Solubilization and functional reconstitution of the protein-translocation enzymes of Escherichia coli.
basic_science · Level V
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- Record sourced from PubMed, PMID 2139227.
- Also identified by PMC identifier 53843.
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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.
Medical subject headings
- Bacterial Proteins
- Cell Membrane
- Escherichia coli
- Escherichia coli Proteins
- Membrane Proteins
- Proton-Translocating ATPases