Relationship of the membrane ATPase from Halobacterium saccharovorum to vacuolar ATPases.
Polyclonal antiserum against subunit A (67 kDa) of the vacuolar ATPase from Neurospora crassa reacted with subunit I (87 kDa) from a membrane ATPase of the extremely halophilic archaebacterium Halobacterium saccharovorum. The halobacterial ATPase was inhibited by nitrate and N-ethylmaleimide; the extent of the latter inhibition was diminished in the presence of adenosine di- or triphosphates. 4-Chloro-7-nitrobenzofurazan inhibited the halobacterial ATPase also in a nucleotide-protectable manner; the bulk of inhibitor was associated with subunit II (60 kDa). The data suggested that this halobacterial ATPase may have conserved structural features from both the vacuolar and the F-type ATPases.
Stan-Lotter
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NASA Ames Research Center, Moffett Field, California 94035.
Bowman
E J
EJ
Hochstein
L I
LI
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000276:immunology*; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000276:immunology; D015153:Blotting, Western; D003429:Cross Reactions; D005033:Ethylmaleimide / Q000494:pharmacology; D005656:Fungal Proteins / Q000276:immunology; D006217:Halobacterium / Q000201:enzymology*; D008970:Molecular Weight; D009492:Neurospora crassa / Q000201:enzymology; D009566:Nitrates / Q000494:pharmacology; D006180:Proton-Translocating ATPases / Q000276:immunology*; D014617:Vacuoles / Q000201:enzymology*
D001426:Bacterial Proteins; D005656:Fungal Proteins; D009566:Nitrates; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases; D005033:Ethylmaleimide