Abstract
If DNA is the information of life, then proteins are the machines of life--but they must be assembled and correctly folded to function. A key step in the protein-folding pathway is the introduction of disulphide bonds between cysteine residues in a process called oxidative protein folding. Many bacteria use an oxidative protein-folding machinery to assemble proteins that are essential for cell integrity and to produce virulence factors. Although our current knowledge of this machinery stems largely from Escherichia coli K-12, this view must now be adjusted to encompass the wider range of disulphide catalytic systems present in bacteria.
MeSH terms
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Bacteria / enzymology
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Bacteria / pathogenicity*
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Bacterial Proteins / chemistry
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Bacterial Proteins / physiology*
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Computational Biology
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Disulfides / metabolism*
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Escherichia coli K12 / enzymology
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Escherichia coli K12 / pathogenicity*
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / physiology*
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Membrane Proteins / chemistry
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Membrane Proteins / physiology*
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Oxidation-Reduction
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Phylogeny
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Protein Disulfide-Isomerases / chemistry
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Protein Disulfide-Isomerases / physiology*
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Protein Folding
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Protein Stability
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Virulence
Substances
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Bacterial Proteins
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Disulfides
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DsbB protein, Bacteria
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Escherichia coli Proteins
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Membrane Proteins
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Protein Disulfide-Isomerases
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dsbA protein, E coli