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Vacuolar proton pumps.

D K Stone1, B P Crider, T C Südhof

  • 1Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235.

Journal of Bioenergetics and Biomembranes
|October 1, 1989
PubMed
Summary
This summary is machine-generated.

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A novel class of proton-translocating ATPases (proton pumps) found in plant, fungal, and mammalian cells are large hetero-oligomers. These pumps share a common evolutionary origin with mitochondrial F1F0-type proton pumps.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • A new class of proton-translocating ATPases has been identified in the endomembranes of various eukaryotic cells.
  • These proton pumps are complex hetero-oligomeric structures with distinct functional domains for ATP hydrolysis and proton translocation.

Purpose of the Study:

  • To discuss the enzymatic characteristics of these novel proton pumps.
  • To review the current understanding of their subunit composition and functional roles.
  • To explore evolutionary relationships based on primary sequence data.

Main Methods:

  • Enzymatic assays to characterize proton pump activity.
  • Analysis of subunit composition and stoichiometry.
  • Bioinformatic analysis of primary sequence data for evolutionary comparisons.

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Main Results:

  • The proton pumps possess distinct ATP hydrolytic and transmembrane proton pore sectors.
  • Detailed enzymatic properties and subunit functions are being elucidated.
  • Sequence data suggest a shared ancestry with F1F0-type ATPases.

Conclusions:

  • These endomembrane proton pumps represent a significant class of cellular energy transducers.
  • Their structural and functional distinctiveness, alongside evolutionary links to F1F0-ATPases, offers new insights into ATPase evolution.
  • Further research into these proton pumps will illuminate fundamental cellular processes.