Structure and expression of subunit A from the bovine chromaffin cell vacuolar ATPase.
Subunit A of the vacuolar H(+)-ATPase class is thought to be responsible for the ATP hydrolysis which drives proton-pumping. We report here the cloning and sequence determination of the first mammalian cDNA encoding a bovine vacuolar ATPase subunit A from an adrenal medulla cDNA library. Northern blots of bovine adrenal medulla RNA reveal a message of approximately 3.8 kb. The predicted peptide sequence, consisting of 618 amino acids with a calculated molecular weight of 68397 daltons, is similar to the sequences of the three known subunit A proteins. beta-Galactosidase-subunit A fusion proteins were immuno-decorated by an antiserum raised to the subunit A protein from corn coleoptile vacuoles.
Pan
Y X
YX
Department of Physiology and Biophysics, University of Cincinnati College of Medicine, OH 45267-0524.
Xu
J
J
Strasser
J E
JE
Howell
M
M
Dean
G E
GE
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000313:Adrenal Medulla / Q000737:chemistry / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D014617:Vacuoles / Q000737:chemistry / Q000201:enzymology*
D000255:Adenosine Triphosphate; D004247:DNA; D000251:Adenosine Triphosphatases