Summary: secretes an inducible acid protease (ACP) when cultivated in the presence of bovine serum albumin as the sole nitrogen source. In order to clone the ACP gene () of , a genomic library was screened with as the probe. Two different ORFs, and , were found to hybridize with the contained a DNA sequence in agreement with the N-terminal amino acid sequence of ACP isolated from culture supernatants. was shown to be expressed and functional in a acid protease mutant () and with SDS-PAGE the protein product showed the same mobility as the ACP secreted by . These results imply that encodes the ACP. The deduced amino acid sequence of is similar to the amino acid sequence of proteases of the pepsin family. As in the case of the and , the 5” extremity of revealed a propeptide containing two Lys-Arg amino acid pairs that have been identified as peptidase processing sites in several yeast-secreted peptides and protein precursors. As judged from the deduced amino acid sequences, the product would be similar to that of ; however, a protein corresponding to was not found in supernatants from liquid cultures. In addition, did not complement the mutant. We conclude that is a pseudogene or serves an as yet unidentified function.


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