Difference between revisions of "PMID:8503954"
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| + | !align=left align='left' bgcolor='#CCCCFF' |Citation | ||
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| + | '''Dailey, FE and Berg, HC''' (1993) Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. ''Proc. Natl. Acad. Sci. U.S.A.'' '''90''':1043-7 | ||
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| + | !align=left align='left' bgcolor='#CCCCFF' |Abstract | ||
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| + | 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. | ||
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| + | !align=left align='left' bgcolor='#CCCCFF' |Links | ||
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| + | [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8503954 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC45807 PMC45807] | ||
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| + | !align=left align='left' bgcolor='#CCCCFF' |Keywords | ||
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| + | Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Movement/physiology; Chromosome Mapping; Cystine/metabolism; Cystine/pharmacology; Disulfides/metabolism; Escherichia coli/genetics; Flagella/chemistry; Flagella/physiology; Flagella/ultrastructure; Isomerases/genetics; Isomerases/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Morphogenesis/drug effects; Morphogenesis/genetics; Mutagenesis; Oxidoreductases/genetics; Oxidoreductases/metabolism; Phenotype; Protein Disulfide-Isomerases; Protein Processing, Post-Translational | ||
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| + | ==Main Points of the Paper == | ||
| + | {{LitSignificance}} | ||
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| + | == Materials and Methods Used == | ||
| + | {{LitMaterials}} | ||
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| + | ==Phenotype Annotations== | ||
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| + | !|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status | ||
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| + | ==Notes== | ||
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| + | ==References== | ||
| + | {{RefHelp}} | ||
| + | <references/> | ||
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| + | [[Category:Publication]] | ||
Latest revision as of 20:17, 11 February 2019
| Citation |
Dailey, FE and Berg, HC (1993) Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 90:1043-7 |
|---|---|
| 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. |
| Links | |
| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cell Movement/physiology; Chromosome Mapping; Cystine/metabolism; Cystine/pharmacology; Disulfides/metabolism; Escherichia coli/genetics; Flagella/chemistry; Flagella/physiology; Flagella/ultrastructure; Isomerases/genetics; Isomerases/metabolism; Membrane Proteins/genetics; Membrane Proteins/metabolism; Morphogenesis/drug effects; Morphogenesis/genetics; Mutagenesis; Oxidoreductases/genetics; Oxidoreductases/metabolism; Phenotype; Protein Disulfide-Isomerases; Protein Processing, Post-Translational |
Main Points of the Paper
Please summarize the main points of the paper.
Materials and Methods Used
Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).
Phenotype Annotations
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| Phenotype of | Taxon Information | Genotype Information (if known) | Condition Information | OMP ID | OMP Term Name | ECO ID | ECO Term Name | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|
Notes
References
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