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The coupling ATPase complex: an evolutionary view.

D A Harris

    Bio Systems
    |January 1, 1981
    PubMed
    Summary
    This summary is machine-generated.

    Primitive cells evolved from phospholipid vesicles, developing fermentation fueled by proton channels and ATP-driven pumps. Early adenosine 5' triphosphate phosphohydrolase (ATPase) structures later diversified, influencing cellular energy systems.

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    Area of Science:

    • Origin of Life Studies
    • Biochemistry
    • Evolutionary Biology

    Background:

    • Early life likely originated from self-assembling phospholipid structures like micelles and vesicles in primordial environments.
    • The development of integrated biochemical systems within these structures, forming primitive cells, was contingent on a shared energy source, such as adenosine triphosphate (ATP).
    • Fermentation emerged as an early metabolic pathway, facilitated by the evolution of proton channels and ATP-driven pumps.

    Purpose of the Study:

    • To elucidate the evolutionary trajectory of primitive cells and their energy-generating mechanisms.
    • To investigate the structural and functional evolution of adenosine 5' triphosphate phosphohydrolase (ATPase) in early cellular life.
    • To understand the role of specific molecular markers in tracing the evolutionary history of prokaryotic and eukaryotic energy systems.

    Main Methods:

    • Analysis of biochemical pathways and molecular structures in early cellular evolution.
    • Examination of the functional characteristics of primitive proton channels and ATPases, including their inhibition by specific chemical agents (dicyclohexylcarbodiimide and 4-chloro 7-nitrobenzofurazan).
    • Comparative analysis of ATPase subunit composition and evolutionary divergence in prokaryotic, mitochondrial, and chloroplast lineages.

    Main Results:

    • Phospholipid vesicles served as precursors to primitive cells, enabling early catalytic and replicative functions.
    • The evolution of proton channels and ATP-driven pumps supported fermentation, a key metabolic process in early cells.
    • Adenosine 5' triphosphate phosphohydrolase (ATPase) evolved from a simple 4-subunit structure to a more complex 8-subunit form, potentially linked to ATP synthesis.
    • Gene duplication and divergence played a role in the evolution of ATPase subunits (alpha and beta).
    • Sensitivity to inhibitors like oligomycin developed after the divergence of mitochondrial and chloroplast lines.

    Conclusions:

    • The evolution of phospholipid vesicles into cellular life involved the integration of energy metabolism, particularly fermentation.
    • The structural complexity and functional specialization of ATPase are key indicators of cellular evolution and energy transduction.
    • The ATPase inhibitor protein is a conserved regulatory element across diverse coupling ATPases, highlighting its fundamental role.