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Rat liver peroxisomes contain in their matrix the a-subunit of the mitochondrial F,-ATPase complex. The identification of this protein in liver peroxisomes has been achieved by immunoelectron microscopy and subcellular fractionation. No /?-subunit of the mitochondrial F,-ATPase complex was detected in the peroxisomal fractions obtained in sucrose gradients or in Nycodenz pelletkd peroxisomes. The consensus peroxisomal targeting sequence (Ala-Lys-Leu) is found at the carboxy terminus of the mature cc-subunit from bovine heart and rat liver mitochondria. Due to the dual subcellular localization of the a-subunit and to the structural homologies that exist between this protein and molecular chaperones [(1990) Biol. Chem. 265,7713-77161 it is suggested that the protein should perform another functional role(s) in both organelles, plus to its characteristic involvement in the regulation of mitochondrial ATPase activity.

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