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- Title
Membrane topology of MaIG, an inner membrane protein from the maltose transport system of <em>Escherichia coli</em>.
- Authors
Dassa, Elie; Muir, Susie
- Abstract
In <em>Escherichia coli</em>, the binding protein-dependent transport system for maltose and maltodextrins is composed of five proteins - LamB, MalE, MalF, MalG and MalK - located in the three layers of the bacterial envelope. Proteins MaiF and MaIG are hydrophobic inner membrane components mediating the energy-dependent translocation of substrates into the cytoplasm. In this paper, we analyse the topology of the MaIG protein by using methods based on the properties of fusions between <em>maIG</em> and <em>'phoA</em>, a truncated gene encoding alkaline phosphatase lacking its translation initiation and exportation signals. Fusions were obtained by using either phage λ TnphoA or by constructing <em>in vitro</em> fusions located randomly within the <em>maIG</em> gene. The deduced topological model suggests that MaIG spans the membrane six times and has its amino- and carboxy-termini in the cytoplasm. These results will be helpful for the interpretation of the phenotypes of mutants in <em>maIG</em>.
- Subjects
ESCHERICHIA coli; CARRIER proteins; BIOLOGICAL transport; MALTOSE; CELL membranes
- Publication
Molecular Microbiology, 1993, Vol 7, Issue 1, p29
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.1993.tb01094.x