Title: Global topology analysis of the Escherichia coli inner membrane proteome. | Journal: Science (New York, N.Y.). 2005 May;308(5726):1321-3 | Authors: Daley DO, Rapp M, Granseth E, Melén K, Drew D, von Heijne G. | 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. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/15919996 |
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