The FgSsb-FgZuo-FgSsz complex regulates multiple stress responses and mycotoxin production via folding the soluble SNARE Vam7 and ß2-tubulin in Fusarium graminearum.
Environ Microbiol
; 19(12): 5040-5059, 2017 Dec.
Article
in En
| MEDLINE
| ID: mdl-29076607
ABSTRACT
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 ß2-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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Tubulin
/
Fungal Proteins
/
Protein Folding
/
HSP70 Heat-Shock Proteins
/
SNARE Proteins
/
Synaptosomal-Associated Protein 25
/
Fusarium
Type of study:
Prognostic_studies
Language:
En
Journal:
Environ Microbiol
Journal subject:
MICROBIOLOGIA
/
SAUDE AMBIENTAL
Year:
2017
Type:
Article
Affiliation country:
China