Oxidative protein folding in bacteria

Molecular Microbiology

Volumn 44, Issue 1, 2002, Pages 1-8

  Collet, Jean Francois ^a,b   Bardwell, James C A ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BACTERIAL PROTEIN; BETA LACTAMASE; CADMIUM; CYTOCHROME C; DISULFIDE; DITHIOTHREITOL; DSBA PROTEIN; ISOMERASE; MERCURY; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; PENICILLIN G; POLYPEPTIDE; PROTEIN DSBB; PROTEIN DSBC; PROTEIN DSBD; PROTEIN DSBG; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN; UNCLASSIFIED DRUG;

CATALYST; DISULFIDE BOND; ELECTRON TRANSPORT; ESCHERICHIA COLI; GENE MUTATION; ISOMERISM; NONHUMAN; OXIDATION; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN STABILITY; PROTEIN STRUCTURE; SHORT SURVEY; STRUCTURE ANALYSIS;

BACTERIA; BACTERIAL PROTEINS; CELL MEMBRANE; ISOMERISM; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA;

EID: 0036224573     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2002.02851.x     Document Type: Short Survey

References (48)

1. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins
2. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA
3. Oxidative protein folding is driven by the electron transport system
4. Reconstitution of a protein disulfide catalytic system
5. Disulfide bonds are generated by quinone reduction
6. Identification of a protein required for disulfide bond formation in vivo
7. A pathway for disulfide bond formation in vivo
8. In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
9. Chaperone activity of DsbC
10. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm
11. Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex
12. The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain
13. Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
14. Novel Rhodobacter capsulatus genes required for the biogenesis of various c-type cytochromes
15. Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12
16. 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
17. Why is DsbA such an oxidizing disulfide catalyst?
18. The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding
19. Crystal structures of reduced and oxidized DsbA: Investigation of domain motion and thiolate stabilization
20. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
21. PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA
22. Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli
23. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
24. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
25. Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli
26. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
27. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
28. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
29. Identification of a segment of DsbB essential for its respiration- coupled oxidation
30. DsbD-catalyzed transport of electrons across the membrane of Escherichia coli
31. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
32. Crystal structure of the DsbA protein required for disulphide bond formation in vivo
33. An essential role for DsbA in cytochrome c synthesis and formate- dependent nitrite reduction by Escherichia coli K-12
34. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo
35. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
36. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
37. Disulfide bond formation in secreton component PulK provides a possible explanation for the role of DsbA in pullulanase secretion
38. Making and breaking disulfide bonds
39. An in vivo pathway for disulfide bond isomerization in Escherichia coli
40. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
41. The requirement for DsbA in pullulanase secretion is independent of disulphide bond formation in the enzyme
42. DsbG, a protein disulfide isomerase with chaperone activity
43. 2+
44. Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
45. The N-terminal sequence (residues 1-65) is essential for dimerization, activities, and peptide binding of Escherichia coli DsbC
46. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
47. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
48. Does DsbA have chaperone-like activity?