High impact information on MET7

• Thus, the combination of FPGS with these folate-mediated reactions can supply each compartment with the polyglutamylated folate coenzymes required for the reactions of C1 metabolism [1].
• The function of each enzyme was demonstrated by complementation of yeast mutants deficient in DHFS or FPGS activity, and by measuring in vitro glutamate incorporation into dihydrofolate or tetrahydrofolate [1].
• In organisms that synthesize tetrahydrofolate de novo, dihydrofolate synthetase (DHFS) and folylpolyglutamate synthetase (FPGS) catalyze the attachment of glutamate residues to the folate molecule [1].
• In contrast, FPGS is present as distinct isoforms in the mitochondria, the cytosol, and the chloroplast [1].
• Immunological crossreactivity of eukaryotic C1-tetrahydrofolate synthase and prokaryotic 10-formyltetrahydrofolate synthetase [2].

Biological context of MET7

• We also mapped the DFR1 gene to a position 1.4 cM proximal to the MET7 locus on chromosome XV [3].
• The met7 mutant becomes petite under normal growth conditions but can be maintained with a grande phenotype if the strain is tup and all media are supplemented with dTMP [4].
• O5248 is a probable folypolyglutamate synthetase, having two structural homologs already sequenced in the yeast genome [5].

Associations of MET7 with chemical compounds

• We show also that folylpolyglutamate synthetase, which catalyzes the extension of the glutamate chains of the folate coenzymes, is encoded by the MET7 gene [6].
• A met7 gly1 strain is auxotrophic for glycine when grown on glucose but prototrophic when grown on glycerol [4].
• In order to determine the metabolic roles of both forms of folylpolyglutamate synthetase, we disrupted the met7 gene and determined that the strain is a methionine auxotroph and an adenine and thymidine auxotroph when grown in the presence of sulfanilamide [4].
• A met7 ser1 strain cannot use glycine to suppress the serine auxotrophy of the ser1 phenotype [4].

References