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. 1990 Apr;87(8):3107–3111. doi: 10.1073/pnas.87.8.3107

Solubilization and functional reconstitution of the protein-translocation enzymes of Escherichia coli.

A J Driessen 1, W Wickner 1
PMCID: PMC53843  PMID: 2139227

Abstract

The SecY protein and other membrane proteins of Escherichia coli were solubilized by mixed micelles of n-octyl beta-D-glucopyranoside, phospholipids, and glycerol. Proteoliposomes formed from this extract by detergent dialysis supported energy-dependent translocation and processing of pro-OmpA. Translocation required ATP, SecY, and SecA and was stimulated by a proton-motive force. These results provide an important assay for the isolation and identification of membrane components involved in protein translocation.

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