The oligomeric state and arrangement of the active bacterial translocon

K Deville, VAM Gold, A Robson, S Whitehouse, RB Sessions, SA Baldwin, SE Radford, I Collinson

Research output: Contribution to journalArticle (Academic Journal)peer-review

51 Citations (Scopus)


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.
Translated title of the contributionThe oligomeric state and arrangement of the active bacterial translocon
Original languageEnglish
Pages (from-to)4659 - 4669
Number of pages11
JournalJournal of Biological Chemistry
Volume286 (6)
Publication statusPublished - Dec 2011


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