Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules

J Biol Chem. 1998 May 1;273(18):10939-47. doi: 10.1074/jbc.273.18.10939.

Abstract

Vacuolar proton-translocating ATPase (holoATPase and free membrane sector) was isolated from bovine chromaffin granules by blue native polyacrylamide gel electrophoresis. A 5-fold excess of membrane sector over holoenzyme was determined in isolated chromaffin granule membranes. M9.2, a novel extremely hydrophobic 9.2-kDa protein comprising 80 amino acids, was detected in the membrane sector. It shows sequence and structural similarity to Vma21p, a yeast protein required for assembly of vacuolar ATPase. A second membrane sector-associated protein (M8-9) was identified and characterized by amino-terminal protein sequencing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Chromaffin Granules / enzymology*
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Mice
  • Molecular Sequence Data
  • Proton-Translocating ATPases / metabolism*
  • Sequence Homology, Nucleic Acid
  • Vacuolar Proton-Translocating ATPases*

Substances

  • ATP6H protein, Bos taurus
  • Membrane Proteins
  • Vacuolar Proton-Translocating ATPases
  • Proton-Translocating ATPases

Associated data

  • GENBANK/P81103
  • GENBANK/P81134
  • GENBANK/Y15285
  • GENBANK/Y15286