Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis

Details

Serval ID
serval:BIB_7B021254C1A3
Type
Article: article from journal or magazin.
Collection
Publications
Title
Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis
Journal
FEBS Letters
Author(s)
Togni  G., Sanglard  D., Falchetto  R., Monod  M.
ISSN
0014-5793 (Print)
Publication state
Published
Issued date
07/1991
Volume
286
Number
1-2
Pages
181-5
Notes
Journal Article --- Old month value: Jul 29
Abstract
The extracellular acid protease of Candida tropicalis was purified from the supernatant fraction of culture medium containing bovine serum albumin as nitrogen source and the NH2-terminal amino acid (aa) sequence of the protein was determined. The gene for the acid protease (ACP) was isolated using a pool of synthetic oligonucleotides as a probe and a segment of the deduced aa sequence was found to be in agreement with the NH2-terminal aa sequence of the protein. The deduced aa sequence of ACP is similar to the aa sequence of proteases of the pepsin family. The nucleotide sequence of the 5' portion of this gene revealed a coding sequence for a 60 residue propeptide containing two Lys-Arg amino acid pairs that have been identified as sites for peptidase processing of several exported peptides and proteins. The final Lys-Arg site occurs at the junction with the mature extracellular form of the acid protease.
Keywords
Amino Acid Sequence Aspartic Endopeptidases/chemistry/*genetics/isolation & purification Base Sequence Candida/enzymology/*genetics Cloning, Molecular DNA, Fungal Electrophoresis, Polyacrylamide Gel Genes, Fungal Molecular Sequence Data Pepsin A/chemistry Restriction Mapping Sequence Alignment
Pubmed
Web of science
Open Access
Yes
Create date
25/01/2008 17:46
Last modification date
20/08/2019 15:36
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