PMID:2062368
| Citation |
Issartel, JP, Koronakis, V and Hughes, C (1991) Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature 351:759-61 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1038/351759a0 |
| Keywords |
Acyl Carrier Protein/metabolism; Acyl Carrier Protein/pharmacology; Acylation; Acyltransferases/metabolism; Amino Acid Sequence; Bacterial Proteins/metabolism; Bacterial Toxins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Fatty Acids/metabolism; Hemolysin Proteins/metabolism; Molecular Sequence Data; Myristic Acid; Myristic Acids/metabolism; Palmitic Acid; Palmitic Acids/metabolism; Protein Precursors/metabolism; Protein Processing, Post-Translational |
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