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

Détails

ID Serval
serval:BIB_7B021254C1A3
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeast Candida tropicalis
Périodique
FEBS Letters
Auteur(s)
Togni  G., Sanglard  D., Falchetto  R., Monod  M.
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
07/1991
Volume
286
Numéro
1-2
Pages
181-5
Notes
Journal Article --- Old month value: Jul 29
Résumé
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.
Mots-clé
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
Oui
Création de la notice
25/01/2008 16:46
Dernière modification de la notice
20/08/2019 14:36
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