Investigating the Structure of the Components of the PolyADP-Ribosylation System in Fusarium Fungi and Evaluating the Expression Dynamics of Its Key Genes

Poly(ADP-ribose) polymerase (PARP) is the key enzyme in polyADP-ribosylation, one of the main post-translational modifications. This enzyme is abundant in eukaryotic organisms. However, information on the PARP structure and its functions in members of the Fungi kingdom is very limited. In this study, we performed a bioinformatic search for homologs of PARP and its antagonist, PARG, in the genomes of four <i>Fusarium</i> strains using their whole-genome sequences annotated and deposited in databases. The <i>F. graminearum</i> PH-1, <i>F. proliferatum</i> ET-1, and <i>F. oxysporum</i> Fo47 strains were shown to possess a single homolog of both PARP and PARG. In addition, the <i>F. oxysporum</i> f. sp. <i>lycopersici</i> strain 4287 contained four additional proteins comprising PARP catalytic domains whose structure was different from that of the remaining identified homologs. Partial nucleotide sequences encoding the catalytic domains of the PARP and PARG homologs were determined in 11 strains of 9 <i>Fusarium</i> species deposited in all-Russian collections, and the phylogenetic properties of the analyzed genes were evaluated. In the toxigenic <i>F. graminearum</i> strain, we demonstrated up-regulation of the gene encoding the PARP homolog upon culturing under conditions stimulating the production of the DON mycotoxin, as well as up-regulation of the gene encoding PARG at later stages of growth. These findings indirectly indicate involvement of the polyADP-ribosylation system in the regulation of the genes responsible for DON biosynthesis.