Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering.

@article{Schiller2008ResiduesOT,
  title={Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering.},
  author={Dirk Schiller and Yu Chin Cheng and Qinglian Liu and William V Walter and Elizabeth A Craig},
  journal={Molecular and cellular biology},
  year={2008},
  volume={28 13},
  pages={4424-33}
}
Translocation of proteins from the cytosol across the mitochondrial inner membrane is driven by the action of the import motor, which is associated with the translocon on the matrix side of the membrane. It is well established that an essential peripheral membrane protein, Tim44, tethers mitochondrial Hsp70 (mtHsp70), the core of the import motor, to the translocon. This Tim44-mtHsp70 interaction, which can be recapitulated in vitro, is destabilized by binding of mtHsp70 to a substrate… CONTINUE READING

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