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Literature summary for 3.4.24.B19 extracted from

  • Graef, M.; Langer, T.
    Substrate specific consequences of central pore mutations in the i-AAA protease Yme1 on substrate engagement (2006), J. Struct. Biol., 156, 101-108.
    View publication on PubMed
Search for more literature for 3.4.24.B19

Application

Application Comment Organism
degradation essential function of the central pore loop for the ATP-dependent translocation of membrane proteins into a proteolytic cavity formed by AAA protease More

Cloned(Commentary)

Cloned (Comment) Organism
expressed in deltayme1 yeast strain More

Protein Variants

Protein Variants Comment Organism
E541Q efficiently precipitates Yta10(1-161)-DHFRmut More
additional information mutants of Yme1, which harbour aromatic, aliphatic, polar and charged residues at position 354 of Yme1, accumulate at similar levels in mitochondria as wild type, when expressed in deltayme1 yeast strain under the control of the endogenous Yme1 promoter, whereas deltayme1 cells do not grow on non-fermentable carbon sources at elevated temperature. Cell growth is restored upon expression of wild type Yme1 harbouring a tyrosine residue at position 354. Replacement by phenylalanine or tryptophan does not impair cell growth under these conditions. The introduction of aliphatic residues allows cell growth to a different extent, improved cell growth with increasing hydrophobicity of the aliphatic amino acids, polar or charged amino acid residues do not support respiratory growth More
additional information mutation in the Walker A- or Walker B-motif within the AAA domain strongly impairs the association of newly synthesized Cox2 with Yme1 More
Y354S weak activity against Cox2, precipitates Yta10(1-161)-DHFRmut More
Y354T weak activity against Cox2 More
Y354W fully restored respiratory growth, only partial activity against Cox2 More

Localization

Localization Comment Organism GeneOntology No. Textmining
inner membrane
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 More
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mitochondrion
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 More 5739
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Organism

Organism UniProt Comment Textmining
More
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 expressed from pRS314 vector
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Cox2 + H2O
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 More ?
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 ?
membrane protein + H2O proteolytic activity depends on the presence of hydrophobic amino acid residues at position 354 within the pore loop of Yme1 More ?
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 ?
Yta10(1-161)-DHFRmut + H2O
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 More ?
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 ?

Synonyms

Synonyms Comment Organism
YME1
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 More