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Title: Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions

Journal Article · · Journal of Bacteriology; (United States)
OSTI ID:5864547
; ; ;  [1]
  1. Washington State Univ., Pullman (United States)

Alkaline phosphatase (PhoA) fusions to TonB amino acids 32, 60, 125, 207, 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.

OSTI ID:
5864547
Journal Information:
Journal of Bacteriology; (United States), Vol. 173:17; ISSN 0021-9193
Country of Publication:
United States
Language:
English