Fig. 1: A. fumigatus sirtuins are active deacetylases.
From: Sirtuin E deacetylase is required for full virulence of Aspergillus fumigatus
A In silico analysis showed that A. fumigatus harbors six schematically represented sirtuins. The sirtuin catalytic domains are colored and flanked by distinct N- and C-terminal extensions. The numbers below each domain indicate the amino acid position for orientation. B Phylogenetic tree of A. fumigatus (Af) and S. cerevisiae (Sc) sirtuins. The sirtuins are divided into Class Ia, Ib, II, and III for both species. C Identity (%) of sirtuin domains among A. fumigatus, Saccharomyces cerevisiae and human. The alignment of full sequences is depicted in Supplementary Fig. 1. D Tridimensional structural analyses of predicted A. fumigatus sirtuin domains compared to S. cerevisiae homologs indicating the catalytic site with conserved histidine and NAD+ binding region. E SDS–PAGE gel of purified A. fumigatus recombinant sirtuins used in the in vitro deacetylation assays. Expected sizes for each protein: AfHstA (41.5 kDa); AfSirA (54.6 kDA); AfSirB (46.9 kDa); AfSirC (34.6 kDa); AfSirD (45.1 kDa); AfSirE (67.1 kDa). F and G In vitro deacetylase activity of A. fumigatus recombinant sirtuins using a-tubulin K40ac (F) and histone H3K56ac (G) peptides as substrates. HstA and SirD were the only enzymes that did not present deacetylase activity. The positive control used in the assays was the Trypanosoma cruzi Sir2rp1.
