TY - JOUR
T1 - Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions
AU - Roof, S. K.
AU - Allard, J. D.
AU - Bertrand, K. P.
AU - Postle, K.
PY - 1991
Y1 - 1991
N2 - 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.
AB - 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.
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U2 - 10.1128/jb.173.17.5554-5557.1991
DO - 10.1128/jb.173.17.5554-5557.1991
M3 - Comment/debate
C2 - 1885532
AN - SCOPUS:0025992835
SN - 0021-9193
VL - 173
SP - 5554
EP - 5557
JO - Journal of bacteriology
JF - Journal of bacteriology
IS - 17
ER -