Analysis of the topology of the cytochrome d terminal oxidase complex of Escherichia coli by alkaline phosphatase fusions

G. Newton, C. ‐H Yun, R. B. Gennis

Research output: Contribution to journalArticlepeer-review

Abstract

The cytochrome d complex of Escherichia coli is a heterodimer located in the bacterial cytoplasmic membrane, where it functions as a terminal oxidase of the aerobic respiratory chain. The topology of each of the two subunits of the cytochrome d complex was analysed by the genetic method involving alkaline phosphatase gene fusions. These fusions were generated by both an in vivo method using the transposon TnphoA and an in vitro method of construction. A total of 48 unique fusions were isolated and the whole‐cell alkaline phosphatase‐specific activities were determined. Data from these fusions, in combination with information from other studies, provide the basis for two‐dimensional models for each of the two subunits, defining the way in which the subunits fold in the inner membrane of E. coli.

Original languageEnglish (US)
Pages (from-to)2511-2518
Number of pages8
JournalMolecular Microbiology
Volume5
Issue number10
DOIs
StatePublished - Oct 1991

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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