Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits.

@article{Gli1993FunctionalRI,
  title={Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits.},
  author={Vincent G{\'e}li},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1993},
  volume={90 13},
  pages={6247-51}
}
  • Vincent Géli
  • Published 1993 in
    Proceedings of the National Academy of Sciences…
The matrix processing peptidase from yeast (Saccharomyces cerevisiae) mitochondria was expressed in Escherichia coli via a plasmid-borne operon encoding the mature forms of the alpha and beta subunits of the enzyme. The subunits assembled into a fully active, soluble enzyme. The mature subunits were also expressed individually. The alpha subunit accumulated in large amounts and was obtained at a purity of 80% after a single chromatographic step. The beta-subunit-producing strain expressed an… CONTINUE READING

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