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Analysis of the topology of the cytochrome d terminal oxidase complex of Escherichia coli by alkaline phosphatase fusions
Author(s) -
Newton G.,
Yun C.H.,
Gennis R. B.
Publication year - 1991
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1991.tb02097.x
Subject(s) - biology , escherichia coli , alkaline phosphatase , cytochrome , biochemistry , cytochrome c oxidase , phosphatase , gene , microbiology and biotechnology , enzyme
Summary 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.