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Papers In Press, published online ahead of print January 10, 2005
Department of Microbiology, Harvard Medical School, Boston, MA 02115
Corresponding Author: jbeckwith{at}hms.harvard.edu
The formation of protein disulfide bonds in the E. coli periplasm by the enzyme DsbA is an inaccurate process. Many eukaryotic proteins with non-consecutive disulfide bonds expressed in E. coli require an additional protein for proper folding, the disulfide bond isomerase DsbC. Here we report studies on a native E. coli periplasmic acid phosphatase, phytase (AppA), which contains three consecutive and one non-consecutive disulfide bonds. We show that AppA requires DsbC for its folding. However, the activity of an AppA mutant lacking its non-consecutive disulfide bond is DsbC-independent. An AppA homolog, Agp, a periplasmic acid phosphatase with similar structure, lacks the non-consecutive disulfide bond, but has the three consecutive disulfide bonds found in AppA. The consecutively disulfide-bonded Agp is not dependent on DsbC, but is rendered dependent by the engineering into it of AppA’s conserved non-consecutive disulfide bond. Taken together, these results provide support for the proposal that proteins with non-consecutive disulfide bonds require DsbC for full activity and that disulfide bonds are formed predominantly during translocation across the cytoplasmic membrane.
J. Biol. Chem, 10.1074/jbc.M411774200
Submitted on October 18, 2004
Revised on January 10, 2005
Accepted on January 10, 2005
The non-consecutive disulfide bond of Echerichia coli phytase (AppA) renders it dependent on the protein disulfide isomerase, DsbC
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