Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules.
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.
Ludwig
J
J
Zentrum der Biologischen Chemie, Universitätsklinikum Frankfurt, D-60590 Frankfurt, Germany.
Kerscher
S
S
Brandt
U
U
Pfeiffer
K
K
Getlawi
F
F
Apps
D K
DK
Schägger
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D002837:Chromaffin Granules / Q000201:enzymology*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D025262:Vacuolar Proton-Translocating ATPases
C112112:ATP6H protein, Bos taurus; D008565:Membrane Proteins; D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases