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A Novel Screening Method for Cell Wall Mutants in Aspergillus niger Identifies UDP-Galactopyranose Mutase as an Important Protein in Fungal Cell Wall Biosynthesis
Author(s) -
Robbert A. Damveld,
Angelique C. W. Franken,
Mark Arentshorst,
Peter J. Punt,
Frans M. Klis,
Cees A. M. J. J. van den Hondel,
Arthur F. J. Ram
Publication year - 2008
Publication title -
genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.792
H-Index - 246
eISSN - 1943-2631
pISSN - 0016-6731
DOI - 10.1534/genetics.107.073148
Subject(s) - biology , mutant , mutase , aspergillus nidulans , complementation , gene , conidiation , genetic screen , cell wall , reporter gene , pectate lyase , phycomyces blakesleeanus , biochemistry , gene expression , enzyme , pectinase
To identify cell wall biosynthetic genes in filamentous fungi and thus potential targets for the discovery of new antifungals, we developed a novel screening method for cell wall mutants. It is based on our earlier observation that the Aspergillus niger agsA gene, which encodes a putative alpha-glucan synthase, is strongly induced in response to cell wall stress. By placing the agsA promoter region in front of a selectable marker, the acetamidase (amdS) gene of A. nidulans, we reasoned that cell wall mutants with a constitutively active cell wall stress response pathway could be identified by selecting mutants for growth on acetamide as the sole nitrogen source. For the genetic screen, a strain was constructed that contained two reporter genes controlled by the same promoter: the metabolic reporter gene PagsA-amdS and PagsA-H2B-GFP, which encodes a GFP-tagged nuclear protein. The primary screen yielded 161 mutants that were subjected to various cell wall-related secondary screens. Four calcofluor white-hypersensitive, osmotic-remediable thermosensitive mutants were selected for complementation analysis. Three mutants were complemented by the same gene, which encoded a protein with high sequence identity with eukaryotic UDP-galactopyranose mutases (UgmA). Our results indicate that galactofuranose formation is important for fungal cell wall biosynthesis and represents an attractive target for the development of antifungals.

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