Cyclophilin catalyzes protein folding in yeast mitochondria.

@article{Matouschek1995CyclophilinCP,
  title={Cyclophilin catalyzes protein folding in yeast mitochondria.},
  author={Andreas Matouschek and Sabine Rospert and Karl Schmid and Benjamin S. Glick and Gottfried Schatz},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 14},
  pages={6319-23}
}
Cyclophilins are a family of ubiquitous proteins that are the intracellular target of the immunosuppressant drug cyclosporin A. Although cyclophilins catalyze peptidylprolyl cis-trans isomerization in vitro, it has remained open whether they also perform this function in vivo. Here we show that Cpr3p, a cyclophilin in the matrix of yeast mitochondria, accelerates the refolding of a fusion protein that was synthesized in a reticulocyte lysate and imported into the matrix of isolated yeast… CONTINUE READING
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