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Related Experiment Videos

Recombinant SFD isoforms activate vacuolar proton pumps.

Z Zhou1, S B Peng, B P Crider

  • 1Division of Molecular Transport, Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75235, USA.

The Journal of Biological Chemistry
|May 21, 1999
PubMed
Summary
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The vacuolar proton pump

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The vacuolar proton pump (V-ATPase) is crucial for cellular processes, involving cytosolic (V1) and membrane (V0) sectors.
  • The V1 sector includes the Sub Fifty-eight-kDa Doublet (SFD) polypeptides, essential for V-ATPase activity but with uncharacterized individual roles.
  • SFD polypeptides are isoforms generated by alternative splicing.

Purpose of the Study:

  • To investigate the distinct functional roles of the 57-kDa (SFDα) and 50-kDa (SFDβ) isoforms of the SFD subunits.
  • To determine if these isoforms are functionally interchangeable in restoring V-ATPase activity.
  • To explore the structural interactions of SFD subunits within the V-ATPase complex.

Main Methods:

  • Expression of recombinant SFDα and SFDβ proteins in Escherichia coli.

Related Experiment Videos

  • Reconstitution of SFD-depleted V-ATPase holoenzyme with recombinant SFD isoforms.
  • Assay of ATPase and proton pumping activities.
  • Analysis of V-ATPase from chromaffin granules.

    • Main Results:

    • Recombinant SFDα and SFDβ restored ATPase and proton pumping activities to SFD-depleted holoenzyme, indicating functional interchangeability.
    • Native V-ATPase from chromaffin granules contains only the SFDα isoform.
    • Both recombinant SFDα and SFDβ equally restored activity to the depleted enzyme.
    • SFDα and SFDβ interact with both V1 and V0 sectors of the V-ATPase.

    Conclusions:

    • SFDα and SFDβ isoforms are functionally interchangeable in restoring V-ATPase activity.
    • Despite interchangeability, native V-ATPases may preferentially incorporate specific isoforms.
    • SFD subunits play critical structural and functional roles in coupling ATP hydrolysis to proton transport.