In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 98, No. 17 ( 2001-08-14), p. 9551-9556
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 (DsbDα) was expressed and purified and shown to form a functional folded domain. Gel filtration results indicate that
DsbDα is monomeric. DsbDα was shown to interact directly with and to reduce the DsbC dimer, thus increasing the isomerase activity of
DsbC. The DsbC–DsbDα 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.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.171315498
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
2001
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
