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PMID: 8503954 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 3 ·1993-02-01 ·Pages 1043-7

Dailey FE, Berg HC

Abstract

We report the isolation and characterization of Escherichia coli mutants (dsbB) that fail to assemble functional flagella unless cystine is present. Flagellar basal bodies obtained from these mutants are missing the L and P rings. This defect in assembly appears to result from an inability to form a disulfide bond in the P-ring protein (FlgI). Cystine suppresses this defect in dsbB strains. We also show that dsbA strains [Bardwell, J. C. A., McGovern, K. & Beckwith, J. (1991) Cell 67, 581-589] fail to assemble P rings, apparently from a similar failure in disulfide bond formation. However, cystine does not completely suppress this defect in dsbA strains. Thus, disulfide bond formation in FlgI is essential for assembly. DsbA likely puts in that bond directly, whereas the DsbB product(s) play a role in oxidizing DsbA, so that it can be active.

MeSH Terms
Bacterial Proteins/genetics,metabolism Cell Movement/physiology Chromosome Mapping Cystine/metabolism,pharmacology Disulfides/metabolism Escherichia coli/genetics Flagella/chemistry,physiology,ultrastructure Isomerases/genetics,metabolism Membrane Proteins/genetics,metabolism Morphogenesis/drug effects,genetics Mutagenesis Oxidoreductases/genetics,metabolism Phenotype Protein Disulfide-Isomerases Protein Processing, Post-Translational
Chemicals
Bacterial Proteins Disulfides DsbB protein, Bacteria Membrane Proteins flgI protein, Bacteria Cystine Oxidoreductases Isomerases Protein Disulfide-Isomerases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Dailey F E
Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.
Berg H C
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.90.3.1043
Published
1993-02-01
Pages
1043-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC45807
Subset
IM
Grants
NIAID NIH HHS · AI16478 · United States
External Links
PubMed source DOI: 10.1073/pnas.90.3.1043 PMC Full Text View journal details
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