THE EXTRACELLULAR ACID PROTEASE GENE OF YARROWIA-LIPOLYTICA - SEQUENCE AND PH-REGULATED TRANSCRIPTION

The gene encoding an acid extracellular protease (AXP) from Yarrowia l ipolytica (Candida olea) 148 was cloned and the complete nucleotide se quence was determined. The amino acid sequence deduced from the nucleo tide sequence reveals that the mature AXP consists of 353 amino acids with an M(r) of 37427. The gene also encodes a putative 17 amino acid hydrophobic prepeptide and a 27 amino acid propeptide containing no po tential N-glycosylation sites. The mature extracellular enzyme is prod uced by cleavage between Phe and Ala. AXP is a member of the aspartyl family of proteases. AXP shows homology to proteases of several fungal genera and to human progastricin. The coding sequence is preceded by a potential regulatory region of 1982 bp. Transcription of both AXP an d alkaline extracellular protease genes of Y. lipolytica 148 is regula ted by the pH of culture.