Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum

Molecular Biology of the Cell

Volumn 11, Issue 9, 2000, Pages 2833-2843

  Frand, A R ^a   Kaiser, C A ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CYSTEINE; DISULFIDE; MEMBRANE PROTEIN; PROTEIN DISULFIDE ISOMERASE; PROTEIN ERO1P; SECRETORY PROTEIN; THIOL; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CELL VIABILITY; CHEMICAL REACTION; COMPLEX FORMATION; CONTROLLED STUDY; DISULFIDE BOND; ELECTRON TRANSPORT; ENDOPLASMIC RETICULUM; GENE MUTATION; GENETIC CONSERVATION; NONHUMAN; OXIDATION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN FOLDING; YEAST;

EID: 0034494605     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.9.2833     Document Type: Article

References (42)

1. Oxidative protein folding is driven by the electron transport system
2. Reconsritution of a protein disulfide catalytic system
3. Protein oxidation: Prime suspect found "not guilty."
4. A pathway for disulfide bond formation in vivo
5. Identification of a protein required for disulfide bond formation in vivo
6. Recent developments in the field of iron-sulfur proteins
7. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
8. The CXXC motif: A rheostat in the active site
9. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
10. Competition between glutathione and protein thiols for disulphide-bond formation
11. Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli
12. Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae
13. Electron avenue: Pathways of disulfide bond formation and isomerization
14. Identification of the three-dimensional thioredoxin motif: Related structure in the ORF3 protein of the Staphylococcus aureus mer operon
15. 2.8-Å structure of yeast serine carboxypeptidase
16. Pathways for protein disulfide bond formation in the endoplasmic reticulum
17. The ER01 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
18. Ero1p oxidizes PDI in a pathway for disulfide bond formation in the endoplasmic reticulum
19. Why is DsbA. such an oxidizing disulfide catalyst?
20. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
21. Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum
22. Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with reducing agent
23. Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation
24. Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers
25. Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulfide 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 coil cells
29. Efficient site-directed mutagenesis using uracil-containing DNA
30. Convergent evolution of similar function in two structurally divergent enzymes
31. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
32. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
33. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
34. Thioredoxin. A fold for all reasons
35. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo
36. Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
37. Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms
38. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
39. Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner
40. Scanning and escape during protein-disulfide isomerase-assisted protein folding
41. A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: Preparation and characterization