C‐terminal propeptide of the Caldariomyces fumago chloroperoxidase: an intramolecular chaperone?

FEBS Letters

Conesa, Ana¹  van den Hondel, Cees A.M.J.J.¹  Punt, Peter J.¹  Weelink, Gerri¹ 

[1] TNO Nutrition and Food Research Institute, Department of Applied Microbiology and Gene Technology, P.O. Box 360, 3700 AJ Zeist, The Netherlands

关键词: Chloroperoxidase;    Chaperone;    Processing;    C-terminal propeptide;    KEX2;    Filamentous fungi;    Haem;   

DOI  :  10.1016/S0014-5793(01)02698-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown