Scientific Article
previous document  unige:11045  next document
add to browser collection
Title

Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli

Authors
Derman, A. I.
Prinz, W. A.
Beckwith, J.
Published in Science. 1993, vol. 262, no. 5140, p. 1744-1747
Abstract Disulfide bonds are rarely found in cytoplasmic proteins. Mutations were selected for in Escherichia coli that allow disulfide bond formation in the cytoplasm. In the presence of these mutations, export-defective versions of alkaline phosphatase and mouse urokinase were able to fold into their enzymatically active conformations in the cytoplasm because their disulfide bonds were formed. The mutations were mapped to the gene for thioredoxin reductase and diminish or eliminate the activity of this enzyme. Thioredoxin itself was found to be unnecessary for this disulfide bond formation. Thioredoxin reductase, but not thioredoxin, is thus implicated in keeping cysteines reduced in cytoplasmic proteins.
Keywords Alkaline Phosphatase/ chemistry/metabolismCysteine/metabolismCytoplasm/ enzymologyDisulfides/metabolismEscherichia coli/ enzymology/genetics/growth & developmentGenes, BacterialMutationOxidation-ReductionProtein FoldingProtein Sorting SignalsRecombinant Proteins/chemistry/metabolismThioredoxin-Disulfide Reductase/genetics/ metabolismUrokinase-Type Plasminogen Activator/ chemistry/metabolism
Identifiers
PMID: 8259521
Full text
Article - document accessible for UNIGE members only Limited access to UNIGE
Other version: http://www.jstor.org/stable/pdfplus/2885094.pdf
Citation
(ISO format)
DERMAN, A. I. et al. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. In: Science, 1993, vol. 262, n° 5140, p. 1744-1747. https://archive-ouverte.unige.ch/unige:11045

188 hits

0 download

Update

Deposited on : 2010-08-27

Export document
Format :
Citation style :