ArticleThe Journal of biological chemistry2011
Na+-translocating membrane pyrophosphatases are widespread in the microbial world and evolutionarily precede H+-translocating pyrophosphatases.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 61 citations in OpenAlex.
- Article
- Different sodium and potassium homeostasis patterns between rare and abundant microbial taxa in biological soil crusts revealed by metatranscriptomics.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Article
- Shift in the metabolic profile of sediment microbial communities during seagrass decline.Environmental microbiome · 2025Article
- NaInternational journal of molecular sciences · 2024Article
- HParasitology research · 2024Review
- Functional and structural asymmetry suggest a unifying principle for catalysis in membrane-bound pyrophosphatases.EMBO reports · 2024Article
- Review
- Exploration of the Catalytic Cycle Dynamics of Vigna Radiata HThe Journal of membrane biology · 2023Article
- Metagenomics Revealed a New Genus 'International journal of molecular sciences · 2023Article
- mPPases create a conserved anionic membrane fingerprint as identified via multi-scale simulations.PLoS computational biology · 2022Article
- Pre-steady-state kinetics and solvent isotope effects support the "billiard-type" transport mechanism in NaProtein science : a publication of the Protein Society · 2022Article
- The Mechanism of Energy Coupling in HInternational journal of molecular sciences · 2022Review
- Experimental Approaches for Testing the Hypothesis of the Emergence of Life at Submarine Alkaline Vents.Life (Basel, Switzerland) · 2021Review
- Metabolic versatility of the nitrite-oxidizing bacterium Nitrospira marina and its proteomic response to oxygen-limited conditions.The ISME journal · 2021Article
- Evolution of the Stator Elements of Rotary Prokaryote Motors.Journal of bacteriology · 2020Review
- The HFrontiers in plant science · 2020Article
- The Function of Membrane Integral Pyrophosphatases From Whole Organism to Single Molecule.Frontiers in molecular biosciences · 2019Review
- Insights into the mechanism of membrane pyrophosphatases by combining experiment and computer simulation.Structural dynamics (Melville, N.Y.) · 2017Article
- Membrane pyrophosphatases from Thermotoga maritima and Vigna radiata suggest a conserved coupling mechanism.Nature communications · 2016Article
- Structural basis for the reversibility of proton pyrophosphatase.Plant signaling & behavior · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane pyrophosphatases (PPases), divided into K(+)-dependent and K(+)-independent subfamilies, were believed to pump H(+) across cell membranes until a recent demonstration that some K(+)-dependent PPases function as Na(+) pumps. Here, we have expressed seven evolutionarily important putative PPases in Escherichia coli and estimated their hydrolytic, Na(+) transport, and H(+) transport activities as well as their K(+) and Na(+) requirements in inner membrane vesicles. Four of these enzymes (from Anaerostipes caccae, Chlorobium limicola, Clostridium tetani, and Desulfuromonas acetoxidans) were identified as K(+)-dependent Na(+) transporters. Phylogenetic analysis led to the identification of a monophyletic clade comprising characterized and predicted Na(+)-transporting PPases (Na(+)-PPases) within the K(+)-dependent subfamily. H(+)-transporting PPases (H(+)-PPases) are more heterogeneous and form at least three independent clades in both subfamilies. These results suggest that rather than being a curious rarity, Na(+)-PPases predominantly constitute the K(+)-dependent subfamily. Furthermore, Na(+)-PPases possibly preceded H(+)-PPases in evolution, and transition from Na(+) to H(+) transport may have occurred in several independent enzyme lineages. Site-directed mutagenesis studies facilitated the identification of a specific Glu residue that appears to be central in the transport mechanism. This residue is located in the cytoplasm-membrane interface of transmembrane helix 6 in Na(+)-PPases but shifted to within the membrane or helix 5 in H(+)-PPases. These results contribute to the prediction of the transport specificity and K(+) dependence for a particular membrane PPase sequence based on its position in the phylogenetic tree, identity of residues in the K(+) dependence signature, and position of the membrane-located Glu residue.
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