Tw. Young et al., THE EXTRACELLULAR ACID PROTEASE GENE OF YARROWIA-LIPOLYTICA - SEQUENCE AND PH-REGULATED TRANSCRIPTION, Microbiology, 142, 1996, pp. 2913-2921
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.