Nature Reviews Microbiology 5, 892-899 (November 2007) | doi:10.1038/nrmicro1767

OpinionInventing the dynamo machine: the evolution of the F-type and V-type ATPases

Armen Y. Mulkidjanian1, Kira S. Makarova2, Michael Y. Galperin2 & Eugene V. Koonin2  About the authors


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.

Author affiliations

  1. Armen Y. Mulkidjanian is at the School of Physics, University of Osnabrück, Osnabrück D-49069, Germany and the A.N. Belozersky Institute of Physico–Chemical Biology, Moscow State University, Moscow 119899, Russia.
  2. Kira S. Makarova, Michael Y. Galperin and Eugene V. Koonin are at the National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894, USA.

Correspondence to: Armen Y. Mulkidjanian1 Email:

Correspondence to: Eugene V. Koonin2 Email:


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