title: cpsA regulates mycotoxin production, morphogenesis and cell wall biosynthesis in the fungus Aspergillus nidulans.
abstract: The model fungus Aspergillus nidulans synthesizes numerous secondary metabolites, including sterigmatocystin (ST). The production of this toxin is positively controlled by the global regulator veA. In the absence of veA (ΔveA), ST biosynthesis is blocked. Previously, we performed random mutagenesis in a ΔveA strain and identified revertant mutants able to synthesize ST, among them RM1. Complementation of RM1 with a genomic library revealed that the mutation occurred in a gene designated as cpsA. While in the ΔveA genetic background cpsA deletion restores ST production, in a veA wild-type background absence of cpsA reduces and delays ST biosynthesis decreasing the expression of ST genes. Furthermore, cpsA is also necessary for the production of other secondary metabolites, including penicillin, affecting the expression of PN genes. In addition, cpsA is necessary for normal asexual and sexual development. Chemical and microscopy analyses revealed that CpsA is found in cytoplasmic vesicles and it is required for normal cell wall composition and integrity, affecting adhesion capacity and oxidative stress sensitivity. The conservation of cpsA in Ascomycetes suggests that cpsA homologs might have similar roles in other fungal species.
authors.affiliation: Department of Biological Sciences, Northern Illinois University, Dekalb, IL, 60115, USA.
authors.forename: Xuehuan
authors.initials: X
authors.lastname: Feng
authors.affiliation: Department of Biological Sciences, Northern Illinois University, Dekalb, IL, 60115, USA.
authors.forename: Vellaisamy
authors.initials: V
authors.lastname: Ramamoorthy
authors.affiliation: Department of Biological Sciences, Northern Illinois University, Dekalb, IL, 60115, USA.
authors.forename: Sandesh S
authors.initials: SS
authors.lastname: Pandit
authors.affiliation: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
authors.forename: Alicia
authors.initials: A
authors.lastname: Prieto
authors.affiliation: Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
authors.forename: Eduardo A
authors.initials: EA
authors.lastname: Espeso
authors.affiliation: Department of Biological Sciences, Northern Illinois University, Dekalb, IL, 60115, USA.
authors.forename: Ana M
authors.identifier: 0000-0003-4641-5175
authors.initials: AM
authors.lastname: Calvo
mesh_terms: D000595:Amino Acid Sequence; D001203:Ascomycota / Q000378:metabolism; D001233:Aspergillus nidulans / Q000235:genetics / Q000378:metabolism*; D002268:Carboxypeptidases / Q000378:metabolism*; D002473:Cell Wall / Q000378:metabolism; D005656:Fungal Proteins / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal / Q000235:genetics; D009024:Morphogenesis; D016296:Mutagenesis; D009154:Mutation; D009183:Mycotoxins / Q000096:biosynthesis / Q000378:metabolism; D013172:Spores, Fungal / Q000254:growth & development; D013241:Sterigmatocystin / Q000096:biosynthesis
chemical_list: D005656:Fungal Proteins; D009183:Mycotoxins; D013241:Sterigmatocystin; D002268:Carboxypeptidases