ArticleJournal of bacteriology2014
Purification and functional reconstitution of a seven-subunit mrp-type na+/h+ antiporter.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Complete Mitochondrial Genome Sequencing of Asian Glass Lizards (Anguidae:Ecology and evolution · 2025Article
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- Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations.Nature communications · 2022Article
- Prokaryotic NaInternational journal of molecular sciences · 2022Review
- A novel gene from the acidophilic bacterium Leptospirillum sp. CF-1 and its role in oxidative stress and chromate tolerance.Biological research · 2022Article
- Genetic and Biochemical Characterization of the NaJournal of bacteriology · 2021Article
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- The Lysine 299 Residue Endows the Multisubunit Mrp1 Antiporter with Dominant Roles in NaApplied and environmental microbiology · 2018Article
- Roles of Staphylococcus aureus Mnh1 and Mnh2 Antiporters in Salt Tolerance, Alkali Tolerance, and Pathogenesis.Journal of bacteriology · 2018Article
- Article
- The Surface Layer Homology Domain-Containing Proteins of AlkaliphilicFrontiers in microbiology · 2018Article
- Proteomic and Mutant Analysis of the COJournal of bacteriology · 2017Article
- Functional Role of MrpA in the MrpABCDEFG Na+/H+ Antiporter Complex from the Archaeon Methanosarcina acetivorans.Journal of bacteriology · 2017Article
- Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea.Frontiers in microbiology · 2017Review
- Functional analysis of PrkA - a putative serine protein kinase from Mesorhizobium alhagi CCNWXJ12-2 - in stress resistance.BMC microbiology · 2016Article
- Adaptation of Staphylococcus xylosus to Nutrients and Osmotic Stress in a Salted Meat Model.Frontiers in microbiology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Mrp antiporters and their homologues in the cation/proton antiporter 3 family of the Membrane Transporter Database are widely distributed in bacteria. They have major roles in supporting cation and cytoplasmic pH homeostasis in many environmental, extremophilic, and pathogenic bacteria. These antiporters require six or seven hydrophobic proteins that form hetero-oligomeric complexes, while most other cation/proton antiporters require only one membrane protein for their activity. The resemblance of three Mrp subunits to membrane-embedded subunits of the NADH:quinone oxidoreductase of respiratory chains and to subunits of several hydrogenases has raised interest in the evolutionary path and commonalities of their proton-translocating domains. In order to move toward a greater mechanistic understanding of these unusual antiporters and to rigorously demonstrate that they function as secondary antiporters, powered by an imposed proton motive force, we established a method for purification and functional reconstitution of the seven-subunit Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4. Na(+)/H(+) antiporter activity was demonstrated by a fluorescence-based assay with proteoliposomes in which the Mrp complex was coreconstituted with a bacterial FoF1-ATPase. Proton pumping by the ATPase upon addition of ATP generated a proton motive force across the membranes that powered antiporter activity upon subsequent addition of Na(+).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.