ArticleThe Journal of biological chemistry2013
Physicochemical factors controlling the activity and energy coupling of an ionic strength-gated ATP-binding cassette (ABC) transporter.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Exploring lipid diversity and minimalism to define membrane requirements for synthetic cells.FEBS letters · 2025Review
- Membrane-embedded CdaA is required for efficient synthesis of second messenger cyclic di-AMP.Communications biology · 2024Article
- Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024Review
- The substrate-binding domains of the osmoregulatory ABC importer OpuA transiently interact.eLife · 2024Article
- Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions.Chemical reviews · 2024Review
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- Structural basis for heme detoxification by an ATP-binding cassette-type efflux pump in gram-positive pathogenic bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Heterodimer Formation of the Homodimeric ABC Transporter OpuA.International journal of molecular sciences · 2021Article
- In silico method for selecting residue pairs for single-molecule microscopy and spectroscopy.Scientific reports · 2021Article
- Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA.Science advances · 2020Article
- A proteoliposome-based system reveals how lipids control photosynthetic light harvesting.The Journal of biological chemistry · 2020Article
- Dual Role of the C-Terminal Domain in Osmosensing by Bacterial Osmolyte Transporter ProP.Biophysical journal · 2018Article
- OpuF, a New Bacillus Compatible Solute ABC Transporter with a Substrate-Binding Protein Fused to the Transmembrane Domain.Applied and environmental microbiology · 2018Article
- Microorganisms maintain crowding homeostasis.Nature reviews. Microbiology · 2017Review
- Bacterial Energy Sensor Aer Modulates the Activity of the Chemotaxis Kinase CheA Based on the Redox State of the Flavin Cofactor.The Journal of biological chemistry · 2016Article
- Structural insight in the toppling mechanism of an energy-coupling factor transporter.Nature communications · 2016Article
- Contributions of Coulombic and Hofmeister Effects to the Osmotic Activation of Escherichia coli Transporter ProP.Biochemistry · 2016Article
- Bacterial responses to osmotic challenges.The Journal of general physiology · 2015Article
- An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing).The Journal of biological chemistry · 2014Article
- Regulation of acetate kinase isozymes and its importance for mixed-acid fermentation in Lactococcus lactis.Journal of bacteriology · 2014Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells control their volume through the accumulation of compatible solutes. The bacterial ATP-binding cassette transporter OpuA couples compatible solute uptake to ATP hydrolysis. Here, we study the gating mechanism and energy coupling of OpuA reconstituted in lipid nanodiscs. We show that anionic lipids are essential both for the gating and the energy coupling. The tight coupling between substrate binding on extracellular domains and ATP hydrolysis by cytoplasmic nucleotide-binding domains allows the study of transmembrane signaling in nanodiscs. From the tight coupling between processes at opposite sides of the membrane, we infer that the ATPase activity of OpuA in nanodiscs reflects solute translocation. Intriguingly, the substrate-dependent, ionic strength-gated ATPase activity of OpuA in nanodiscs is at least an order of magnitude higher than in lipid vesicles (i.e. with identical membrane lipid composition, ionic strength, and nucleotide and substrate concentrations). Even with the chemical components the same, the lateral pressure (profile) of the nanodiscs will differ from that of the vesicles. We thus propose that membrane tension limits translocation in vesicular systems. Increased macromolecular crowding does not activate OpuA but acts synergistically with ionic strength, presumably by favoring gating interactions of like-charged surfaces via excluded volume effects.
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