Amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria and its homology with the delta-subunit of the F1-ATPase of Escherichia coli

FEBS Lett. 1984 Jan 23;166(1):19-22. doi: 10.1016/0014-5793(84)80036-8.

Abstract

The complete amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria is reported. The protein contains 190 amino acids and has a molecular mass of 20 967. Its structure is characterized by a concentration of charged amino acids in the two terminal segments (N 1-77 and C 128-190) of the protein, whereas its central region is more hydrophobic. The earlier reported homology of the protein with the delta-subunit of E. coli F1, based on the terminal amino acid sequences of OSCP, is further substantiated.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases*
  • Amino Acid Sequence
  • Animals
  • Biological Evolution
  • Carrier Proteins*
  • Cattle
  • Escherichia coli / enzymology*
  • Macromolecular Substances
  • Membrane Proteins*
  • Mitochondria, Heart / enzymology*
  • Mitochondrial Proton-Translocating ATPases
  • Oligomycins / pharmacology

Substances

  • Carrier Proteins
  • Macromolecular Substances
  • Membrane Proteins
  • Oligomycins
  • Adenosine Triphosphatases
  • Mitochondrial Proton-Translocating ATPases
  • oligomycin sensitivity-conferring protein