NDLI: Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli

Content Provider	PubMed Central
Author	Ruiz, Natividad Gronenberg, Luisa S. Kahne, Daniel Silhavy, Thomas J.
Abstract	The outer membrane (OM) of most Gram-negative bacteria contains lipopolysaccharide (LPS) in the outer leaflet. LPS, or endotoxin, is a molecule of important biological activities. In the host, LPS elicits a potent immune response, while in the bacterium, it plays a crucial role by establishing a barrier to limit entry of hydrophobic molecules. Before LPS is assembled at the OM, it must be synthesized at the inner membrane (IM) and transported across the aqueous periplasmic compartment. Much is known about the biosynthesis of LPS but, until recently, little was known about its transport and assembly. We applied a reductionist bioinformatic approach that takes advantage of the small size of the proteome of the Gram-negative endosymbiont Blochmannia floridanus to search for novel factors involved in OM biogenesis. This led to the discovery of two essential Escherichia coli IM proteins of unknown function, YjgP and YjgQ, which are required for the transport of LPS to the cell surface. We propose that these two proteins, which we have renamed LptF and LptG, respectively, are the missing transmembrane components of the ABC transporter that, together with LptB, functions to extract LPS from the IM en route to the OM.
Related Links	http://dx.doi.org/10.1073/pnas.0801196105
Ending Page	5542
Page Count	6
Starting Page	5537
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	105
Language	English
Publisher	National Academy of Sciences
Publisher Date	2008-04-08
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface

Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli.

Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli

Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane

Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli.

Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles.

The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel.

Translocation of phospholipids from the inner to the outer membrane of Escherichia coli.

Crosstalk between the lipopolysaccharide and phospholipid pathways during outer membrane biogenesis in Escherichia coli

Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli

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Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface

Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli.

Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli

Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane

Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli.

Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles.

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Translocation of phospholipids from the inner to the outer membrane of Escherichia coli.

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Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli