PMID:10025954
| Citation |
Battistoni, A, Mazzetti, AP and Rotilio, G (1999) In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli. FEBS Lett. 443:313-6 |
|---|---|
| Abstract |
We have found that the in vivo folding of periplasmic Escherichia coli Cu,Zn superoxide dismutase is assisted by DsbA, which catalyzes the efficient formation of its single disulfide bond, whose integrity is essential to ensure full catalytic activity to the enzyme. In line with these findings, we also report that the production of recombinant Xenopus laevis Cu,Zn superoxide dismutase is enhanced when the enzyme is exported in the periplasmic space or is expressed in thioredoxin reductase mutant strains. Our data show that inefficient disulfide bond oxidation in the bacterial cytoplasm inhibits Cu,Zn superoxide dismutase folding in this cellular compartment. |
| Links | |
| Keywords |
Animals; Cytoplasm/enzymology; Disulfides/metabolism; Dithiothreitol/pharmacology; Escherichia coli/enzymology; Escherichia coli/genetics; Kinetics; Mutation; Oxidation-Reduction/drug effects; Periplasm/enzymology; Protein Conformation/drug effects; Protein Disulfide-Isomerases/genetics; Protein Disulfide-Isomerases/physiology; Protein Folding; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Superoxide Dismutase/biosynthesis; Superoxide Dismutase/chemistry; Superoxide Dismutase/genetics; Superoxide Dismutase/metabolism; Thioredoxin-Disulfide Reductase/genetics; Thioredoxin-Disulfide Reductase/physiology; Xenopus laevis/genetics |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.