ArticleThe Journal of biological chemistry2010
Single site mutations in the hetero-oligomeric Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4 that affect Na+/H+ antiport activity, sodium exclusion, individual Mrp protein levels, or Mrp complex formation.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Enrichment and characterization of a haloalkaline-tolerant anammox bacterium.The ISME journal · 2026Article
- 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
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structure of the respiratory MBS complex reveals iron-sulfur cluster catalyzed sulfane sulfur reduction in ancient life.Nature communications · 2020Article
- Article
- Nature and bioprospecting of haloalkaliphilics: a review.World journal of microbiology & biotechnology · 2020Review
- Improved Salt Tolerance and Metabolomics Analysis ofFrontiers in bioengineering and biotechnology · 2020Article
- Polar or Charged Residues Located in Four Highly Conserved Motifs Play a Vital Role in the Function or pH Response of a UPF0118 Family NaFrontiers in microbiology · 2020Article
- The complete genome sequence of Rhodobaca barguzinensis alga05 (DSM 19920) documents its adaptation for life in soda lakes.Extremophiles : life under extreme conditions · 2018Article
- Structure of an Ancient Respiratory System.Cell · 2018Article
- The Lysine 299 Residue Endows the Multisubunit Mrp1 Antiporter with Dominant Roles in NaApplied and environmental microbiology · 2018Article
- 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
- Differences in the phenotypic effects of mutations in homologous MrpA and MrpD subunits of the multi-subunit Mrp-type NaExtremophiles : life under extreme conditions · 2017Article
- Article
- A giant molecular proton pump: structure and mechanism of respiratory complex I.Nature reviews. Molecular cell biology · 2015Review
- Regulation of CO2 Concentrating Mechanism in Cyanobacteria.Life (Basel, Switzerland) · 2015Review
- Purification and functional reconstitution of a seven-subunit mrp-type na+/h+ antiporter.Journal of bacteriology · 2014Article
- MrpA functions in energy conversion during acetate-dependent growth of Methanosarcina acetivorans.Journal of bacteriology · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Mrp systems are widely distributed and structurally complex cation/proton antiporters. Antiport activity requires hetero-oligomeric complexes of all six or seven hydrophobic Mrp proteins (MrpA-MrpG). Here, a panel of site-directed mutants in conserved or proposed motif residues was made in the Mrp Na(+)(Li(+))/H(+) antiporter from an alkaliphilic Bacillus. The mutant operons were expressed in antiporter-deficient Escherichia coli KNabc and assessed for antiport properties, support of sodium resistance, membrane levels of each Mrp protein, and presence of monomeric and dimeric Mrp complexes. Antiport did not depend on a VFF motif or a conserved tyrosine pair, but a role for a conserved histidine in a potential quinone binding site of MrpA was supported. The importance of several acidic residues for antiport was confirmed, and the importance of additional residues was demonstrated (e.g. three lysine residues conserved across MrpA, MrpD, and membrane-bound respiratory Complex I subunits (NuoL/M/N)). The results extended indications that MrpE is required for normal membrane levels of other Mrp proteins and for complex formation. Moreover, mutations in several other Mrp proteins lead to greatly reduced membrane levels of MrpE. Thus, changes in either of the two Mrp modules, MrpA-MrpD and MrpE-MrpG, influence the other. Two mutants, MrpB-P37G and MrpC-Q70A, showed a normal phenotype but lacked the MrpA-MrpG monomeric complex while retaining the dimeric hetero-oligomeric complex. Finally, MrpG-P81A and MrpG-P81G mutants exhibited no antiport activity but supported sodium resistance and a low [Na(+)](in). Such mutants could be used to screen hypothesized but uncharacterized sodium efflux functions of Mrp apart from Na(+) (Li(+))/H(+) antiport.
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