Article
Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.
The Journal of biological chemistry - 25 Dec 1991
Cabelli R J, Dolan K M, Qian L P, Oliver D B
Abstract excerpt
The subcellular localization of SecA, a protein essential for the catalysis of general protein export, was studied to better understand its state(s) and function(s) within Escherichia coli cells. In a wild-type strain approximately half of the cellular SecA content was found to be associated with the inner membrane, while the remainder was soluble. Association of SecA protein with the inner membrane required the...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Bacterial Proteins
- Base Sequence
- Blotting, Western
- Cardiolipins
- Cell Fractionation
- Cell Membrane
- Chromatography, Gel
- Electrophoresis, Polyacrylamide Gel