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Immunological detection of the mitochondrial F 1 ‐ATPase α subunit in the matrix of rat liver peroxisomes
Author(s) -
Cuezva J.M.,
Santarén J.F.,
González P.,
Valcarce C.,
Luis A.M.,
Izquierdo J.M.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81237-i
Subject(s) - peroxisome , mitochondrial matrix , protein subunit , immunoelectron microscopy , biology , biochemistry , mitochondrion , cell fractionation , aaa proteins , atpase , organelle , gamma subunit , subcellular localization , microbiology and biotechnology , cytosol , enzyme , cytoplasm , gene , immunohistochemistry , immunology
Rat liver peroxisomes contain in their matrix the α‐subunit of the mitochondrial F 1 ‐ATPase complex. The identification of this protein in liver peroxisomes has been achieved by immunoelectron microscopy and subcellular fractionation. No β‐subunit of the mitochondrial F 1 ‐ATPase complex was detected in the peroxisomal fractions obtained in sucrose gradients or in Nycodenz pelletted peroxisomes. The consensus peroxisomal targeting sequence (Ala‐Lys‐Leu) is found at the carboxy terminus of the mature α‐subunit from bovine heart and rat liver mitochondria. Due to the dual subcellular localization of the α‐subunit and to the structural homologies that exist between this protein and molecular chaperones [(1990) Biol. Chem. 265, 7713‐7716] 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.