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Gene Review

PIM1  -  ATP-dependent Lon protease PIM1

Saccharomyces cerevisiae S288c

Synonyms: LON, Lon protease homolog, mitochondrial, YBL022C, YBL0440
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Disease relevance of PIM1


High impact information on PIM1

  • Yeast cells lacking a functional LON gene contained a nonfunctional mitochondrial genome, were respiratory-deficient, and lacked an ATP-dependent proteolytic activity present in the mitochondria of Lon+ cells [3].
  • Transcripts of COXI and COB genes harboring multiple introns are degraded in the absence of PIM1 [4].
  • The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondria [4].
  • The identification of a multicopy suppressor, which stabilizes mtDNA in the absence of PIM1, enabled us to characterize novel functions of PIM1 protease during mitochondrial biogenesis [4].
  • Moreover, deficiencies in the splicing of COXI and COB transcripts, which appear to be restricted to introns encoding mRNA maturases, were observed in cells lacking the PIM1 gene [4].

Biological context of PIM1

  • The ATP-dependent PIM1 protease, a Lon-like protease localized in the mitochondrial matrix, is required for mitochondrial genome integrity in yeast [4].
  • These results establish multiple, essential functions of the ATP-dependent PIM1 protease during mitochondrial gene expression [4].
  • Disruption of the PIM1 gene results in an osmoremediable thermosensitive phenotype reminiscent of that observed in mutants affected in the MAPK Slt2/ Mpk1 of Saccharomyces cerevisiae, which is involved in ensuring cell wall integrity [2].
  • These results demonstrate overlapping substrate specificities of PIM1 and the m-AAA protease, and they assign a central role to the mtHsp70 system during the degradation of misfolded polypeptides by both proteases [5].
  • PRP20 is related, both in structure and function, to the RCC1 gene of mammals and the PIM1 gene of Schizosaccharomyces pombe, both of which appear to regulate entry into mitosis and chromosome condensation [6].

Associations of PIM1 with chemical compounds

  • Furthermore, pim1 mutants are hypersensitive to caffeine and cell wall-destabilising compounds [2].

Physical interactions of PIM1

  • However, unlike misfolded proteins associated with mt-hsp70, hsp78-bound polypeptides are not efficiently degraded by the ATP-dependent PIM1 protease [7].

Other interactions of PIM1

  • In the absence of functional mt-hsp70 or Mdj1p misfolded proteins either remain associated with mt-hsp70 or form aggregates and thereby are no longer substrates for PIM1 protease [8].
  • Mitochondrial DNA instability mutants of the bifunctional protein Ilv5p have altered organization in mitochondria and are targeted for degradation by Hsp78 and the Pim1p protease [9].


  1. PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function in the yeast Saccharomyces cerevisiae. Van Dyck, L., Pearce, D.A., Sherman, F. J. Biol. Chem. (1994) [Pubmed]
  2. Pim1, a MAP kinase involved in cell wall integrity in Pichia pastoris. Cosano, I.C., Martín, H., Flández, M., Nombela, C., Molina, M. Mol. Genet. Genomics (2001) [Pubmed]
  3. Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration. Suzuki, C.K., Suda, K., Wang, N., Schatz, G. Science (1994) [Pubmed]
  4. The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondria. van Dyck, L., Neupert, W., Langer, T. Genes Dev. (1998) [Pubmed]
  5. ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system. Savel'ev, A.S., Novikova, L.A., Kovaleva, I.E., Luzikov, V.N., Neupert, W., Langer, T. J. Biol. Chem. (1998) [Pubmed]
  6. Defects in mRNA 3'-end formation, transcription initiation, and mRNA transport associated with the yeast mutation prp20: possible coupling of mRNA processing and chromatin structure. Forrester, W., Stutz, F., Rosbash, M., Wickens, M. Genes Dev. (1992) [Pubmed]
  7. Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. Schmitt, M., Neupert, W., Langer, T. EMBO J. (1995) [Pubmed]
  8. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. Wagner, I., Arlt, H., van Dyck, L., Langer, T., Neupert, W. EMBO J. (1994) [Pubmed]
  9. Mitochondrial DNA instability mutants of the bifunctional protein Ilv5p have altered organization in mitochondria and are targeted for degradation by Hsp78 and the Pim1p protease. Bateman, J.M., Iacovino, M., Perlman, P.S., Butow, R.A. J. Biol. Chem. (2002) [Pubmed]
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