Abstract:
:The multimeric membrane protein complex translocase mediates the transport of preproteins across and integration of membrane proteins into the inner membrane of Escherichia coli. The translocase consists of the peripheral membrane-associated ATPase SecA and the heterotrimeric channel-forming complex consisting of SecY, SecE and SecG. We have investigated the quaternary structure of the SecYEG complex in proteoliposomes. Fluorescence resonance energy transfer demonstrates that SecYEG forms oligomers when embedded in the membrane. Freeze-fracture techniques were used to examine the oligomeric composition under non-translocating and translocating conditions. Our data show that membrane-embedded SecYEG exists in a concentration-dependent equilibrium between monomers, dimers and tetramers, and that dynamic exchange of subunits between oligomers can occur. Remarkably, the formation of dimers and tetramers in the lipid environment is stimulated significantly by membrane insertion of SecA and by the interaction with translocation ligands SecA, preprotein and ATP, suggesting that the active translocation channel consists of multiple SecYEG complexes.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Scheuring J,Braun N,Nothdurft L,Stumpf M,Veenendaal AK,Kol S,van der Does C,Driessen AJ,Weinkauf Sdoi
10.1016/j.jmb.2005.09.058keywords:
subject
Has Abstractpub_date
2005-11-25 00:00:00pages
258-71issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(05)01134-4journal_volume
354pub_type
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