The oligomeric distribution of SecYEG is altered by SecA and translocation ligands.

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 Biol

authors

Scheuring J,Braun N,Nothdurft L,Stumpf M,Veenendaal AK,Kol S,van der Does C,Driessen AJ,Weinkauf S

doi

10.1016/j.jmb.2005.09.058

keywords:

subject

Has Abstract

pub_date

2005-11-25 00:00:00

pages

258-71

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)01134-4

journal_volume

354

pub_type

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