Human mitochondrial import receptor, Tom20p. Use of glutathione to reveal specific interactions between Tom20‐glutathione S‐transferase and mitochondrial precursor proteins

@article{Schleiff1997HumanMI,
  title={Human mitochondrial import receptor, Tom20p. Use of glutathione to reveal specific interactions between Tom20‐glutathione S‐transferase and mitochondrial precursor proteins},
  author={Enrico Schleiff and Gordon C. Shore and Ing Swie Goping},
  journal={FEBS Letters},
  year={1997},
  volume={404}
}

The mitochondrial outer membrane protein import machinery: a new player in apoptosis?

Recently, several pBCL-2s have been shown to interact with components of the translocase of the outer membrane (TOM), a complex responsible for the import into and across the MOM of nuclear encoded mitochondrial proteins.

Cloning and Characterization of a 35-kDa Mouse Mitochondrial Outer Membrane Protein MOM35 with High Homology to Tom40

A 35-kDa protein from a mouse cDNA library with a 25% overall amino acididentity to yTom40 and 27% identity to nTom40 is cloned and contains a highly conserved region with possible physiological importance that interacts specifically in vitro with preproteins proposed to be imported by a Tom40-dependent pathway.

The tail-anchoring domain of Bfl1 and HCCS1 targets mitochondrial membrane permeability to induce apoptosis

It is shown that ATAP targets specifically to mitochondria, and induces caspase-dependent apoptosis that does not require Bax or Bak, and proposed that both ATAP and MTS could be used as therapeutic peptides to induce cell death in the treatment of cancer cells.

Sorting of Preproteins into Mitochondria

Several observations, including sequence comparisons of the mitochondrial 16 S RNA, indicate that mitochondria evolved from early a-proteobacteria by endosymbiosis, and appear to contain a homologous set of Tom and Tim proteins and to apply the same mechanistic principles.

Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70*

It is concluded that each of the three import receptors binds preproteins independently and by a different mechanism.

Self-association and precursor protein binding of Saccharomyces cerevisiae Tom40p, the core component of the protein translocation channel of the mitochondrial outer membrane.

Simultaneous self-assembly and precursor protein binding suggest that Tom40p contains at least two different domains mediating these processes, which should be useful for analysing protein-protein interactions involving individual or groups of components of the mitochondrial import machinery.

References

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The protein import receptor of mitochondria.

Import and insertion of proteins into the mitochondrial outer membrane.

What is known about the various steps leading to protein insertion into the outer membrane is described, and the energetics that favor vectorial translocation into and across this membrane are discussed.