Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 6, Pages 4659-4669Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.175638
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Funding
- BBSRC [BB/F002343/1]
- Wellcome Trust [080705/Z/06/Z]
- [084452]
- [082140]
- Biotechnology and Biological Sciences Research Council [BB/F002343/1] Funding Source: researchfish
- BBSRC [BB/F002343/1] Funding Source: UKRI
- Wellcome Trust [080705/Z/06/Z] Funding Source: Wellcome Trust
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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-dependent association of SecYEG with pre-protein, active transport requires SecYEG dimers arranged in the back-to-back conformation. Molecular modeling of this dimeric structure, in conjunction with the new functional data, provides a rationale for the presence of both active and passive copies of SecYEG in the functional translocon.
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