ArticleBiology direct2008
Evolutionary primacy of sodium bioenergetics.
Article in Biology direct, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 161 citations in OpenAlex.
- Article
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- ProAD - A database of rotary ion-translocating ATPases in prokaryotic genomes.Frontiers in molecular biosciences · 2024Article
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- Life strategies for Aminicenantia in subseafloor oceanic crust.The ISME journal · 2023Article
- An Initial Proteomic Analysis of Biogas-Related Metabolism ofMicroorganisms · 2023Article
- Desulfatitalea alkaliphila sp. nov., an alkalipilic sulfate- and arsenate- reducing bacterium isolated from a terrestrial mud volcano.Extremophiles : life under extreme conditions · 2023Article
- Determining resident microbial community members and their correlations with geochemistry in a serpentinizing spring.Frontiers in microbiology · 2023Article
- On the potential roles of phosphorus in the early evolution of energy metabolism.Frontiers in microbiology · 2023Review
- The rapid evolution of flagellar ion selectivity in experimental populations ofScience advances · 2022Article
- Deep-branching acetogens in serpentinized subsurface fluids of Oman.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Occurrence of Capnophilic Lactic Fermentation in the Hyperthermophilic Anaerobic BacteriumInternational journal of molecular sciences · 2022Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
18 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
backgroundThe F- and V-type ATPases are rotary molecular machines that couple translocation of protons or sodium ions across the membrane to the synthesis or hydrolysis of ATP. Both the F-type (found in most bacteria and eukaryotic mitochondria and chloroplasts) and V-type (found in archaea, some bacteria, and eukaryotic vacuoles) ATPases can translocate either protons or sodium ions. The prevalent proton-dependent ATPases are generally viewed as the primary form of the enzyme whereas the sodium-translocating ATPases of some prokaryotes are usually construed as an exotic adaptation to survival in extreme environments.
resultsWe combine structural and phylogenetic analyses to clarify the evolutionary relation between the proton- and sodium-translocating ATPases. A comparison of the structures of the membrane-embedded oligomeric proteolipid rings of sodium-dependent F- and V-ATPases reveals nearly identical sets of amino acids involved in sodium binding. We show that the sodium-dependent ATPases are scattered among proton-dependent ATPases in both the F- and the V-branches of the phylogenetic tree.
conclusionBarring convergent emergence of the same set of ligands in several lineages, these findings indicate that the use of sodium gradient for ATP synthesis is the ancestral modality of membrane bioenergetics. Thus, a primitive, sodium-impermeable but proton-permeable cell membrane that harboured a set of sodium-transporting enzymes appears to have been the evolutionary predecessor of the more structurally demanding proton-tight membranes. The use of proton as the coupling ion appears to be a later innovation that emerged on several independent occasions.
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