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Fig. 1 | Microbiome

Fig. 1

From: Post-translational regulation of autophagy is involved in intra-microbiome suppression of fungal pathogens

Fig. 1

Rapamycin secreted by Streptomyces hygroscopicus S89 alters fungal autophagy and global acetylome in Fusarium graminearum. a Phylogenetic tree of Streptomyces strains. Bar plots on the right describe the abundance (number) and the radius of antagonistic inhibition zone (cm) of tested bacterial strains. b Fungal autophagy was induced by S89 and its supernatant. The wild-type F. graminearum strain PH-1 labeled with GFP-Atg8 was co-cultured with S89 or supernatant, and the GFP-Atg8 translocation in mycelia was observed using a confocal microscope. Vacuoles were labeled with the CMAC dye. Bar = 10 μm. c Fungal autophagy flux in the strain PH-1::GFP-Atg8 upon various treatments. Total proteins extracted from mycelia were immunoblotted using the anti-GFP antibody. The extent of autophagy was estimated by calculating the amount of free GFP vs the total amount of intact GFP-Atg8 plus free GFP (the numbers appear underneath the blot). The protein samples were also detected with anti-GAPDH antibody as a loading control. d Antifungal activity of S89 supernatant and rapamycin. e LC-MS profile of rapamycin purified from the supernatant of S89 and the model strain S. hygroscopicus NRRL5491. Pure rapamycin was used as a positive control. f–h Acetylome profiles of F. graminearum in co-cultures with S89, S89 supernatant, or rapamycin. Total proteins were immunoblotted using the indicated antibodies. The anti-acetylated-lysine antibody (α-Acetyl-Lys) was used for detecting acetylated proteins, and the anti-acetyl-histone H3 antibody (α-H3ac) for detecting histone 3 acetylation. Proteins samples were also detected with anti-GAPDH or anti-H3 antibody as a loading control. Asterisks indicate histone bands

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