Article
Covalently dimerized SecA is functional in protein translocation.
The Journal of biological chemistry - 21 Oct 2005
de Keyzer Jeanine, van der Sluis Eli O, Spelbrink Robin E J, Nijstad Niels, de Kruijff Ben, Nouwen Nico, van der Does Chris, Driessen Arnold J M
Abstract excerpt
The ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli. SecA exists as a dimer in solution, but the exact oligomeric state of SecA during membrane binding and preprotein translocation is a topic of debate. To study the requirements of oligomeric changes in SecA during protein translocation, a non-dissociable SecA dimer was formed by...
Topics
- Adenosine Triphosphatases
- Bacterial Proteins
- Cell Membrane
- Cross-Linking Reagents
- Cysteine
- Cytoplasm
- Dimerization
- Disulfides
- Dose-Response Relationship, Drug
- Escherichia coli
- Kinetics
- Membrane Transport Proteins
- Mutation