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J. Biol. Chem., Vol. 263, Issue 33, 17251-17254, Nov, 1988

Molecular cloning of the beta-subunit of a possible non-F0F1 type ATP synthase from the acidothermophilic archaebacterium, Sulfolobus acidocaldarius

K Denda, J Konishi, T Oshima, T Date and M Yoshida
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.

The gene which encodes the beta subunit of the novel membrane- associated ATPase has been identified and characterized. The beta subunit, which is most likely the soluble part of the non-F0F1 type H+- ATPase, was obtained from the archaebacterium, Sulfolobus acidocaldarius. In terms of its location, it follows just after the gene for its alpha subunit. It is comprised of 1398 nucleotides, corresponding to a protein of 465 amino acids, and the consensus sequence in the nucleotide binding proteins is poorly conserved. Together with previously described results, the distant homology of the S. acidocaldarius ATPase alpha and beta subunits when compared to those of F0F1-ATPases indicates that this archaebacterial ATPase belongs to an ion-translocating ATPase family uniquely different than F0F1-ATPases even if S. acidocaldarius ATPase and F0F1-ATPases have been derived from a common ancestral ATPase.
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