DsbC Activation by the N-terminal Domain of DsbD

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2001 Aug 9

PMID 11493705

Citations 15

Authors

D Goldstone

P W Haebel

F KATZEN

M W Bader

J C Bardwell

J Beckwith

P Metcalf

Affiliations

Soon will be listed here.

Abstract

The correct formation of disulfide bonds in the periplasm of Escherichia coli involves Dsb proteins, including two related periplasmic disulfide-bond isomerases, DsbC and DsbG. DsbD is a membrane protein required to maintain the functional oxidation state of DsbC and DsbG. In this work, purified proteins were used to investigate the interaction between DsbD and DsbC. A 131-residue N-terminal fragment of DsbD (DsbDalpha) was expressed and purified and shown to form a functional folded domain. Gel filtration results indicate that DsbDalpha is monomeric. DsbDalpha was shown to interact directly with and to reduce the DsbC dimer, thus increasing the isomerase activity of DsbC. The DsbC-DsbDalpha complex was characterized, and formation of the complex was shown to require the N-terminal dimerization domain of DsbC. These results demonstrate that DsbD interacts directly with full-length DsbC and imply that no other periplasmic components are required to maintain DsbC in the functional reduced state.

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