Journal
MICROBIAL PATHOGENESIS
Volume 44, Issue 2, Pages 151-158Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.micpath.2007.09.001
Keywords
Type Ill secretion system; Secretin; Disulfide bond formation; EPEC
Categories
Funding
- Grant-in-Aids for Scientific Research (C) [17590398, 18590435]
- Grant-in-Aids for Scientific Research for Young Scientists (B) [17790292]
- 21st Century COE Research Grant from the Japanese Ministry of Education, Culture, Sports, Sciences, and Technology. Support
- Kitasato University Research Grant for Young Researchers
- Grants-in-Aid for Scientific Research [17790292, 17590398, 18590435] Funding Source: KAKEN
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The formation of disulfide bond is essential for the folding, activity, and stability of many secreted proteins of Gram-negative bacteria. The disulfide oxidoreductase, DsbA, introduces disulfide bonds into exported proteins from the cytoplasm. In pathogenic bacteria, DsbA is required to process virulence determinants for their folding and assembly. In this study, we investigated the role of DsbA in enteropathogenic Escherichia coli. Here, we show that the DsbA is required for stable expression of outer membrane secretin EscC. DsbA has no effect oil LEE transcription as measured with LEE-lacZ fusions. Replacement of either cysteine residue 136 or 155 of EscC with a serine resulted in reduced level of EscC, similar to the effect of the dsbA mutation. These results demonstrate the role of DsbA ill assembly of the type Ill secretion apparatus. (C) 2007 Elsevier Ltd. All rights reserved.
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