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PAM18  -  Pam18p

Saccharomyces cerevisiae S288c

Synonyms: Mitochondrial import inner membrane translocase subunit TIM14, Presequence translocated-associated motor subunit PAM18, TIM14, YLR008C
 
 
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High impact information on PAM18

  • 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 [1].
  • The novel J-protein (encoded by PAM18/YLR008c/TIM14) is required for the interaction of mtHsp70 with Tim44 and protein translocation into the matrix [2].
  • Mitochondria from cells depleted of Tim14 are deficient in the import of proteins mediated by the TIM23 complex [3].
  • TIM14 genes are present in the genomes of virtually all eukaryotes [3].
  • Neither substantial reduction in the ability of Pam18 to stimulate Ssc1's ATPase activity, nor the presence of an active J domain in Pam16, had deleterious effects on cell growth, indicating the lack of importance of two of these biochemical properties [4].
 

Biological context of PAM18

  • However, a previously unstudied essential gene, PAM18, encodes an 18-kDa protein that contains a J domain and is localized to the mitochondrial inner membrane [5].
  • Tim14 is a component of the yeast inner mitochondrial membrane presequence translocase, suggesting that the unique phenotype of DCMA may be the result of defective mitochondrial protein import [6].
 

Regulatory relationships of PAM18

  • Mdj2 is expressed at a lower level compared with Tim14, and its complex with Tim16 is less stable [7].
 

Other interactions of PAM18

  • Tim16 is a J-like protein that forms a stable subcomplex with Tim14 and recruits it to the translocase [7].
  • The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2 [7].
  • The presequence translocase-associated protein import motor (PAM) contains four essential subunits: the matrix heat shock protein 70 (mtHsp70) and its three cochaperones Mge1, Tim44 and Pam18 [8].
  • In the present study we analyzed Mdj2 and compared it with Tim14 [7].

References

  1. 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]
  2. A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria. Truscott, K.N., Voos, W., Frazier, A.E., Lind, M., Li, Y., Geissler, A., Dudek, J., Müller, H., Sickmann, A., Meyer, H.E., Meisinger, C., Guiard, B., Rehling, P., Pfanner, N. J. Cell Biol. (2003) [Pubmed]
  3. Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria. Mokranjac, D., Sichting, M., Neupert, W., Hell, K. EMBO J. (2003) [Pubmed]
  4. Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane. D'Silva, P.R., Schilke, B., Walter, W., Craig, E.A. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  5. J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix. D'Silva, P.D., Schilke, B., Walter, W., Andrew, A., Craig, E.A. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  6. Mutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like condition. Davey, K.M., Parboosingh, J.S., McLeod, D.R., Chan, A., Casey, R., Ferreira, P., Snyder, F.F., Bridge, P.J., Bernier, F.P. J. Med. Genet. (2006) [Pubmed]
  7. The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2. Mokranjac, D., Sichting, M., Popov-Celeketić, D., Berg, A., Hell, K., Neupert, W. J. Biol. Chem. (2005) [Pubmed]
  8. Pam16 has an essential role in the mitochondrial protein import motor. Frazier, A.E., Dudek, J., Guiard, B., Voos, W., Li, Y., Lind, M., Meisinger, C., Geissler, A., Sickmann, A., Meyer, H.E., Bilanchone, V., Cumsky, M.G., Truscott, K.N., Pfanner, N., Rehling, P. Nat. Struct. Mol. Biol. (2004) [Pubmed]
 
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