Identification of a segment of DsbB essential for its respiration-coupled oxidation

Molecular Microbiology

Volumn 39, Issue 1, 2001, Pages 158-165

  Kobayashi, T ^a   Takahashi, Y ^a   Ito, K ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; OXIDOREDUCTASE;

AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL RESPIRATION; DISULFIDE BOND; DNA FLANKING REGION; ESCHERICHIA COLI; GENE DELETION; GENE INSERTION; MUTAGENESIS; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; DITHIOTHREITOL; DRUG RESISTANCE, MICROBIAL; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, INSERTIONAL; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGEN CONSUMPTION; PROTEIN CONFORMATION; PROTEIN DISULFIDE-ISOMERASE;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0035186732     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2001.02229.x     Document Type: Article

References (18)

1. In vitro catalysis of oxidative folding of disulfide-bonded proteins by the Escherichia coli dsbA (ppfA) gene product
2. Redox potentials of glutaredoxins of the thioredoxin superfamily determined by direct protein-protein redox equilibria
3. Oxidative protein folding is driven by the electron transport system
4. Disulfide bonds are generated by quinone reduction
5. The CXXC motif: A rheostat in the active site
6. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
7. Why is DsbA such an oxidizing disulfide catalyst?
8. Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation
9. Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coll
10. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
11. Redox states of DsbA in the periplasm of Escherichia coli
12. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
13. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
14. A simple screen for permissive sites in proteins: Analysis of Escherichia coli Lac permease
15. Protein folding in the bacterial periplasm
16. Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo
17. The genetics of disulfide bond metabolism
18. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo