The biogenesis of rat-liver mitochondrial ATPase. Evidence that the N,N′-dicyclohexyl carbodiimide-binding protein is synthesized outside the mitochondria

  • De Jong L
  • Holtrop M
  • Kroon A
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Abstract

1. 1. Radioactive N,N′-dicyclohexyl carbodiimide (DCCD) is bound as effectively to the N,N′-dicyclohexyl carbodiimide- and oligomycin-sensitive ATPase complex in submitochondrial particles of normal rat liver as to the similar but partially N,N′-dicyclohexyl carbodiimide- and oligomycin-insensitive complex of thiamphenicol-treated rats. The latter complex is deficient in 3 subunits (subunit 6, 7 and 10). 2. 2. Radioactive N,N′-dicyclohexyl carbodiimide is exclusively bound to the subunits present in the bands 8 and 11 of SDS-PAA gels of the purified ATPase complex. These subunits, most likely the dimer and monomer of the N,N′-dicyclohexyl carbodiimide-binding protein, are products of the cytoplasmic protein synthesis. 3. 3. The results together indicate that the N,N′-dicyclohexyl carbodiimide-insensitivity of the ATPase complex formed during in vitro inhibition of mitochondrial protein synthesis, is not caused by a lack of inhibitor binding protein. The same holds for the oligomycin-insensitivity. © 1980.

Author-supplied keywords

  • (Rat liver)
  • Dicyclohexyl carbodiimide-binding protein
  • Mitochondrial ATPase synthesis
  • Oligomycin-sensitivity
  • Protein synthesis

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Authors

  • L. De Jong

  • M. Holtrop

  • A. M. Kroon

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