EC Number |
Protein Variants |
Reference |
---|
3.4.24.B19 | E540Q |
inactive |
719236 |
3.4.24.B19 | E541Q |
efficiently precipitates Yta10(1-161)-DHFRmut |
670047 |
3.4.24.B19 | E541Q |
point mutation, inactive |
653335 |
3.4.24.B19 | E541Q |
proteolytically inactive |
681916 |
3.4.24.B19 | E541Q |
site-directed mutagenesis, exchange in the active site, no complementation of deficient mutant cell DELTAyme1 |
650958 |
3.4.24.B19 | H486Y |
inactive |
-, 754234 |
3.4.24.B19 | K327R |
point mutation at the ATP-binding site, catalytically inactive |
653335 |
3.4.24.B19 | more |
construction of inactive mutant by site-directed mutagenesis in the ATP and Zn2+ binding domains, inactivation of the enzyme causes several distinct phenotypes: an increased rate of DNA escape from mitochondria, temperature-sensitive growth on nonfermentable carbon sources, extremely slow growth when mitochondrial DNA is completely absent from the cell, and altered morphology of the mitochondrial compartment |
653183 |
3.4.24.B19 | more |
inactivation of the enzyme causes pleiotropic defects, including impaired respiration and aberrant mitochondrial morphology |
649814 |
3.4.24.B19 | more |
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 |
670047 |