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A new ABC transporter mediating the detachment of lipid-modified proteins from membranes

Nature Cell Biology volume 2, pages 212–218 (2000)Cite this article

Abstract

Lipoproteins in Escherichia coli are anchored to the periplasmic side of either the inner or the outer membrane by a lipid moiety that is covalently attached to the amino-terminal cysteine residue. Membrane specificity depends on a sorting signal at position 2 of the lipoprotein. Lipoproteins directed to the outer membrane are released from the inner membrane in an ATP-dependent manner through the formation of a complex with LolA, a periplasmic chaperone. However, the ATPase involved in this reaction has not been identified. Here we show, using reconstituted proteoliposomes, that a new complex, LolCDE, belonging to the ATP-binding cassette (ABC) transporter family, catalyses the release of lipoproteins in LolA- and sorting-signal-dependent manners. The LolCDE complex differs mechanistically from all other ABC transporters as it is not involved in the transmembrane transport of substrates. This new mechanism is evolutionarily conserved in other Gram-negative bacteria.

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Figure 1: Reconstitution of the lipoprotein-releasing apparatus into proteoliposomes.
Figure 2: Amplification of the lipoprotein-releasing apparatus.
Figure 3: LolD belongs to the ABC transporter family and is essential for lipoprotein release.
Figure 4: LolCDE catalyses the release of lipoproteins from the outer leaflet of the lipid bilayer.
Figure 5: LolD homologues in Gram-negative bacteria.
Figure 6: LolC and LolE homologues in Gram-negative bacteria.
Figure 7: The sorting and outer-membrane localization of E. coli lipoproteins is mediated by Lol factors.

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Acknowledgements

We thank M. Wachi for E. coli DLP79-22 and R. Ishihara for secretarial support. The unfinished sequence data were provided by the Sanger center (Sty, Ype and Bpe), the University of Oklahoma (Aac and Ngo), the Institute of Genomic Research (Vch, Spu and Nme), the University of Washington Genome center and PathoGenesis Corporation (Pae), the University of Minnesota (Pmu) and the Washington University Genome Sequencing center (Kpn). This work was supported by CREST of the Japan Science and Technology Corporation, and grants from the Ministry of Education, Science, Sport and Culture of Japan to H.T.

Correspondence and requests for materials should be addressed to H.T.

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  1. Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan

    Toshiharu Yakushi, Kazuhiro Masuda, Shin-ichiro Narita, Shin-ichi Matsuyama & Hajime Tokuda

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  1. Toshiharu Yakushi
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  2. Kazuhiro Masuda
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  5. Hajime Tokuda
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Correspondence to Hajime Tokuda.

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Yakushi, T., Masuda, K., Narita, Si. et al. A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat Cell Biol 2, 212–218 (2000). https://doi.org/10.1038/35008635

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