was shown to possess a secreted aspartic proteinase gene family of at least four members . Within the family there was 77-87% identity at the nucleotide level and 76-92% identity at the amino acid level. Transcription of three members of this gene family required an acidic medium (pH<4.5) and either nitrogen or sulphur derepression. Regulation was co-ordinate and hierarchical, with pH occupying the higher position in the hierarchy. Exogenous protein increased transcript levels, probably via the provision of metabolic intermediates rather than by direct induction of gene expression. was not expressed under these conditions. SAP1-SAP4 are predicted to have almost identical substrate-binding sites and therefore substrate specificity. It is proposed that exist to provide amplified expression of the secreted aspartic proteinase because protein, an important secondary nitrogen source for this fungus, requires extensive degradation to make its nitrogen available to the cell.


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