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Significance Proteins embedded in biological membranes are important targets for therapeutic intervention. However, they tend to be far more challenging to deal with than soluble proteins. We have used the anticoagulant target VKORc1 to investigate membrane protein expression bottlenecks in the bacteriumEscherichia coli . When this poorly expressed enzyme is mutagenized or introduced to a library ofE. coli mutants, functional expression is achieved. This approach gave clues on why certain foreign membrane proteins fail to correctly assimilate inE. coli membranes including mis-matches in membrane protein assembly signals. We also identified key critical residues in two components of membrane protein assembly and quality control for rational manipulations to enhance functional expression. Finally, we demonstrate the high-throughput screening for potential anticoagulants using bacteria.

Altered Escherichia coli membrane protein assembly machinery allows proper membrane assembly of eukaryotic protein vitamin K epoxide reductase