CHARACTERIZATION OF ATP12, A YEAST NUCLEAR GENE REQUIRED FOR THE ASSEMBLY OF THE MITOCHONDRIAL F1-ATPASE
UNSPECIFIED. (1991) CHARACTERIZATION OF ATP12, A YEAST NUCLEAR GENE REQUIRED FOR THE ASSEMBLY OF THE MITOCHONDRIAL F1-ATPASE. JOURNAL OF BIOLOGICAL CHEMISTRY, 266 (12). pp. 7517-7523. ISSN 0021-9258Full text not available from this repository.
Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta-subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. Recently, two different complementation groups (G13, G57), consisting of yeast nuclear mutants with defective F1, have been described. Biochemical analyses indicate that the mutational block in both groups of mutants affects a critical step needed for the assembly of the alpha and beta-subunits into the F1 oligomer after their transport into mitochondria. In this study the ATP12 gene representative of the nuclear respiratory-deficient mutant of S. cerevisiae (pet) complementation group G57 has been cloned and the encoded product partially characterized. The ATP 12 reading frame is 975 base pairs long and codes for a protein of M(r) = 36,587. The ATP 12 protein is not homologous to the subunits of F1 whose sequences are known, nor does it exhibit significant primary structure similarity to any known protein. In vitro import assays indicate that ATP 12 protein is synthesized as a precursor approximately 3 kDa larger than the mature protein. The mitochondrial localization of the protein has been confirmed by Western blot analysis of mitochondrial proteins with an antibody against a hybrid protein expressed from a trpE-ATP 12 fusion. Fractionation of mitochondria indicates further that the ATP 12 protein is either a minor component of the matrix compartment or is weakly bound to the matrix side of the inner membrane. The molecular weight of the native protein, estimated from its sedimentation properties in sucrose gradients, is at least two times larger than the monomer. This suggests that the ATP 12 protein is probably part of a larger complex.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||JOURNAL OF BIOLOGICAL CHEMISTRY|
|Publisher:||AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC|
|Date:||25 April 1991|
|Number of Pages:||7|
|Page Range:||pp. 7517-7523|
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