Title
C-terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?
Author
Centraal Instituut voor Voedingsonderzoek TNO TNO Voeding
Conesa, A.
Weelink, G.
van den Hondel, C.A.M.J.J.
Punt, P.J.
Publication year
2001
Abstract
The Caldariomyces fumago chloroperoxidase (CPO) is synthesised as a 372-aa precursor which undergoes two proteolytic processing events: removal of a 21-aa N-terminal signal peptide and of a 52-aa C-terminal propeptide. The Aspergillus niger expression system developed for CPO was used to get insight into the function of this C-terminal propeptide. A. niger transformants expressing a CPO protein from which the C-terminal propeptide was deleted failed in producing any extracellular CPO activity, although the CPO polypeptide was synthesised. Expression of the full-length gene in an A. niger strain lacking the KEX2-like protease PclA also resulted in the production of CPO cross-reactive material into the culture medium, but no CPO activity. Based on these results, a function of the C-terminal propeptide in CPO maturation is indicated. © 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. Molecular Sequence Numbers: GENBANK: AJ300448, X04486; Chemicals/CAS: Chloride Peroxidase, EC 1.11.1.10; DNA Primers; Enzyme Precursors; Molecular Chaperones
Subject
Amino Acid Sequence
Ascomycota
Aspergillus niger
Base Sequence
Chloride Peroxidase
DNA Primers
Enzyme Precursors
Gene Expression
Molecular Chaperones
Molecular Sequence Data
Protein Conformation
C-terminal propeptide
Chaperone
Chloroperoxidase
Filamentous fungi
Haem
KEX2
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DOI
https://doi.org/10.1016/s0014-5793(01)02698-9
TNO identifier
72350
ISSN
0014-5793
Source
FEBS Letters, 503 (503), 117-120
Document type
article