High impact information on ADH3

• We demonstrated that the first intron in the A. nidulans ADH3 gene was not efficiently spliced in S. cerevisiae whereas the promoter region was utilized weakly [1].
• Random amino acid changes were produced in the wild-type presequence by bisulfite mutagenesis of the ADH3 gene [2].
• Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae [3].
• A strain containing a null allele of ADH3 did not have a detectably altered phenotype [3].
• A genomic clone of CHL12 was isolated and used to map its physical position on the right arm of chromosome XIII near the ADH3 locus [4].

Associations of ADH3 with chemical compounds

• Deletion of ADH3, encoding mitochondrial alcohol dehydrogenase, did not affect respiratory growth in aerobic, glucose-limited chemostat cultures [5].
• This chromosome contains the ADH2 and ADH3 loci, that code for the ADHII and ADHIII isoenzymes of alcohol dehydrogenase, which are involved in ethanol oxidative utilization during biological ageing of wines [6].
• The methyl formate synthase activity of C. boidinii was found in the mitochondrial fraction in subcellular fractionation experiments, suggesting that methyl formate synthase is a homolog of Saccharomyces cerevisiae Adh3p [7].

Other interactions of ADH3

• However, when both ADH3 and NDI1 were deleted, metabolism became respirofermentative, indicating that the ethanol-acetaldehyde shuttle is essential for respiratory growth of the ndi1 delta mutant [5].
• (v) Ethanol induction, as seen for ACS2, ADH3 and MDH1, might be mediated via the sequence CGGSGCCGRAG [8].

References