Literature DB >> 21195693

Characterization of interactions between LPS transport proteins of the Lpt system.

Alexandra Bowyer1, Jason Baardsnes, Eunice Ajamian, Linhua Zhang, Miroslaw Cygler.   

Abstract

The lipopolysaccharide transport system (Lpt) in Gram-negative bacteria is responsible for transporting lipopolysaccharide (LPS) from the cytoplasmic surface of the inner membrane, where it is assembled, across the inner membrane, periplasm and outer membrane, to the surface where it is then inserted in the outer leaflet of the asymmetric lipid bilayer. The Lpt system consists of seven known LPS transport proteins (LptA-G) spanning from the cytoplasm to the cell surface. We have shown that the periplasmic component, LptA is able to form a stable complex with the inner membrane anchored LptC but does not interact with the outer membrane anchored LptE. This suggests that the LptC component of the LptBFGC complex may act as a dock for LptA, allowing it to bind LPS after it has been assembled at the inner membrane. That no interaction between LptA and LptE has been observed supports the theory that LptA binds LptD in the LptDE homodimeric complex at the outer membrane. Crown
Copyright © 2010. Published by Elsevier Inc. All rights reserved.

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Year:  2010        PMID: 21195693     DOI: 10.1016/j.bbrc.2010.12.121

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  18 in total

1.  Regulated assembly of the transenvelope protein complex required for lipopolysaccharide export.

Authors:  Elizaveta Freinkman; Suguru Okuda; Natividad Ruiz; Daniel Kahne
Journal:  Biochemistry       Date:  2012-06-08       Impact factor: 3.162

2.  Concentration-dependent oligomerization and oligomeric arrangement of LptA.

Authors:  Jacqueline A Merten; Kathryn M Schultz; Candice S Klug
Journal:  Protein Sci       Date:  2011-12-21       Impact factor: 6.725

3.  Disruption of LptA oligomerization and affinity of the LptA-LptC interaction.

Authors:  Kathryn M Schultz; Jimmy B Feix; Candice S Klug
Journal:  Protein Sci       Date:  2013-11       Impact factor: 6.725

4.  Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.

Authors:  Istvan Botos; Nadim Majdalani; Stephen J Mayclin; Jennifer Gehret McCarthy; Karl Lundquist; Damian Wojtowicz; Travis J Barnard; James C Gumbart; Susan K Buchanan
Journal:  Structure       Date:  2016-05-05       Impact factor: 5.006

5.  Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG.

Authors:  Qingshan Luo; Xu Yang; Shan Yu; Huigang Shi; Kun Wang; Le Xiao; Guangyu Zhu; Chuanqi Sun; Tingting Li; Dianfan Li; Xinzheng Zhang; Min Zhou; Yihua Huang
Journal:  Nat Struct Mol Biol       Date:  2017-04-10       Impact factor: 15.369

Review 6.  Insertion of proteins and lipopolysaccharide into the bacterial outer membrane.

Authors:  Istvan Botos; Nicholas Noinaj; Susan K Buchanan
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2017-08-05       Impact factor: 6.237

7.  Dominant negative lptE mutation that supports a role for LptE as a plug in the LptD barrel.

Authors:  Marcin Grabowicz; Jennifer Yeh; Thomas J Silhavy
Journal:  J Bacteriol       Date:  2013-01-11       Impact factor: 3.490

8.  The LptD chaperone LptE is not directly involved in lipopolysaccharide transport in Neisseria meningitidis.

Authors:  Martine P Bos; Jan Tommassen
Journal:  J Biol Chem       Date:  2011-06-24       Impact factor: 5.157

Review 9.  Lipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane.

Authors:  Janine M May; David J Sherman; Brent W Simpson; Natividad Ruiz; Daniel Kahne
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2015-10-05       Impact factor: 6.237

Review 10.  Lipopolysaccharide transport and assembly at the outer membrane: the PEZ model.

Authors:  Suguru Okuda; David J Sherman; Thomas J Silhavy; Natividad Ruiz; Daniel Kahne
Journal:  Nat Rev Microbiol       Date:  2016-03-30       Impact factor: 60.633

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