Global Topology Analysis of the Escherichia coli Inner Membrane Proteome

Author:

Daley Daniel O.12,Rapp Mikaela12,Granseth Erik12,Melén Karin12,Drew David12,von Heijne Gunnar12

Affiliation:

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

2. Stockholm Bioinformatics Center, AlbaNova, 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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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