ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019
The lipid environment determines the activity of the Escherichia coli ammonium transporter AmtB.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 34 citations in OpenAlex.
- Investigating the Effect of Membrane Composition on the Selective Ammonium Transport of Escherichia coli AmtB Membrane Proteins.ACS applied engineering materials · 2025Article
- How sensor Amt-like proteins integrate ammonium signals.Science advances · 2024Article
- Article
- Ammonia-oxidizing bacteria and archaea exhibit differential nitrogen source preferences.Nature microbiology · 2024Article
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- Prokaryotic ammonium transporters: what has three decades of research revealed?Microbiology (Reading, England) · 2023Article
- Investigating the Lipid Selectivity of Membrane Proteins in Heterogeneous Nanodiscs.Analytical chemistry · 2022Article
- Article
- What have molecular simulations contributed to understanding of Gram-negative bacterial cell envelopes?Microbiology (Reading, England) · 2022Review
- Model architectures for bacterial membranes.Biophysical reviews · 2022Review
- Native-like membrane models of E. coli polar lipid extract shed light on the importance of lipid composition complexity.BMC biology · 2021Article
- Article
- Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae.Journal of molecular biology · 2020Article
- Measuring Remodeling of the Lipid Environment Surrounding Membrane Proteins with Lipid Exchange and Native Mass Spectrometry.Analytical chemistry · 2020Article
- A twin histidine motif is the core structure for high-affinity substrate selection in plant ammonium transporters.The Journal of biological chemistry · 2020Article
- Yeast filamentation signaling is connected to a specific substrate translocation mechanism of the Mep2 transceptor.PLoS genetics · 2020Article
- Functional Characterization of SLC Transporters Using Solid Supported Membranes.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- Computational Modeling of Realistic Cell Membranes.Chemical reviews · 2019Review
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5 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The movement of ammonium across biologic membranes is a fundamental process in all living organisms and is mediated by the ubiquitous ammonium transporter/methylammonium permease/rhesus protein (Amt/Mep/Rh) family of transporters. Recent structural analysis and coupled mass spectrometry studies have shown that the Escherichia coli ammonium transporter AmtB specifically binds 1-palmitoyl-2-oleoyl phosphatidylglycerol (POPG). Upon POPG binding, several residues of AmtB undergo a small conformational change, which stabilizes the protein against unfolding. However, no studies have so far been conducted, to our knowledge, to explore whether POPG binding to AmtB has functional consequences. Here, we used an in vitro experimental assay with purified components, together with molecular dynamics simulations, to characterize the relation between POPG binding and AmtB activity. We show that the AmtB activity is electrogenic. Our results indicate that the activity, at the molecular level, of Amt in archaebacteria and eubacteria may differ. We also show that POPG is an important cofactor for AmtB activity and that, in the absence of POPG, AmtB cannot complete the full translocation cycle. Furthermore, our simulations reveal previously undiscovered POPG binding sites on the intracellular side of the lipid bilayer between the AmtB subunits. Possible molecular mechanisms explaining the functional role of POPG are discussed.-Mirandela, G. D., Tamburrino, G., Hoskisson, P. A., Zachariae, U., Javelle, A. The lipid environment determines the activity of the Escherichia coli ammonium transporter AmtB.
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