Ontology highlight
ABSTRACT:
SUBMITTER: Deville K
PROVIDER: S-EPMC3039378 | biostudies-literature | 2011 Feb
REPOSITORIES: biostudies-literature
Deville Karine K Gold Vicki A M VA Robson Alice A Whitehouse Sarah S Sessions Richard B RB Baldwin Stephen A SA Radford Sheena E SE Collinson Ian I
The Journal of biological chemistry 20101105 6
Protein secretion in bacteria is driven through the ubiquitous SecYEG complex by the ATPase SecA. The structure of SecYEG alone or as a complex with SecA in detergent reveal a monomeric heterotrimer enclosing a central protein channel, yet in membranes it is dimeric. We have addressed the functional significance of the oligomeric status of SecYEG in protein translocation using single molecule and ensemble methods. The results show that while monomers are sufficient for the SecA- and ATP-dependen ...[more]