title: Ustilago maydis phosphodiesterases play a role in the dimorphic switch and in pathogenicity.
abstract: Components of the cAMP (cyclic AMP) signalling cascades are conserved from fungi to humans, and are particularly important for fungal dimorphism and pathogenicity. Previous work has described two phosphodiesterases, UmPde1 and UmPde2, in Ustilago maydis which show strong phosphodiesterase activity. We further characterized the biological function(s) of these phosphodiesterases in U. maydis. Specifically, we examined their possible role(s) in regulation of the cAMP-dependent protein kinase A (PKA) pathway and their roles in filamentous growth and pathogenicity. We found that UmPde1, which shares 35 % similarity with Cryptococcus neoformans Pde1, also displays functional homology with this enzyme. UmPde1 complements the capsule-formation defect of C. neoformans strains deleted for Pde1. In U. maydis, the cell morphology of the umpde1 deletion mutant resembled the multiple budding phenotypes seen with the ubc1 mutant, which lacks the regulatory subunit of PKA. Interestingly, on low-ammonium medium, umpde2 deletion strains showed a reduction in filamentation that was comparable to that of ubc1 deletion strains; however, umpde1 deletion strains showed normal filamentation on low-ammonium medium. Furthermore, both the ubc1 deletion strain in which the PKA pathway was constitutively active and the umpde1 deletion strains were significantly reduced in pathogenicity, while the umpde2 deletion strains showed a trend for reduced pathogenicity compared with wild-type strains. These data support a role for the phosphodiesterases UmPde1 and UmPde2 in regulating the U. maydis cAMP-dependent PKA pathway through modulation of cAMP levels, thus affecting dimorphic growth and pathogenicity.
authors.affiliation: Department of Biology, Program on Disease Evolution, University of Louisville, Louisville, KY 40208, USA.
authors.forename: Charu
authors.initials: C
authors.lastname: Agarwal
authors.affiliation: Department of Biology, Program on Disease Evolution, University of Louisville, Louisville, KY 40208, USA.
authors.forename: Kavita B
authors.initials: KB
authors.lastname: Aulakh
authors.affiliation: Department of Biology, Program on Disease Evolution, University of Louisville, Louisville, KY 40208, USA.
authors.forename: Kaly
authors.initials: K
authors.lastname: Edelen
authors.affiliation: Department of Biology, Program on Disease Evolution, University of Louisville, Louisville, KY 40208, USA.
authors.forename: Michael
authors.initials: M
authors.lastname: Cooper
authors.affiliation: Department of Biology, Program on Disease Evolution, University of Louisville, Louisville, KY 40208, USA.
authors.forename: R Margaret
authors.initials: RM
authors.lastname: Wallen
authors.affiliation: Department of Biology, Program on Disease Evolution, University of Louisville, Louisville, KY 40208, USA.
authors.forename: Seth
authors.initials: S
authors.lastname: Adams
authors.affiliation: Department of Biology, Program on Disease Evolution, University of Louisville, Louisville, KY 40208, USA.
authors.forename: David J
authors.initials: DJ
authors.lastname: Schultz
authors.affiliation: Department of Biology, Program on Disease Evolution, University of Louisville, Louisville, KY 40208, USA.
authors.forename: Michael H
authors.initials: MH
authors.lastname: Perlin
mesh_terms: D000242:Cyclic AMP / Q000378:metabolism; D017868:Cyclic AMP-Dependent Protein Kinases / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal; D010727:Phosphoric Diester Hydrolases / Q000235:genetics / Q000378:metabolism*; D010935:Plant Diseases / Q000382:microbiology*; D014588:Ustilago / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000472:pathogenicity*; D014774:Virulence; D003313:Zea mays / Q000382:microbiology
chemical_list: D005656:Fungal Proteins; D000242:Cyclic AMP; D017868:Cyclic AMP-Dependent Protein Kinases; D010727:Phosphoric Diester Hydrolases