Ontology highlight
ABSTRACT:
SUBMITTER: Dalal K
PROVIDER: S-EPMC3306715 | biostudies-literature | 2012 Mar
REPOSITORIES: biostudies-literature
Dalal Kush K Chan Catherine S CS Sligar Stephen G SG Duong Franck F
Proceedings of the National Academy of Sciences of the United States of America 20120229 11
The SecA ATPase associates with the SecY complex to push preproteins across the bacterial membrane. Because a single SecY is sufficient to create the conducting channel, the function of SecY oligomerization remains unclear. Here, we have analyzed the translocation reaction using nanodiscs. We show that one SecY copy is sufficient to bind SecA and the preprotein, but only the SecY dimer together with acidic lipids supports the activation of the SecA translocation ATPase. In discs, the dimer is pr ...[more]