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J. Biol. Chem., Vol. 267, Issue 11, 7386-7394, Apr, 1992
SH Ackerman, J Martin and A Tzagoloff
In Saccharomyces cerevisiae, expression of functional F1-ATPase requires
two proteins encoded by the ATP11 and ATP12 genes. Mutations in either gene
block some crucial late step in assembly of F1, causing the alpha and beta
subunits to accumulate in mitochondria as inactive aggregates (Ackerman, S.
H., and Tzagoloff, A. (1991) Proc. Natl. Acad. Sci. U.S.A. 87, 4986-4990).
In the present study we have cloned and determined the sequence of ATP11.
The encoded product is protein of 37 kDa with no obvious homology to any
known protein. In vitro import assays of ATP11 precursor and immunochemical
evidence indicate that the protein is located in mitochondria. A fusion was
made between ATP11 and a short sequence coding for 78 amino acids with the
biotination signal of bacterial transcarboxylase. The protein expressed
from this construct complements atp11 mutants, indicating that the addition
of the extra 78 amino acids at the carboxyl terminus of the ATP11 protein
does not compromise its function. The hybrid protein is detected in
mitochondria with antibodies and with peroxidase-conjugated avidin.
Biotinated ATP11 protein can be partially purified by affinity
chromatography on monomeric or tetrameric avidin coupled to Sepharose. A
fraction eluted from the avidin column and enriched for the biotinated
ATP11 protein also contains the alpha and beta subunits of F1-ATPase.
Characterization of ATP11 and detection of the encoded protein in mitochondria of Saccharomyces cerevisiae
Department of Biological Sciences, Columbia University, New York, New York 10027.
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