| Literature DB >> 1885532 |
S K Roof1, J D Allard, K P Bertrand, K Postle.
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.Entities:
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Year: 1991 PMID: 1885532 PMCID: PMC208271 DOI: 10.1128/jb.173.17.5554-5557.1991
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490