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

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 Mr of 37427....

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Bibliographic Details
Published in:Microbiology (Society for General Microbiology) 1996-10, Vol.142 (10), p.2913-2921
Main Authors: Young, T.W, Wadeson, A, Glover, D.J, Quincey, R.V, Butlin, M.J, Kamei, E.A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aspartic Acid Endopeptidases - chemistry
Aspartic Acid Endopeptidases - genetics
Aspartic Acid Endopeptidases - isolation & purification
Aspartic Acid Endopeptidases - metabolism
Base Sequence
Cloning, Molecular
Codon
Fungal Proteins
genbank/x97068
Gene Expression Regulation, Fungal
Genes, Fungal - genetics
Hydrogen-Ion Concentration
Molecular Sequence Data
Molecular Weight
plant biochemistry
plant breeding
plant genetics
plant physiology
Protein Precursors - genetics
Protein Processing, Post-Translational
RNA, Fungal - analysis
RNA, Messenger - analysis
Saccharomycetales - enzymology
Saccharomycetales - genetics
Sequence Alignment
Sequence Analysis
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Transcription, Genetic
Yeasts - enzymology
Yeasts - genetics
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Description
Summary: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 Mr 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 V. lipolytica 148 is regulated by the pH of culture.
ISSN:1350-0872
1465-2080
DOI:10.1099/13500872-142-10-2913