The targeting information of the mitochondrial outer membrane isoform of cytochrome b5 is contained within the carboxyl-terminal region

FEBS Lett. 1995 Aug 14;370(1-2):69-74. doi: 10.1016/0014-5793(95)00797-d.

Abstract

Two isoforms of mammalian cytochrome b5, which have homologous cytosolic amino-terminal catalytic domains, are located one on endoplasmic reticulum (ER b5) the other on mitochondrial outer membranes (OM b5). A cDNA coding for the previously unknown carboxyl-terminal domain of OM b5 was cloned and a chimera between the catalytic domain of ER b5 and the carboxyl-terminal region of OM b5 was expressed in cultured mammalian cells. The chimera localized to mitochondria, indicating that the carboxyl-terminal 43 amino acids of OM b5 contain sufficient information to target the catalytic domain of ER b5 to the mitochondrial outer membrane.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Cell Line
  • Chlorocebus aethiops
  • Cloning, Molecular
  • Cytochromes b5 / biosynthesis
  • Cytochromes b5 / chemistry*
  • Cytochromes b5 / metabolism*
  • DNA Primers
  • Endoplasmic Reticulum / metabolism
  • Intracellular Membranes / metabolism*
  • Kidney
  • Liver / metabolism
  • Mammals
  • Mitochondria / metabolism*
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Rats
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Transfection

Substances

  • DNA Primers
  • Recombinant Fusion Proteins
  • Cytochromes b5

Associated data

  • GENBANK/X96392