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A broadly conserved fungal alcohol oxidase (AOX) facilitates fungal invasion of plants

ABSTRACT: Alcohol oxidases are ecologically important enzymes which facilitate a number of plant-fungal interactions. Within Ascomycota they are primarily associated with methylotrophy, as a peroxisomal alcohol oxidase (AOX) catalyzing the conversion of methanol to formaldehyde in methylotrophic yeast. In this study we demonstrate that AOX orthologs are phylogenetically conserved proteins which are common in the genomes of non-methylotrophic, plant-associating fungi. Additionally, AOX orthologs are highly expressed during infection in a range of diverse pathosystems. To study the role of AOX in plant colonization, AOX knockout mutants were generated in the broad host range pathogen Sclerotinia sclerotiorum. Disease assays in soybean showed that these mutants had a significant virulence defect as evidenced by markedly reduced stem lesions and mortality rates. Chemical genomics suggest that SsAOX may function as an aromatic alcohol oxidase, and growth assays demonstrate that ΔSsAOX is incapable of properly utilizing plant extract as a nutrient source. Profiling of known aromatic alcohols point towards the monolignol coniferyl alcohol (CoA) as a possible substrate for SsAOX. As CoA and other monolignols are ubiquitous among land plants, the presence of highly conserved AOX orthologs throughout Ascomycota imply that this is a broadly conserved protein used by ascomycete fungi during plant colonization.

ORGANISM(S): Sclerotinia sclerotiorum

PROVIDER: GSE212269 | GEO | 2022/12/02

REPOSITORIES: GEO

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Project description:Various environmental bacteria were adapted to the presence of toxic and recalcitrant organic solvents. Cupriavidus metallidurans CH34, a β-proteobacterium that was found in industrial environments is known as a bacterial model to study heavy metal resistance. Interestingly, genome screening of CH34 also reveals the existence of genes involved in the degradation of recalcitrant organic solvents, such acetone and aromatic compounds. Here, we showed that this bacterium could resist a large variety of organic solvents, and was also able to metabolize some of them. In particular, investigations were focused on acetone and isopropanol catabolism. Integrative studies based on transcriptomic (DNA microarrays), proteomic (2D-DIGE and Isotope-Coded Protein Label technology) and biochemical analyses (enzyme purification and characterization) showed a similar catabolic pathway for both molecules which involved the AcxABC acetone carboxylase. First, isopropanol is oxidized into acetone by the Adh alcohol dehydrogenase. Acetoacetate production from acetone is then catalyzed by the acetone carboxylase. The generated acetoacetate molecules are then transformed by the PacIJ 3-oxoacid CoA-transferase, to acetoacetyl-CoA and succinate. Finally, an acetyl-CoA acetyltransferase catalyses the hydrolysis of acetoacetyl-CoA into 2 acetyl-CoA that are introduced into the glyoxylate cycle. As demonstrated, key enzymes of the acetone/isopropanol catabolism (encoded by acx and ald genes) are under the control of a σ54-dependent RNA polymerase. Moreover, the catabolic pathway involved in acetone and isopropanol consumption was repressed when gluconate was given as alternative carbon substrate, displaying a new example of diauxie. The results presented here provide a comprehensive picture of acetone and isopropanol biodegradation in Cupriavidus metallidurans CH34 and strongly support the fact that CH34 can be considered as a solvent tolerant bacterium. Two-condition experiments. Comparing samples after induction with acetone versus non-induced samples. Biological triplicate. Each array contains 3 technical replicates.

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A broadly conserved fungal alcohol oxidase (AOX) facilitates fungal invasion of plants

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