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/debatepeer-review

72 Scopus citations

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 - 1991

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions'. Together they form a unique fingerprint.

Cite this