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Originally published In Press as doi:10.1074/jbc.M206816200 on August 26, 2002

J. Biol. Chem., Vol. 277, Issue 45, 43512-43518, November 8, 2002
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Aminoacylation of the N-terminal Cysteine Is Essential for Lol-dependent Release of Lipoproteins from Membranes but Does Not Depend on Lipoprotein Sorting Signals*

Ayumu FukudaDagger , Shin-ichi MatsuyamaDagger , Takashi HaraDagger , Jiro Nakayama§, Hiromichi Nagasawa§, and Hajime TokudaDagger ||

From the Dagger  Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan and the § Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan

Lipoproteins are present in a wide variety of bacteria and are anchored to membranes through lipids attached to the N-terminal cysteine. The Lol system of Escherichia coli mediates the membrane-specific localization of lipoproteins. Aspartate at position 2 functions as a Lol avoidance signal and causes the retention of lipoproteins in the inner membrane, whereas lipoproteins having residues other than aspartate at position 2 are released from the inner membrane and localized to the outer membrane by the Lol system. Phospholipid:apolipoprotein transacylase, Lnt, catalyzes the last step of lipoprotein modification, converting apolipoprotein into mature lipoprotein. To reveal the importance of this aminoacylation for the Lol-dependent membrane localization, apolipoproteins were prepared by inhibiting lipoprotein maturation. Lnt was also purified and used to convert apolipoprotein into mature lipoprotein in vitro. The release of these lipoproteins was examined in proteoliposomes. We show here that the aminoacylation is essential for the Lol-dependent release of lipoproteins from membranes. Furthermore, lipoproteins with aspartate at position 2 were found to be aminoacylated both in vivo and in vitro, indicating that the lipoprotein-sorting signal does not affect lipid modification.

* This work was supported by grants from Core Research for Engineering, Science, and Technology (CREST) of the Japan Science and Technology Corporation and the Ministry of Education, Science, Sports and Culture of Japan (to H. T.).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.

Present address: Dept. of Bioscience and Bio/Technology, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan.

|| To whom correspondence should be addressed. Tel.: 81-3-5841-7830; Fax: 81-3-5841-8464; E-mail: htokuda@iam.u-tokyo.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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