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Scientific article
English

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

Contributors

Derman, A. I.; Prinz, W. A.; Belin, Dominique; Beckwith, J.

Published in

Science, vol. 262, no. 5140, p. 1744-1747

Publication date

1993

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/metabolism
  • Cysteine/metabolism
  • Cytoplasm/ enzymology
  • Disulfides/metabolism
  • Escherichia coli/ enzymology/genetics/growth & development
  • Genes, Bacterial
  • Mutation
  • Oxidation-Reduction
  • Protein Folding
  • Protein Sorting Signals
  • Recombinant Proteins/chemistry/metabolism
  • Thioredoxin-Disulfide Reductase/genetics/ metabolism
  • Urokinase-Type Plasminogen Activator/ chemistry/metabolism

UNIGE affiliation entities

Not a UNIGE publication

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.

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Article

Identifiers

Additional URL for this publication

http://www.jstor.org/stable/pdfplus/2885094.pdf

Journal ISSN

0036-8075
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1downloads

Technical informations

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27/08/2010 13:33:24

First validation

27/08/2010 13:33:24

Update

14/03/2023 16:02:04

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14/03/2023 16:02:04

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