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J. Biol. Chem., Vol. 263, Issue 28, 13994-14001, Oct, 1988
EJ Bowman, K Tenney and BJ Bowman
The vacuolar membrane of Neurospora crassa contains a H+-translocating
ATPase composed of at least three subunits with approximate molecular
weights of 70,000, 60,000, and 15,000. Both genomic and cDNA clones
encoding the largest subunit, which appears to contain the active site of
the enzyme, have been isolated and sequenced. The gene for this subunit,
designated vma-1, contains six small introns (60-131 base pairs) and
encodes a hydrophilic protein of 607 amino acids, Mr 67,121. Within the
sequence is a putative nucleotide-binding region, consistent with the
proposal that this subunit contains the site of ATP hydrolysis. This 67-kDa
polypeptide shows high homology (62% identical residues overall and 84% in
the middle of the protein) to the analogous polypeptide of a higher plant
vacuolar ATPase. The hypothesis that the vacuolar ATPase is related to F0F1
ATPases is strongly supported by the finding of considerable homology
between the 67-kDa subunit of the Neurospora vacuolar ATPase and both the
alpha and beta subunits of F0F1 ATPases.
Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of vma-1 encoding the 67-kDa subunit reveals homology to other ATPases
Department of Biology, Thimann Laboratories, University of California, Santa Cruz 95064.
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