Disease relevance of ADE8

• The E. coli GAR transformylase shows greater homology to the GAR transformylase domain of the trifunctional Gart polypeptide of Drosophila than to the single GAR transformylase of Saccharomyces [1].

High impact information on ADE8

• Supporting data include homology between the AIRS and GART domains of this gene and the published sequence of these domains from other organisms, and localization of the cloned gene to human chromosome 21, where the GART gene has been shown to map [2].
• Second, the GART-encoding region of the mutant was cloned, inserted into a yeast-Escherichia coli shuttle vector, and used to transform mutant yeast [3].
• Insertion of (CAG)50 or (CTG)50 repeats into a promoter that drives expression of the reporter gene ADE8 results in loss of expression and white colony color [4].
• Mapping data indicate that STE14 resides on chromosome IV, tightly linked to ADE8 [5].
• The meiotic behavior of two graded series of deletion mutations in the ADE8 gene in Saccharomyces cerevisiae was analyzed to investigate the molecular basis of meiotic recombination [6].

Biological context of ADE8

• The ADE8 and HIS3 genes have been cloned together on a high-copy vector (pRS4213), providing a plasmid for red-white colour screening in the ade2 Delta 0 ade8 Delta 0 strains we have generated [7].
• Two new pRS family Saccharomyces cerevisiae-Escherichia coli shuttle vectors containing ADE8 (one low-copy, pRS4110, and one high-copy, pRS4210) have been produced for use in conjunction with the new strains [7].
• We have determined the complete DNA sequence of a segment derived from Drosophila melanogaster that complements a yeast adenine-8 (ade8) mutation [8].
• Thus, these results suggest that the 10-formyl-THF binding site differs significantly between the GAR transformylase and 10-formyl-THF synthetase families, and that the conserved aspartate plays different roles in the two enzymes [9].
• This sequence, and the predicted 789 amino acid sequence encoded, both show a high degree of homology with the functionally equivalent ade5,7 gene sequence of Saccharomyces cerevisiae (approx. 60% overall in both cases) and Gart gene sequences of Drosophila melanogaster [10].

Associations of ADE8 with chemical compounds

• These results, together with the sequence of the S. cerevisiae ADE8 gene encoding glycinamide ribotide transformylase, show that the entire Drosophila large polypeptide can be accounted for by the three enzymatic activities [11].
• In the yeast Saccharomyces cerevisiae the ade2, and/or the ade1, mutation in the adenine biosynthetic pathway leads to the accumulation of a cell-limited red pigment, while epistatic mutations in the same pathway, i.e. ade8, preclude this phenomenon, resulting in normal white colonies [12].
• This construction results in ADE8+ function that responds to glucose and ethanol in a manner similar to that for the chromosomal ADHI gene, as determined by a simple quantitative color assay for ADE8+ function [8].
• The isolation of a human cDNA encoding the multifunctional protein containing GAR synthetase, AIR synthetase, and GAR transformylase by functional complementation of purine auxotrophy in yeast has been reported [13].

Other interactions of ADE8

• A plasmid containing the ADE3/ADE8 gene and the wild-type gene of interest must then be transformed into the strain, which results in red colonies with white sectors where the plasmid has been lost [14].
• The Saccharomyces cerevisiae ADE5,7 protein is homologous to overlapping Drosophila melanogaster Gart polypeptides [11].
• This recombinational event is detected as a phenotypic shift from red to white colonies, due to the mitotic loss of the plasmid portion containing the yeast ADE8 gene in a recipient ade1 ade2 ade8 genetic background [15].
• A 2 mu plasmid carrying the gene was integrated and mapped to chromosome IV, between trp4 and ade8, by the method of marker loss [16].

References