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J Biol Chem, Vol. 275, Issue 4, 2472-2478, January 28, 2000
From the Department of Microbiology and the Groningen Biomolecular
Sciences and Biotechnology Institute, University of Groningen,
Kerklaan 30, 9751 NN Haren, The Netherlands
To determine the phospholipid requirement of the
preprotein translocase in vitro, the Escherichia
coli SecYEG complex was purified in a delipidated form using
the detergent dodecyl maltoside. SecYEG was reconstituted into
liposomes composed of defined synthetic phospholipids, and
proteoliposomes were analyzed for their preprotein translocation and
SecA translocation ATPase activity. The activity strictly required the
presence of anionic phospholipids, whereas the non-bilayer lipid
phosphatidylethanolamine was found stimulatory. The latter effect could
also be induced by dioleoylglycerol, a lipid that adopts a non-bilayer
conformation. Phosphatidylethanolamine derivatives that prefer the
bilayer state were unable to stimulate translocation. In the absence of
SecG, activity was reduced, but the phospholipid requirement was
unaltered. Remarkably, non-bilayer lipids were found essential for the
activity of the Bacillus subtilis SecYEG complex. Optimal
activity required a mixture of anionic and non-bilayer lipids at
concentrations that correspond to concentrations found in the natural membrane.
Non-bilayer Lipids Stimulate the Activity of the Reconstituted
Bacterial Protein Translocase*
*
This work was supported by a PIONIER grant of the
Netherlands Organization for Scientific Research (N.W.O.) and by CEC
Biotech Grants BIO2 CT 930254 and BIO4 CT 960097.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 31-50-3632164;
Fax: 31-50-3632154; E-mail: A.J.M.DRIESSEN@BIOL.RUG.NL.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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