SUMOylation regulates low temperature survival and oxidative DNA damage tolerance in Botrytis cinerea.
Wenyong ShaoKewei SunTianling MaHuixian JiangMatthias HahnZhonghua MaChen JiaoYanni YinPublished in: The New phytologist (2023)
● SUMOylation as one of the protein post-translational modifications plays crucial roles in multiple biological processes of eukaryotic organisms. Botrytis cinerea is a devastating fungal pathogen and capable of infecting plant hosts at low temperature. However, the molecular mechanisms of low temperature adaptation are largely unknown in fungi. ● Combining with biochemical methods and biological analyses, we report that SUMOylation regulates pathogen survival at low temperature and oxidative DNA damage response during infection in B. cinerea. The heat shock protein (Hsp70) BcSsb and E3 ubiquitin ligase BcRad18 were identified as substrates of SUMOylation, moreover their SUMOylation both requires a single unique SUMO-interacting motif (SIM). ● SUMOylated BcSsb regulates β-tubulin accumulation, thereby affecting the stability of microtubules and consequently mycelial growth at low temperature. On the other hand, SUMOylated BcRad18 modulates mono-ubiquitination of the sliding clamp protein proliferating cell nuclear antigen (PCNA), which is involved in response to oxidative DNA damage during infection. ● Our study uncovers the molecular mechanisms of SUMOylation-mediated low temperature survival and oxidative DNA damage tolerance during infection in a devastating fungal pathogen, which provides novel insights into low temperature adaptation and pathogenesis for post-harvest pathogens as well as new targets for inhibitor invention in disease control.