We have identified in the promoter of the FBP1 gene from Saccharomyces cerevisiae, which codes for fructose-1,6-bisphosphatase, two elements which can form specific DNAprotein complexes and which confer glucose-repressed expression to an heterologous reporter gene. Complex formation and activation of transcription by either element require a functional CAT1 gene and are not blocked by a hap2-1 mutation, although this mutation interferes with maximal expression of the FBP1 gene. A sequence from one of the elements acts as a weak upstream activating sequence, but its activity can be stimulated up to 10-fold by neighboring sequences. A further element of the promoter has been characterized, which forms a specific DNAprotein complex only when a nuclear extract from derepressed cells is used. This element does not activate transcription in a heterologous promoter. The DNA sequences of the three elements involved in protein binding, defined by DNase I footprinting, have no homology with consensus sequences for known activating factors.

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