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Applied and Environmental Microbiology, January 2000, p. 363-368, Vol. 66, No. 1
0099-2240/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Characterization of the Kexin-Like Maturase of Aspergillus niger

Ruud Jalving, Peter J. I. van de Vondervoort, Jaap Visser, and Peter J. Schaap*

Section Molecular Genetics of Industrial Microorganisms, Wageningen University, Wageningen, The Netherlands

Received 2 August 1999/Accepted 1 November 1999

Secreted yields of foreign proteins may be enhanced in filamentous fungi through the use of translational fusions in which the target protein is fused to an endogenous secreted carrier protein. The fused proteins are usually separated in vivo by cleavage of an engineered Kex2 endoprotease recognition site at the fusion junction. We have cloned the kexin-encoding gene of Aspergillus niger (kexB). We constructed strains that either overexpressed KexB or lacked a functional kexB gene. Kexin-specific activity doubled in membrane-protein fractions of the strain overexpressing KexB. In contrast, no kexin-specific activity was detected in the similar protein fractions of the kexB disruptant. Expression in this loss-of-function strain of a glucoamylase human interleukin-6 fusion protein with an engineered Kex2 dibasic cleavage site at the fusion junction resulted in secretion of unprocessed fusion protein. The results show that KexB is the endoproteolytic proprotein processing enzyme responsible for the processing of (engineered) dibasic cleavage sites in target proteins that are transported through the secretion pathway of A. niger.

* Corresponding author. Mailing address: Section Molecular Genetics of Industrial Microorganisms, Wageningen University, Dreijenlaan 2, 6703 HA, Wageningen, The Netherlands. Phone: 31 317 485142. Fax: 31 317 484011. E-mail: Peter.Schaap{at}algemeen.mgim.wau.nl.

Applied and Environmental Microbiology, January 2000, p. 363-368, Vol. 66, No. 1
0099-2240/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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