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Fungal siderophore biosynthesis is partially localized in peroxisomes
Author(s) -
Gründlinger Mario,
Yasmin Sabiha,
Lechner Beatrix Elisabeth,
Geley Stephan,
Schrettl Markus,
Hynes Michael,
Haas Hubertus
Publication year - 2013
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12225
Subject(s) - biology , siderophore , peroxisome , biosynthesis , microbiology and biotechnology , computational biology , biochemistry , enzyme , gene
Summary Siderophores play a central role in iron metabolism and virulence of most fungi. Both A spergillus fumigatus and A spergillus nidulans excrete the siderophore triacetylfusarinine C ( TAFC ) for iron acquisition. In A . fumigatus , green fluorescence protein‐tagging revealed peroxisomal localization of the TAFC biosynthetic enzymes SidI (mevalonyl‐ CoA ligase), SidH (mevalonyl‐ CoA hydratase) and SidF (anhydromevalonyl‐ CoA transferase), while elimination of the peroxisomal targeting signal ( PTS ) impaired both, peroxisomal SidH ‐targeting and TAFC biosynthesis. The analysis of A . nidulans mutants deficient in peroxisomal biogenesis, ATP import or protein import revealed that cytosolic mislocalization of one or two but, interestingly, not all three enzymes impairs TAFC production during iron starvation. The PTS motifs are conserved in fungal orthologues of SidF , SidH and SidI . In agreement with the evolutionary conservation of the partial peroxisomal compartmentalization of fungal siderophore biosynthesis, the SidI orthologue of coprogen‐type siderophore‐producing N eurospora crassa was confirmed to be peroxisomal. Taken together, this study identified and characterized a novel, evolutionary conserved metabolic function of peroxisomes.