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Related Experiment Videos

Evolution of structure and function of V-ATPases.

H Kibak1, L Taiz, T Starke

  • 1Biology Department, University of California, Santa Cruz 95064.

Journal of Bioenergetics and Biomembranes
|August 1, 1992
PubMed
Summary

The evolution of proton pumping ATPases (ATP synthase) reveals conserved structures across all life, originating from a common ancestral gene before the last common ancestor. This suggests ancient origins for catalytic and noncatalytic subunits.

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Area of Science:

  • Evolutionary Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Proton pumping ATPases (ATP synthase) are fundamental energy-transducing enzymes conserved across all extant life forms.
  • The structural similarity between V- and F-type ATPases suggests a shared evolutionary origin.

Purpose of the Study:

  • To investigate the evolutionary history of V- and F-type ATPases/ATP synthases.
  • To predict the ancestral subunit structure and understand the evolution of paralogous subunits.
  • To correlate structure and function for insights into early bioenergetics.

Main Methods:

  • Sequence analysis of V- and F-type ATPases/ATP synthases.
  • Phylogenetic analysis to map gene duplication events.
  • Comparative analysis of subunit structures and functions across organisms.

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Main Results:

  • V- and F-type ATPases evolved from a single ancestral enzyme present before the last common ancestor.
  • Gene duplication events for catalytic and noncatalytic subunits predate the last common ancestor.
  • Established a correlation between V/F-ATPase structure and function, with implications for early bioenergetics and proto-eukaryotes.

Conclusions:

  • The V/F-type ATPases possess a deep evolutionary history, with key subunit duplications occurring very early.
  • Understanding these evolutionary relationships provides insights into the bioenergetic strategies of ancient life forms.
  • Analysis of V-ATPase isoforms in eukaryotes suggests later gene duplications related to tissue-specific or organelle-specific functions.