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

  title={Human mitochondrial import receptor, Tom20p. Use of glutathione to reveal specific interactions between Tom20‐glutathione S‐transferase and mitochondrial precursor proteins},
  author={E. Schleiff and G. Shore and I. Goping},
  journal={FEBS Letters},
© 1997 Federation of European Biochemical Societies. 
Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane.
Bcl-2alpha shows a unique pattern of interactions with the components of the mitochondrial TOM complex, demonstrating that at least two different pathways lead from the import receptor Tom20 into the mitochondrial outer membrane. Expand
Import and assembly of proteins into mitochondria of mammalian cells.
Recent advances in understanding of protein import into mitochondria are outlined, focusing on the characterisation of cytosolic molecular chaperones that are involved in binding to mitochondrial-targeted preproteins, as well as the identification of both conserved and novel subunits of the import machineries of the outer and inner mitochondrial membranes. Expand
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. Expand
Structural elements of the mitochondrial preprotein-conducting channel Tom40 dissolved by bioinformatics and mass spectrometry.
The outer surface of the Tom40 barrel reveals two conserved amino acid clusters, which might be important for mitochondrial pre-sequence peptide binding as it is only present in Tom40 but not in VDAC proteins. Expand
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. Expand
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. Expand
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. Expand
Peptide library approach with a disulfide tether to refine the Tom20 recognition motif in mitochondrial presequences.
A refined, common motif for the recognition by Tom20 was deduced, and it was found that the segment consisting of residues 14-20 of the ALDH presequence was locally optimized in the sequence space, with respect to Tom20 binding. Expand
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. Expand
Expression, purification, and in vitro characterization of the human outer mitochondrial membrane receptor human translocase of the outer mitochondrial membrane 20.
It was found that specific dimerization of the cytosolic domain of hTom20 is necessary in order to prevent aggregation of the protein and it is proposed that the function of the cysteine is to promote Dimerization as found in the absence of dithiothreitol. Expand


The protein import receptor of mitochondria.
It is proposed that the two receptor subcomplexes can act together as a single, multifunctional receptor that binds simultaneously to different regions of a precursor molecule. Expand
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. Expand