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ReportsGlobal Topology Analysis of the Escherichia coli Inner Membrane Proteome
The protein complement of cellular membranes is notoriously resistant to standard proteomic analysis and structural studies. As a result, membrane proteomes remain ill-defined. Here, we report a global topology analysis of the Escherichia coli inner membrane proteome. Using C-terminal tagging with the alkaline phosphatase and green fluorescent protein, we established the periplasmic or cytoplasmic locations of the C termini for 601 inner membrane proteins. By constraining a topology prediction algorithm with this data, we derived high-quality topology models for the 601 proteins, providing a firm foundation for future functional studies of this and other membrane proteomes. We also estimated the overexpression potential for 397 green fluorescent protein fusions; the results suggest that a large fraction of all inner membrane proteins can be produced in sufficient quantities for biochemical and structural work.
1 Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden. * These authors contributed equally to this work.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)
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