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C‐terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?
Author(s) -
Conesa Ana,
Weelink Gerri,
van den Hondel Cees A.M.J.J.,
Punt Peter J.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02698-9
Subject(s) - protein precursor , chemistry , aspergillus niger , biochemistry , protease , chaperone (clinical) , extracellular , signal peptide , peptide , gene , recombinant dna , enzyme , medicine , pathology
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.