ArticleExtremophiles : life under extreme conditions2017
Differences in the phenotypic effects of mutations in homologous MrpA and MrpD subunits of the multi-subunit Mrp-type Na
Article in Extremophiles : life under extreme conditions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Membrane-domain mutations in respiratory complex I impede catalysis but do not uncouple proton pumping from ubiquinone reduction.PNAS nexus · 2022Article
- Ion transfer mechanisms in Mrp-type antiporters from high resolution cryoEM and molecular dynamics simulations.Nature communications · 2022Article
- pH Homeostasis and Sodium Ion Pumping by Multiple Resistance and pH Antiporters inFrontiers in microbiology · 2021Article
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Sodium antiporters of Pseudomonas aeruginosa in challenging conditions: effects on growth, biofilm formation, and swarming motility.Journal, genetic engineering & biotechnology · 2020Article
- Article
- A Hydrophobic Small Protein, BpOF4_01690, Is Critical for Alkaliphily of AlkaliphilicFrontiers in microbiology · 2018Article
- Functional Role of MrpA in the MrpABCDEFG Na+/H+ Antiporter Complex from the Archaeon Methanosarcina acetivorans.Journal of bacteriology · 2017Article
- International Conference on Extremophiles 2016.Extremophiles : life under extreme conditions · 2017Article
- Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea.Frontiers in microbiology · 2017Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Mrp antiporters are the sole antiporters in the Cation/Proton Antiporter 3 family of transporter databases because of their unusual structural complexity, 6-7 hydrophobic proteins that function as a hetero-oligomeric complex. The two largest and homologous subunits, MrpA and MrpD, are essential for antiport activity and have direct roles in ion transport. They also show striking homology with proton-conducting, membrane-embedded Nuo subunits of respiratory chain complex I of bacteria, e.g., Escherichia coli. MrpA has the closest homology to the complex I NuoL subunit and MrpD has the closest homology to the complex I NuoM and N subunits. Here, introduction of mutations in MrpD, in residues that are also present in MrpA, led to defects in antiport function and/or complex formation. No significant phenotypes were detected in strains with mutations in corresponding residues of MrpA, but site-directed changes in the C-terminal region of MrpA had profound effects, showing that the MrpA C-terminal region has indispensable roles in antiport function. The results are consistent with a divergence in adaptations that support the roles of MrpA and MrpD in secondary antiport, as compared to later adaptations supporting homologs in primary proton pumping by the respiratory chain complex I.
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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.