Journal
ENVIRONMENTAL MICROBIOLOGY
Volume 19, Issue 12, Pages 5040-5059Publisher
WILEY
DOI: 10.1111/1462-2920.13968
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Funding
- National Natural Science Fund for Distinguished Young Scholar [31525020]
- National Science Foundation [31571945, 31401696]
- STS program [KFJ-STS-ZDTP-002]
- China Agriculture Research System [CARS-3-1-15]
- Fundamental Research Funds for the Central Universities [2017FZA6014]
- Dabeinong Funds for Discipline Development and Talent Training in Zhejiang University
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Hsp70 proteins play important roles in protein folding in the budding yeast, but their functions in pathogenic fungi are largely unknown. Here, we found that Fusarium graminearum Hsp70 proteins FgSsb, FgSsz and their cochaperone FgZuo formed a complex. This complex was required for microtubule morphology, vacuole fusion and endocytosis. More importantly, the 2-tubulin FgTub2 and SNARE protein FgVam7 were identified as targeting proteins of this complex. We further found that the complex FgSsb-FgZuo-FgSsz controlled sensitivity of F. graminearum to the antimicrotubule drug carbendazim and cold stress via regulating the folding of FgTub2. Moreover, this complex assisted the folding of FgVam7, subsequently modulated vacuole fusion and responses to heavy metal, osmotic and oxidative stresses. In addition, the deletion of this complex led to dramatically decreased deoxynivalenol biosynthesis. This study uncovers a novel regulating mechanism of Hsp70 in multiple stress responses in a filamentous fungus.
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