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Science. 2005 May 27;308(5726):1321-3.

Global topology analysis of the Escherichia coli inner membrane proteome.

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  • 1Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.

Abstract

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.

PMID:
15919996
[PubMed - indexed for MEDLINE]
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