ArticleThe Journal of biological chemistry2016
Lipid Requirements for the Enzymatic Activity of MraY Translocases and in Vitro Reconstitution of the Lipid II Synthesis Pathway.
Article in The Journal of biological chemistry, 2016. 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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31 citing papers in PubMed, 64 citations in OpenAlex.
- Membrane Composition Reshapes the Folding Landscape of a pH-Responsive Peptide.The journal of physical chemistry letters · 2026Article
- Lipopeptide antibiotics disrupt interactions of undecaprenyl phosphate with UptA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cryo-EM structure of cell-free synthesized human histamine 2 receptor/GNature communications · 2024Article
- The mechanism of the phage-encoded protein antibiotic from ΦX174.Science (New York, N.Y.) · 2023Article
- Too Much or Not Enough: The Role ofmBio · 2023Article
- Minimal Out-of-Equilibrium Metabolism for Synthetic Cells: A Membrane Perspective.ACS synthetic biology · 2023Review
- The antibacterial activity of berberine againstFrontiers in microbiology · 2023Article
- Reconstitution of prenyltransferase activity on nanodiscs by components of the rubber synthesis machinery of the Para rubber tree and guayule.Scientific reports · 2022Article
- How lipids affect the energetics of co-translational alpha helical membrane protein folding.Biochemical Society transactions · 2022Review
- Transfer mechanism of cell-free synthesized membrane proteins into mammalian cells.Frontiers in bioengineering and biotechnology · 2022Article
- Cell-Free Synthesis Strategies to Probe Co-translational Folding of Proteins Within Lipid Membranes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- β-Lactams against the Fortress of the Gram-PositiveChemical reviews · 2021Review
- Article
- Cell-free expression tools to study co-translational folding of alpha helical membrane transporters.Scientific reports · 2020Article
- Co-Translational Protein Folding in Lipid Membranes.Trends in biochemical sciences · 2019Review
- Hydrogen-deuterium exchange mass spectrometry of membrane proteins in lipid nanodiscs.Chemistry and physics of lipids · 2019Review
- Functionality of membrane proteins overexpressed and purified from E. coli is highly dependent upon the strain.Scientific reports · 2019Article
- Structure and activity of lipid bilayer within a membrane-protein transporter.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Aminoribosylated Analogues of Muraymycin Nucleoside Antibiotics.Molecules (Basel, Switzerland) · 2018Article
- Analogues of Muraymycin Nucleoside Antibiotics with Epimeric Uridine-Derived Core Structures.Molecules (Basel, Switzerland) · 2018Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Screening of new compounds directed against key protein targets must continually keep pace with emerging antibiotic resistances. Although periplasmic enzymes of bacterial cell wall biosynthesis have been among the first drug targets, compounds directed against the membrane-integrated catalysts are hardly available. A promising future target is the integral membrane protein MraY catalyzing the first membrane associated step within the cytoplasmic pathway of bacterial peptidoglycan biosynthesis. However, the expression of most MraY homologues in cellular expression systems is challenging and limits biochemical analysis. We report the efficient production of MraY homologues from various human pathogens by synthetic cell-free expression approaches and their subsequent characterization. MraY homologues originating from Bordetella pertussis, Helicobacter pylori, Chlamydia pneumoniae, Borrelia burgdorferi, and Escherichia coli as well as Bacillus subtilis were co-translationally solubilized using either detergent micelles or preformed nanodiscs assembled with defined membranes. All MraY enzymes originating from Gram-negative bacteria were sensitive to detergents and required nanodiscs containing negatively charged lipids for obtaining a stable and functionally folded conformation. In contrast, the Gram-positive B. subtilis MraY not only tolerates detergent but is also less specific for its lipid environment. The MraY·nanodisc complexes were able to reconstitute a complete in vitro lipid I and lipid II forming pipeline in combination with the cell-free expressed soluble enzymes MurA-F and with the membrane-associated protein MurG. As a proof of principle for future screening platforms, we demonstrate the inhibition of the in vitro lipid II biosynthesis with the specific inhibitors fosfomycin, feglymycin, and tunicamycin.
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