The transmembrane segment of Tom20 is recognized by Mim1 for docking to the mitochondrial TOM complex.

@article{Hulett2008TheTS,
  title={The transmembrane segment of Tom20 is recognized by Mim1 for docking to the mitochondrial TOM complex.},
  author={Joanne M. Hulett and Franziska B Lueder and Nickie C. Chan and Andrew J. Perry and P Peter Wolynec and Vladimir A. Likic and Paul R. Gooley and Trevor Lithgow},
  journal={Journal of molecular biology},
  year={2008},
  volume={376 3},
  pages={694-704}
}
Mitochondria cannot be made de novo. Mitochondrial biogenesis requires that up to 1000 proteins are imported into mitochondria, and the protein import pathway relies on hetero-oligomeric translocase complexes in both the inner and outer mitochondrial membranes. The translocase in the outer membrane, the TOM complex, is composed of a core complex formed from the beta-barrel channel Tom40 and additional subunits each with single, alpha-helical transmembrane segments. How alpha-helical… CONTINUE READING

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