Stable association of 70-kDa heat shock protein induces latent multisite specificity of a unisite-specific endonuclease in yeast mitochondria.

@article{Mizumura1999StableAO,
  title={Stable association of 70-kDa heat shock protein induces latent multisite specificity of a unisite-specific endonuclease in yeast mitochondria.},
  author={H. Mizumura and Takehiko Shibata and Nobuhiro Morishima},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 36},
  pages={25682-90}
}
The multisite-specific endonuclease Endo.SceI of yeast mitochondria is unique among endonucleases because its 50-kDa subunit forms a stable dimer with the mitochondrial 70-kDa heat shock protein (mtHSP70), which otherwise fulfills a chaperone function by binding transiently to unfolded proteins. Here we show that the mtHSP70 subunit confers broader sequence… CONTINUE READING