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Gene Review

TOM6  -  Tom6p

Saccharomyces cerevisiae S288c

Synonyms: ISP6, MOM8B, Mitochondrial import receptor subunit TOM6, Mitochondrial import site protein ISP6, Translocase of outer membrane 6 kDa subunit, ...
 
 
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High impact information on TOM6

  • Tom40 is an essential constituent of the GIP, whereas Tom6 and Tom7 modulate the assembly and dissociation of the Tom machinery [1].
  • Immunoprecipitation of the gene product, ISP42p, from mitochondria solubilized under mild conditions reveals a multi-protein complex containing ISP6p and ISP42p [2].
  • Genetic and biochemical characterization of ISP6, a small mitochondrial outer membrane protein associated with the protein translocation complex [2].
  • This novel gene, denoted ISP6, encodes a 61 amino acid integral membrane protein of the mitochondrial outer membrane, which is oriented with its amino-terminus facing the cytosol [2].
  • Tom7 and Tom6 have been found in Neurospora and yeast, Tom5 has been found so far only in the latter organism [3].
 

Biological context of TOM6

  • Biogenesis of ISP6, a small carboxyl-terminal anchored protein of the receptor complex of the mitochondrial outer membrane [4].
  • The insertion pathway of these proteins shares a common binding site with the general import pathway as the assembly of both Tom6 and Tom7 was competed by a matrix-destined precursor protein [5].
  • In vivo this fusion protein lost its ability to suppress the temperature-sensitive phenotype of an isp42 mutant, while the other fusion protein DHFR-6, which was found targeted correctly to mitochondria, suppressed the mutant as well as the wild-type ISP6 [4].
 

Physical interactions of TOM6

  • Tom40 exists in a homo-oligomeric assembly and dynamically interacts with Tom6 [6].
  • In addition, Tom6 was observed to interact with Tom22 in a manner that depends on the presence of preproteins in transit [5].
 

Other interactions of TOM6

  • Disruption of the ISP6 gene is without apparent effect in wild type yeast cells, but is lethal in temperature-sensitive isp42 mutants [2].

References

  1. Tom5 functionally links mitochondrial preprotein receptors to the general import pore. Dietmeier, K., Hönlinger, A., Bömer, U., Dekker, P.J., Eckerskorn, C., Lottspeich, F., Kübrich, M., Pfanner, N. Nature (1997) [Pubmed]
  2. Genetic and biochemical characterization of ISP6, a small mitochondrial outer membrane protein associated with the protein translocation complex. Kassenbrock, C.K., Cao, W., Douglas, M.G. EMBO J. (1993) [Pubmed]
  3. Role of Tom5 in maintaining the structural stability of the TOM complex of mitochondria. Schmitt, S., Ahting, U., Eichacker, L., Granvogl, B., Go, N.E., Nargang, F.E., Neupert, W., Nussberger, S. J. Biol. Chem. (2005) [Pubmed]
  4. Biogenesis of ISP6, a small carboxyl-terminal anchored protein of the receptor complex of the mitochondrial outer membrane. Cao, W., Douglas, M.G. J. Biol. Chem. (1995) [Pubmed]
  5. Assembly of Tom6 and Tom7 into the TOM core complex of Neurospora crassa. Dembowski, M., Kunkele, K.P., Nargang, F.E., Neupert, W., Rapaport, D. J. Biol. Chem. (2001) [Pubmed]
  6. Dynamics of the TOM complex of mitochondria during binding and translocation of preproteins. Rapaport, D., Künkele, K.P., Dembowski, M., Ahting, U., Nargang, F.E., Neupert, W., Lill, R. Mol. Cell. Biol. (1998) [Pubmed]
 
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