Abstract
An Escherichia coli K-12 mutant, isolated on the basis of its inability to catalyze formate-dependent nitrite reduction, was characterized. The mutant was defective in the synthesis of all known c-type cytochromes during anaerobic growth. The mutation was localized by conjugation, transduction, and Southern blotting experiments to the dsbA gene at minute 87 on the E. coli chromosome and was complemented by the wild-type allele. Both DsbA and the recently described DipZ protein were shown to be essential for cytochrome c synthesis, suggesting that they act sequentially in a pathway for cytochrome c assembly in the E. coli periplasm.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / physiology
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Chromosome Mapping
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Cytochrome c Group / biosynthesis*
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli Proteins*
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Formates
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Genes, Bacterial / genetics
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Isomerases / genetics
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Isomerases / physiology*
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Membrane Proteins / physiology
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Mutation
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Nitrites / metabolism*
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Oxidation-Reduction
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Oxidoreductases
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Protein Disulfide-Isomerases
Substances
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Bacterial Proteins
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Cytochrome c Group
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Escherichia coli Proteins
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Formates
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Membrane Proteins
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Nitrites
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formic acid
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Oxidoreductases
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DsbD electron transport protein, E coli
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Isomerases
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Protein Disulfide-Isomerases