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Science 10 December 1993:
Vol. 262. no. 5140, pp. 1744 - 1747
DOI: 10.1126/science.8259521
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Articles

Science, Vol 262, Issue 5140, 1744-1747
Copyright © 1993 by American Association for the Advancement of Science

articles

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

AI Derman, WA Prinz, D Belin, and J Beckwith

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.

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.


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