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The extracellular acid protease gene of Yarrowia lipolytica: sequence and pH-regulated transcription

1996; Microbiology Society; Volume: 142; Issue: 10 Linguagem: Inglês

10.1099/13500872-142-10-2913

1465-2080

Thomas W. Young, A. Wadeson, David Glover, R V Quincey, Mike Butlin, E. A. Kamei,

RNA and protein synthesis mechanisms

The gene encoding an acid extracellular protease (AXP) from Yarrowia lipolytica (Candida olea) 148 was cloned and the complete nucleotide sequence was determined. The amino acid sequence deduced from the nucleotide 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 potential N-glycosylation sites. The mature extracellular enzyme is produced 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 and alkaline extracellular protease genes of Y. lipolytica 148 is regulated by the pH of culture.