ArticleThe Biochemical journal2010
The reconstituted Escherichia coli MsbA protein displays lipid flippase activity.
Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 64 citations in OpenAlex.
- Klebsiella pneumoniae employs a type VI secretion system to overcome microbiota-mediated colonization resistance.Nature communications · 2025Article
- Reconstitution of ATP-dependent lipid transporters: gaining insight into molecular characteristics, regulation, and mechanisms.Bioscience reports · 2023Review
- The Alternating Access Mechanism in Mammalian Multidrug Resistance Transporters and Their Bacterial Homologs.Membranes · 2023Article
- Biosensor for Multimodal Characterization of an Essential ABC Transporter for Next-Generation Antibiotic Research.ACS applied materials & interfaces · 2023Article
- Localized cardiolipin synthesis is required for the assembly of MreB during the polarized cell division of Chlamydia trachomatis.PLoS pathogens · 2022Article
- Checkpoints That Regulate Balanced Biosynthesis of Lipopolysaccharide and Its Essentiality inInternational journal of molecular sciences · 2021Review
- Energetics of lipid transport by the ABC transporter MsbA is lipid dependent.Communications biology · 2021Article
- The Role of the Membrane in Transporter Folding and Activity.Journal of molecular biology · 2021Review
- Impact of spent engine oil contamination on the antibiotic resistome of a tropical agricultural soil.Ecotoxicology (London, England) · 2021Article
- Cardiolipin aids in lipopolysaccharide transport to the gram-negative outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Enzymatic trans-bilayer lipid transport: Mechanisms, efficiencies, slippage, and membrane curvature.Biochimica et biophysica acta. Biomembranes · 2021Review
- Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system.Nature microbiology · 2019Article
- Structural Insights into the Lipid A Transport Pathway in MsbA.Structure (London, England : 1993) · 2019Article
- Functional Reconstitution of HlyB, a Type I Secretion ABC Transporter, in Saposin-A Nanoparticles.Scientific reports · 2019Article
- Probing membrane protein properties using droplet interface bilayers.Experimental biology and medicine (Maywood, N.J.) · 2019Article
- Function and Biogenesis of Lipopolysaccharides.EcoSal Plus · 2018Review
- The lipopolysaccharide transport (Lpt) machinery: A nonconventional transporter for lipopolysaccharide assembly at the outer membrane of Gram-negative bacteria.The Journal of biological chemistry · 2017Review
- Structural basis for lipopolysaccharide extraction by ABC transporter LptBNature structural & molecular biology · 2017Article
- Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017Review
- Comparative Analyses of Transport Proteins Encoded within the Genomes of Bdellovibrio bacteriovorus HD100 and Bdellovibrio exovorus JSS.Journal of molecular microbiology and biotechnology · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The MsbA protein is an essential ABC (ATP-binding-cassette) superfamily member in Gram-negative bacteria. This 65 kDa membrane protein is thought to function as a homodimeric ATP-dependent lipid translocase or flippase that transports lipid A from the inner to the outer leaflet of the cytoplasmic membrane. We have previously shown that purified MsbA from Escherichia coli displays high ATPase activity, and binds to lipids and lipid-like molecules, including lipid A, with affinity in the low micromolar range. Bacterial membrane vesicles isolated from E. coli overexpressing His6-tagged MsbA displayed ATP-dependent translocation of several fluorescently NBD (7-nitrobenz-2-oxa-1,3-diazole)-labelled phospholipid species. Purified MsbA was reconstituted into proteoliposomes of E. coli lipid and its ability to translocate NBD-labelled lipid derivatives was characterized. In this system, the protein displayed maximal lipid flippase activity of 7.7 nmol of lipid translocated per mg of protein over a 20 min period for an acyl chain-labelled PE (phosphatidylethanolamine) derivative. The protein showed the highest rates of flippase activity when reconstituted into an E. coli lipid mixture. Substantial flippase activity was also observed for a variety of other NBD-labelled phospholipids and glycolipids, including molecules labelled on either the headgroup or the acyl chain. Lipid flippase activity required ATP hydrolysis, and was dependent on the concentration of ATP and NBD-lipid. Translocation of NBD-PE was inhibited by the presence of the putative physiological substrate lipid A. The present paper represents the first report of a direct measurement of the lipid flippase activity of purified MsbA in a reconstituted system.
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