Aspergillus protein degradation pathways with different secreted protease sets at neutral and acidic pH.

Détails

ID Serval
serval:BIB_E5632500E3A6
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Aspergillus protein degradation pathways with different secreted protease sets at neutral and acidic pH.
Périodique
Journal of Proteome Research
Auteur(s)
Sriranganadane D., Waridel P., Salamin K., Reichard U., Grouzmann E., Neuhaus J.-M., Quadroni M., Monod M.
ISSN
1535-3907 (electronic)
ISSN-L
1535-3893
Statut éditorial
Publié
Date de publication
2010
Volume
9
Numéro
7
Pages
3511-3519
Langue
anglais
Résumé
Aspergillus fumigatus grows well at neutral and acidic pH in a medium containing protein as the sole nitrogen source by secreting two different sets of proteases. Neutral pH favors the secretion of neutral and alkaline endoproteases, leucine aminopeptidases (Laps) which are nonspecific monoaminopeptidases, and an X-prolyl dipeptidase (DppIV). Acidic pH environment promotes the secretion of an aspartic endoprotease of pepsin family (Pep1) and tripeptidyl-peptidases of the sedolisin family (SedB and SedD). A novel prolyl peptidase, AfuS28, was found to be secreted in both alkaline and acidic conditions. In previous studies, Laps were shown to degrade peptides from their N-terminus until an X-Pro sequence acts as a stop signal. X-Pro sequences can be then removed by DppIV, which allows Laps access to the following residues. We have shown that at acidic pH Seds degrade large peptides from their N-terminus into tripeptides until Pro in P1 or P'1 position acts as a stop for these exopeptidases. However, X-X-Pro and X-X-X-Pro sequences can be removed by AfuS28 thus allowing Seds further sequential proteolysis. In conclusion, both alkaline and acidic sets of proteases contain exoprotease activity capable of cleaving after proline residues that cannot be removed during sequential digestion by nonspecific exopeptidases.
Mots-clé
Secretome, Aspergillus Fumigatus, Sedolisin, Prolylpeptidase, Protein Acidic Hydrolysis, Enzyme Synergy, Protein Degradation Mechanism, Peptide-Transport Gene, Candida-Albicans, Trichophyton-Rubrum, Polyacrylamide-Gels, Nonspecific Aminopeptidase, Saccharomyces-Cerevisiae, Aspartyl Proteinases, Mass-Spectrometry, Statistical-Model, Fumigatus
Pubmed
Web of science
Création de la notice
19/07/2010 14:30
Dernière modification de la notice
20/08/2019 16:08
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