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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

TIM22  -  Tim22p

Saccharomyces cerevisiae S288c

Synonyms: D0884, Mitochondrial import inner membrane translocase subunit TIM22, YDL217C
 
 
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High impact information on TIM22

  • Import of proteins of the AAC family is independent of Tim23, and import of matrix targeting signals containing preproteins is independent of Tim22 [1].
  • Tim10p readily dissociated from the complex and was required to transport carrier precursors across the outer membrane; Tim12p was firmly bound to Tim22p and mediated the insertion of carriers into the inner membrane [2].
  • The soluble Tim9p-Tim10p (Tim, translocase of inner membrane) complex of the mitochondrial intermembrane space mediates the import of the carrier proteins and is a component of the TIM22 import system [3].
  • Thus, biogenesis of the Tim23.17 complex depends on the Tim22 complex, which is the translocase identified as mediating the import of carrier proteins [4].
  • Finally, the tim54-1 mutation destabilizes the Tim22 protein, but not Tim23p or Tim17p [5].
 

Anatomical context of TIM22

 

Physical interactions of TIM22

  • A cryptic matrix targeting signal of the yeast ADP/ATP carrier normally inserted by the TIM22 complex is recognized by the TIM23 machinery [8].
 

Other interactions of TIM22

  • We suggest that the 70-kDa complexes facilitate import, similar to the outer membrane receptors of the TOM (hetero-oligomeric translocase of the outer membrane) complex, and the essential role of Tim9p and Tim10p may be to mediate protein insertion in the inner membrane with the TIM22 complex [9].
  • The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane [5].
  • The TIM22 protein import pathway of the yeast mitochondrion contains several components, including a family of five proteins (Tim8p, -9p, -10p, -12p, and -13p [Tim, for translocase of inner membrane]) that are located in the intermembrane space and are 25% identical [9].
  • We suggest that Tim18p functions in the assembly and stabilization of the TIM22 complex but does not directly participate in protein insertion into the inner membrane [6].
  • We report that import of the preprotein of Tim22 requires Tom20, although it uses the carrier Tim route [10].

References

  1. Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22. Sirrenberg, C., Bauer, M.F., Guiard, B., Neupert, W., Brunner, M. Nature (1996) [Pubmed]
  2. Import of mitochondrial carriers mediated by essential proteins of the intermembrane space. Koehler, C.M., Jarosch, E., Tokatlidis, K., Schmid, K., Schweyen, R.J., Schatz, G. Science (1998) [Pubmed]
  3. The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier. Curran, S.P., Leuenberger, D., Oppliger, W., Koehler, C.M. EMBO J. (2002) [Pubmed]
  4. Biogenesis of Tim23 and Tim17, integral components of the TIM machinery for matrix-targeted preproteins. Káldi, K., Bauer, M.F., Sirrenberg, C., Neupert, W., Brunner, M. EMBO J. (1998) [Pubmed]
  5. The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane. Kerscher, O., Holder, J., Srinivasan, M., Leung, R.S., Jensen, R.E. J. Cell Biol. (1997) [Pubmed]
  6. Tim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane. Koehler, C.M., Murphy, M.P., Bally, N.A., Leuenberger, D., Oppliger, W., Dolfini, L., Junne, T., Schatz, G., Or, E. Mol. Cell. Biol. (2000) [Pubmed]
  7. The dynamic dimerization of the yeast ADP/ATP carrier in the inner mitochondrial membrane is affected by conserved cysteine residues. Dyall, S.D., Agius, S.C., De Marcos Lousa, C., Trezeguet, V., Tokatlidis, K. J. Biol. Chem. (2003) [Pubmed]
  8. A cryptic matrix targeting signal of the yeast ADP/ATP carrier normally inserted by the TIM22 complex is recognized by the TIM23 machinery. Vergnolle, M.A., Sawney, H., Junne, T., Dolfini, L., Tokatlidis, K. Biochem. J. (2005) [Pubmed]
  9. The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex. Murphy, M.P., Leuenberger, D., Curran, S.P., Oppliger, W., Koehler, C.M. Mol. Cell. Biol. (2001) [Pubmed]
  10. Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathway. Kurz, M., Martin, H., Rassow, J., Pfanner, N., Ryan, M.T. Mol. Biol. Cell (1999) [Pubmed]
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