, Biochemistry.

[37]  J. Camakaris,et al.  Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K‐12 , 1995, Molecular microbiology.

[38]  H. Crooke,et al.  The biogenesis of c‐type cytochromes in Escherichia coli requires a membrane‐bound protein, DipZ, with a protein disulphide isomerase‐like domain , 1995, Molecular microbiology.

[39]  F. Jacob-Dubuisson,et al.  PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[40]  C. Georgopoulos,et al.  The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. , 1994, The EMBO journal.

[41]  John Kuriyan,et al.  Crystal structure of the DsbA protein required for disulphide bond formation in vivo , 1993, Nature.

[42]  C. Georgopoulos,et al.  Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[43]  T. Creighton,et al.  The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. , 1993, Biochemistry.

[44]  D. Belin,et al.  A pathway for disulfide bond formation in vivo. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[45]  H. Berg,et al.  Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[46]  Koreaki Ito,et al.  Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. , 1992, The EMBO journal.

[47]  J. Beckwith,et al.  Identification of a protein required for disulfide bond formation in vivo , 1991, Cell.