Abstract
Alkaline phosphatase (PhoA) fusions to TonB amino acids 32, 60, 125, 207, and 239 (the carboxy terminus) all showed high PhoA activity; a PhoA fusion to TonB amino acid 12 was inactive. The full-length TonB-PhoA fusion protein was associated with the cytoplasmic membrane and retained partial TonB function. These results support a model in which TonB is anchored in the cytoplasmic membrane by its hydrophobic amino terminus, with the remainder of the protein, including its hydrophobic carboxy terminus, extending into the periplasm.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5554-5557 |
| Number of pages | 4 |
| Journal | Journal of bacteriology |
| Volume | 173 |
| Issue number | 17 |
| DOIs |
|
| State | Published - 1991 |
All Science Journal Classification (ASJC) codes
- Microbiology
- Molecular Biology
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