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

S. K. Roof, J. D. Allard, K. P. Bertrand, K. Postle

Research output: Contribution to journalComment/debate

70 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)5554-5557
Number of pages4
JournalJournal of bacteriology
Volume173
Issue number17
DOIs
StatePublished - Jan 1 1991

Fingerprint

Phosphoric Monoester Hydrolases
Cell Membrane
Escherichia coli
Amino Acids
Periplasm
Membranes
Phosphoprotein Phosphatases
Alkaline Phosphatase
Proteins

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

Roof, S. K. ; Allard, J. D. ; Bertrand, K. P. ; Postle, K. / Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions. In: Journal of bacteriology. 1991 ; Vol. 173, No. 17. pp. 5554-5557.
@article{b9f218c085704779bacb6a5490e1658b,
title = "Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions",
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.",
author = "Roof, {S. K.} and Allard, {J. D.} and Bertrand, {K. P.} and K. Postle",
year = "1991",
month = "1",
day = "1",
doi = "10.1128/jb.173.17.5554-5557.1991",
language = "English (US)",
volume = "173",
pages = "5554--5557",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "17",

}

Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions. / Roof, S. K.; Allard, J. D.; Bertrand, K. P.; Postle, K.

In: Journal of bacteriology, Vol. 173, No. 17, 01.01.1991, p. 5554-5557.

Research output: Contribution to journalComment/debate

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 - 1991/1/1

Y1 - 1991/1/1

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.

UR - http://www.scopus.com/inward/record.url?scp=0025992835&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025992835&partnerID=8YFLogxK

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

VL - 173

SP - 5554

EP - 5557

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 17

ER -