Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation.
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Issartel JP, Koronakis V, Hughes C
Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation.
Nature. 1991 Jun 27;351(6329):759-61.
- PubMed ID
- 2062368 [ View in PubMed]
- Abstract
Haemolysin secreted by pathogenic Escherichia coli binds to mammalian cell membranes, disrupting cellular activities and lysing cells by pore-formation. It is synthesized as nontoxic prohaemolysin (proHlyA), which is activated intracellularly by a mechanism dependent on the cosynthesized HlyC. Haemolysin is one of a family of membrane-targeted toxins, including the leukotoxins of Pasteurella and Actinobacillus and the bifunctional adenylate cyclase haemolysin of Bordetella pertussis, which require this protoxin activation 1-5. HlyC alone cannot activate proHlyA, but requires a cytosolic activating factor6. Here we report the cytosolic activating factor is identical to the acyl carrier protein and that activation to mature toxin is achieved by the transfer of a fatty acyl group from acyl carrier protein to proHlyA. Only acyl carrier protein, not acyl-CoA, can promote HlyC-directed proHlyA acylation, but a range of acyl groups are effective.