MAP kinase Hog1 mediates a cytochrome P450 oxidoreductase to promote the Sporisorium scitamineum cell survival under oxidative stress

The MAP kinase high osmolarity glycerol 1 (Hog1) plays a central role in responding to external oxidative stress in budding yeast Saccchromyces cerevisiae. However, the downstream responsive elements regulated by Hog1 remain poorly understood. In this study, we report that a Sporisorium scitamineum orthologue of Hog1, named as SsHog1, induced transcriptional expression of a putative cytochrome P450 oxidoreductase encoding gene SsCPR1, to antagonize oxidative stress. We found that upon exposure to hydrogen peroxide (H2O2), SsHog1 underwent strikingly phosphorylation, which was proved to be critical for transcriptional induction of SsCPR1. Loss of SsCPR1 led to hypersensitive to oxidative stress similar as the sshog1 Delta mutant did, but was resistant to osmotic stress, which is different from the sshog1 Delta mutant. On the other hand, overexpression of SsCPR1 in the sshog1 Delta mutant could partially restore its ability of oxidative stress tolerance, which indicated that the Hog1 MAP kinase regulates the oxidative stress response specifically through cytochrome P450 (SsCpr1) pathway. Overall, our findings highlight a novel MAPK signalling pathway mediated by Hog1 in regulation of the oxidative stress response via the cytochrome P450 system, which plays an important role in host-fungus interaction.

Automated summary

Hog1 MAP kinase plays a central role in responding to external oxidative stress, inducing the transcription of SsCPR1 to antagonize oxidative stress. The phosphorylation state of SsHog1 is critical for the transcriptional induction of SsCPR1, highlighting a novel MAPK signaling pathway regulated by Hog1 in the oxidative stress response via the cytochrome P450 system.