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Gene Review

AFG3  -  AAA family ATPase AFG3

Saccharomyces cerevisiae S288c

Synonyms: ATPase family gene 3 protein, Mitochondrial respiratory chain complexes assembly protein AFG3, Tat-binding homolog 10, YER017C, YTA10
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High impact information on AFG3

  • The mitochondrial members of the highly conserved AAA family, Yta10p and Yta12p, constitute a membrane-embedded complex of about 850 kDa [1].
  • Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria [2].
  • Deletion of YTA10 or YTA12 impairs degradation of non-assembled inner membrane proteins and assembly of respiratory chain complexes [3].
  • Mutational inactivation of the proteolytic function of the matrix-localized Yta10p (Afg3p) AAA-protease partially stabilizes Cox2p in an mss2 mutant but does not restore assembly of cytochrome oxidase [4].
  • Here we show that both Mrs2 and Yta10 transiently accumulate as sorting intermediates in the matrix before they integrate into the inner membrane [5].

Biological context of AFG3

  • Three metalloproteases belonging to the AAA superfamily (Yme1p, Afg3p and Rca1p) are involved in protein turnover and respiratory chain complex assembly in the yeast inner mitochondrial membrane [6].
  • Cells harbouring proteolytically inactive forms of both Yta10p and Yta12p are respiratory deficient and exhibit a pleiotropic phenotype similar to Deltayta10 and Deltayta12 cells [3].
  • Yta10p, as deduced from the nucleotide sequence, is 761 amino acids in length (predicted molecular mass 84.5 kDa) [7].
  • We report here that Yta10p is a yeast mitochondrial protein and that import is dependent on a membrane potential and accompanied by processing to a protein of approximately 73 kDa [7].
  • Yta10p-dependent degradation requires divalent metal ions and the hydrolysis of ATP [8].

Anatomical context of AFG3


Other interactions of AFG3

  • Neither Afg3p nor Yme1p is responsible for the degradation of Cox subunits [9].
  • Three genes for mitochondrial proteins suppress null-mutations in both Afg3 and Rca1 when over-expressed [10].


  1. The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Arlt, H., Tauer, R., Feldmann, H., Neupert, W., Langer, T. Cell (1996) [Pubmed]
  2. Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon. Rep, M., van Dijl, J.M., Suda, K., Schatz, G., Grivell, L.A., Suzuki, C.K. Science (1996) [Pubmed]
  3. The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease. Arlt, H., Steglich, G., Perryman, R., Guiard, B., Neupert, W., Langer, T. EMBO J. (1998) [Pubmed]
  4. Peripheral mitochondrial inner membrane protein, Mss2p, required for export of the mitochondrially coded Cox2p C tail in Saccharomyces cerevisiae. Broadley, S.A., Demlow, C.M., Fox, T.D. Mol. Cell. Biol. (2001) [Pubmed]
  5. Insertion of bitopic membrane proteins into the inner membrane of mitochondria involves an export step from the matrix. Baumann, F., Neupert, W., Herrmann, J.M. J. Biol. Chem. (2002) [Pubmed]
  6. The mitochondrial inner membrane AAA metalloprotease family in metazoans. Juhola, M.K., Shah, Z.H., Grivell, L.A., Jacobs, H.T. FEBS Lett. (2000) [Pubmed]
  7. Yta10p, a member of a novel ATPase family in yeast, is essential for mitochondrial function. Tauer, R., Mannhaupt, G., Schnall, R., Pajic, A., Langer, T., Feldmann, H. FEBS Lett. (1994) [Pubmed]
  8. Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria. Pajic, A., Tauer, R., Feldmann, H., Neupert, W., Langer, T. FEBS Lett. (1994) [Pubmed]
  9. Absence of the mitochondrial AAA protease Yme1p restores F0-ATPase subunit accumulation in an oxa1 deletion mutant of Saccharomyces cerevisiae. Lemaire, C., Hamel, P., Velours, J., Dujardin, G. J. Biol. Chem. (2000) [Pubmed]
  10. Three genes for mitochondrial proteins suppress null-mutations in both Afg3 and Rca1 when over-expressed. Rep, M., Nooy, J., Guélin, E., Grivell, L.A. Curr. Genet. (1996) [Pubmed]
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