CLONING OF THE GLUTAMINE - FRUCTOSE-6-PHOSPHATE AMIDOTRANSFERASE GENE FROM YEAST - PHEROMONAL REGULATION OF ITS TRANSCRIPTION

  • 25 May 1989
    • journal article
    • research article
    • Vol. 264  (15) , 8753-8758
Abstract
The activity of the amino sugar-synthesizing enzyme L-glutamine:D-fructose-6-phosphate amidotransferase (EC 2.6.1.16) in haploid a cells of Saccharomyces cerevisiae increases 1.7-fold after .alpha. factor addition. The gene (the gene should be called GFA1 for glutamine:fructose-6-phosphate amidotransferase) for the enzyme has been cloned by complementing the gcn1 mutation (Whelan, W.L., Ballou, C.E. (1975) J. Bacteriol. 125, 1545-1557). Its expression is increased 2-3 times within 15 min when the mating pheromone is added. The gene codes for a protein of 716 amino acids in length. It is highly homologous (64%) to the corresponding gene of Escherichia coli, except for a sequence coding for 83 amino acids (numbers 204-286), which is lacking in E. coli. The aminoterminal region of the coding sequence als shows a high degree of homology tothe corresponding sequence of the E. coli and S. cereviaiae L-glutamine:phosphoribosylpyrophosphate amidotransferase. In the promotor region of the S. cerevisiae L-glutamine:D-fructose-6-phosphate amidotransferase gene th heptanucleotide "TGAAACA," shown tobe required for pheromone control of transcription (Kronstad, J.W., Holly, J. A., and MacKay, V. L. (1987) Cell 50, 369-377), is present six times.

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