The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

TIM17  -  protein transporter TIM17

Saccharomyces cerevisiae S288c

Synonyms: J0648, MIM17, MPI2, Mitochondrial import inner membrane translocase subunit TIM17, Mitochondrial inner membrane protein MIM17, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of TIM17

  • If Tim17p, another inner membrane import component, is overexpressed along with Tim23Cp, the toxicity of Tim23Cp is largely reversed and the Tim23-1 protein no longer disappears [1].
 

High impact information on TIM17

  • Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17 [2].
  • Tim17 is crucial for the switch by performing two separable functions: promotion of inner membrane insertion and binding of Pam18 to form the functional TIM-PAM complex [2].
  • Two known components, MIM23 and MIM17, and two novel components, MIM33 and MIM14, were found as constituents of this complex [3].
  • We conclude that the hydrophobic domain encoded by tim23C targets Tim23p to the mitochondria and mediates the direct interaction between Tim23p and Tim17p [1].
  • Moreover, expression of the truncated Tim17 variant led to a dominant negative effect on the mitochondrial membrane potential [4].
 

Biological context of TIM17

 

Anatomical context of TIM17

  • Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria [4].
 

Associations of TIM17 with chemical compounds

  • The replacement of these positions by positively charged residues results in a strong growth defect, which can be cured by reverting two conserved positive charges into aspartate residues between transmembrane domains two and three of Tim17 [4].
  • By an alanine-scanning approach we identified two conserved negative charges in the N terminus of Tim17 as critical for Tim17 function [4].
 

Physical interactions of TIM17

  • Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules [1].
 

Regulatory relationships of TIM17

  • On the basis of these observations we propose that charged residues in Tim17 are critical for the preprotein-induced gating of the TIM23 translocase [4].
 

Other interactions of TIM17

  • Preproteins carrying amino-terminal signals mainly use Tom20, the general import pore (GIP) complex and the Tim23-Tim17 complex [8].
  • A screening for yeast mutants impaired in mitochondrial protein import led to the identification of two genes (MPII and MPI2) encoding the essential components MIM44 and MIM17 of the inner membrane import machinery [9].

References

  1. Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules. Ryan, K.R., Leung, R.S., Jensen, R.E. Mol. Cell. Biol. (1998) [Pubmed]
  2. Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Chacinska, A., Lind, M., Frazier, A.E., Dudek, J., Meisinger, C., Geissler, A., Sickmann, A., Meyer, H.E., Truscott, K.N., Guiard, B., Pfanner, N., Rehling, P. Cell (2005) [Pubmed]
  3. The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system. Berthold, J., Bauer, M.F., Schneider, H.C., Klaus, C., Dietmeier, K., Neupert, W., Brunner, M. Cell (1995) [Pubmed]
  4. Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria. Meier, S., Neupert, W., Herrmann, J.M. J. Biol. Chem. (2005) [Pubmed]
  5. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane. Bömer, U., Meijer, M., Maarse, A.C., Hönlinger, A., Dekker, P.J., Pfanner, N., Rassow, J. EMBO J. (1997) [Pubmed]
  6. The preprotein translocase of the mitochondrial inner membrane: function and evolution. Rassow, J., Dekker, P.J., van Wilpe, S., Meijer, M., Soll, J. J. Mol. Biol. (1999) [Pubmed]
  7. Functional and physical interactions of components of the yeast mitochondrial inner-membrane import machinery (MIM). Blom, J., Dekker, P.J., Meijer, M. Eur. J. Biochem. (1995) [Pubmed]
  8. 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]
  9. Identification of MIM23, a putative component of the protein import machinery of the mitochondrial inner membrane. Dekker, P.J., Keil, P., Rassow, J., Maarse, A.C., Pfanner, N., Meijer, M. FEBS Lett. (1993) [Pubmed]
 
WikiGenes - Universities