Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli

Applied and Environmental Microbiology

Volumn 66, Issue 9, 2000, Pages 3960-3965

  Kurokawa, Y ^a   Yanagi, H ^a   Yura, T ^a  

^a NONE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HORSERADISH PEROXIDASE; ISOENZYME; ISOMERASE; POLYPEPTIDE; RECOMBINANT PROTEIN;

ARTICLE; BACTERIUM CULTURE; DISULFIDE BOND; ESCHERICHIA COLI; GENE OVEREXPRESSION; NONHUMAN; PEPTIDE SYNTHESIS; PLASMID; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN STABILITY;

CALCIUM CHLORIDE; DISULFIDES; ESCHERICHIA COLI; HORSERADISH PEROXIDASE; PERIPLASM; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; PROTEIN TRANSPORT; RECOMBINANT PROTEINS;

ARMORACIA RUSTICANA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0033827610     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.9.3960-3965.2000     Document Type: Article

References (33)

1. Dsb-insensitive expression of CcrA, a metallo-β-lactamase from Bacteroides fragilis, in Escherichia coli after amino acid substitution at two cysteine residues within CcrA
2. Recombinant protein expression in Escherichia coli
3. Building bridges: Disulphide bond formation in the cell
4. A pathway for disulfide bond formation in vivo
5. Expression of human placental alkaline phosphatase in Escherichia coli
6. Efficient folding of protein with multiple disulfide bonds in the Escherichia coli cytoplasm
7. Probing the structural role of an alpha beta loop of maltose-binding protein by mutagenesis: Heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies
8. Electron avenue: Pathways of disulfide bond formation and isomerization
9. Structure of the horseradish peroxidase isozyme C genes
10. Genomic DNA structure of two new horseradish-peroxidase-encoding genes
11. Expression of correctly folded proteins in Escherichia coli
12. Baculovirus expression and characterization of catalytically active horseradish peroxidase
13. Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation
14. Vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductase DsbA ad DsbC
15. Protein folding activities of Escherichia coli protein disulfide isomerase
16. Functional expression of horse-radish peroxidase in E. coli by directed evolution
17. Strategies for achieving high-level expression of genes in Escherichia coli
18. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
19. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo
20. Protein folding in the bacterial periplasm
21. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
22. How do polypeptides cross the mitochondrial membranes?
23. Chaperone coexpression plasmids: Differential and synergistic roles of Dna-K-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
24. Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases in the yield of a heterologous secreted protein with disulfide bonds
25. Expression of active human tissue-type plasminogen activator in Escherichia coli
26. An in vivo pathway for disulfide bond isomerization in Escherichia coli
27. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
28. 2+ and heme
29. Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds
30. Conformational states in denaturants of cytochrome c and horseradish peroxidases examined by fluorescence and circular dichroism
31. Effect of redox environment on the in vitro and in vivo folding of RTEM-1 beta-lactamase and Escherichia coli alkaline phosphatase
32. Protein folding in the periplasm of Escherichia coli