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.
CITATION STYLE
Heras, B., Shouldice, S. R., Totsika, M., Scanlon, M. J., Schembri, M. A., & Martin, J. L. (2009). DSB proteins and bacterial pathogenicity. Nature Reviews Microbiology. https://doi.org/10.1038/nrmicro2087
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