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- W2765452015 abstract "Summary 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 β2‐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." @default.
- W2765452015 created "2017-11-10" @default.
- W2765452015 creator A5006215775 @default.
- W2765452015 creator A5029765836 @default.
- W2765452015 creator A5046992986 @default.
- W2765452015 creator A5066002102 @default.
- W2765452015 creator A5074504754 @default.
- W2765452015 creator A5090306776 @default.
- W2765452015 date "2017-11-24" @default.
- W2765452015 modified "2023-10-06" @default.
- W2765452015 title "The FgSsb-FgZuo-FgSsz complex regulates multiple stress responses and mycotoxin production via folding the soluble SNARE Vam7 and β2-tubulin in<i>Fusarium graminearum</i>" @default.
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