Inventing the dynamo machine: the evolution of the F-type and V-type ATPases
Abstract
The rotary proton- and sodium-translocating ATPases are reversible molecular machines present in all cellular life forms that couple ion movement across membranes with ATP hydrolysis or synthesis. Sequence and structural comparisons of F- and V-type ATPases have revealed homology between their catalytic and membrane subunits, but not between the subunits of the central stalk that connects the catalytic and membrane components. Based on this pattern of homology, we propose that these ATPases originated from membrane protein translocases, which, themselves, evolved from RNA translocases. We suggest that in these ancestral translocases, the position of the central stalk was occupied by the translocated polymer.
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Prokaryotic ATPases show a clear dichotomy into eubacterial (F-type) and archaebacterial (A-type) ATPases.
“Consistent with that, prokaryotic ATPases show a clear dichotomy into two types: the eubacterial (or F-type) ATPase and the archaebacterial (or A-type) ATPase [121].”
From Early bioenergetic evolution (2013) · cites this paper as [121]
Archaea and Bacteria contain primarily A/V-type and F-type ATP synthase subunits, respectively, and eukaryotes harbor complexes of both types.
“Archaea and Bacteria contain primarily A/V-type and F-type subunits, respectively, and eukaryotes harbor complexes of both types”
From ATP synthase evolution on a cross-braced dated tree of life (2023) · cites this paper as [29]
The catalytic and non-catalytic subunits of the ATP synthase R1 component are paralogs that arose prior to LUCA through an ancient duplication of a RecA family protein (P-loop NTPase) followed by loss of catalytic function in one subunit.
“The catalytic and non-catalytic subunits comprising the soluble hetero-hexameric R1 component, are paralogs to each other. They arose prior to LUCA through an ancient duplication of a RecA family protein (P-loop NTPase) followed by the loss of the catalytic function in one subunit”
From ATP synthase evolution on a cross-braced dated tree of life (2023) · cites this paper as [29]
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- Authors
- Mulkidjanian, A. Y., Makarova, K. S., Galperin, M. Y., & Koonin, E. V.
- Affiliations
- Osnabrück University (DE)
- National Institutes of Health (US)
- Corresponding author
- Mulkidjanian, Armen Y.
- Koonin, Eugene V.
- Venue
- Nature Reviews Microbiology
- Published
- 2007-11
- Volume
- 5
- Issue
- 11
- Pages
- 892-899
- ISSN
- 1740-1526 (ISSN-L)
- 1740-1534
- OpenAlex
- W2001138638
- Cited by
- 210
- References
- 95
- Citations by year
- 2026: 7 · 2025: 9 · 2024: 10 · 2023: 7 · 2022: 9 · 2021: 15 · 2020: 15 · 2019: 14 · 2018: 9 · 2017: 15 · 2016: 9 · 2015: 16 · 2014: 11 · 2013: 16 · 2012: 9
- FWCI
- 0.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- F0F1-ATP synthase, V-type ATPase, molecular machines, bioenergetics
- MeSH terms
- Adenosine Triphosphatases, Proton-Translocating ATPases, Evolution, Molecular, Cation Transport Proteins
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