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

Elizabeth A. Kamei

School of Biochemistry, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK

¹Author for correspondence: Thomas W. Young. Tel: +44 121 414 5437. Fax: +44 121 414 3982. e-mail: t.w.young@bham.ac.uk

ABSTRACT

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.

Present address: Faculty of Engineering, Gunma University, 5-1 Tenjin Cho 1 Chome Kiryu Shi, Gunma, Japan 376.

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