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>

Liu, Zunyong; Wang, Zhihui; Huang, Mengmeng; Yan, Leiyan; Ma, Zhonghua; Yin, Yanni

doi:10.1111/1462-2920.13968

Cited by 19 publications

(19 citation statements)

References 107 publications

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“…S1), which were consistent with the results of acetylome in various organisms (Lv et al ., ; Zhou et al ., ; Zhou et al ., ). And orthologs of these acetylated proteins have been shown to be involved in virulence in pathogenic fungi, including F. graminearum (Zheng et al ., ; Liu et al ., ), C. albicans (Gong et al ., ) and B. cinerea (Gonzalez et al ., ), indicating that acetylation may contribute to pathogenicity in A. flavus . In addition, the latest research also showed that in human fungal pathogens, such as Cryptococcus neoformans , C. albicans , and A. fumigatus , the levels of protein acetylation in pathogenic fungi correlate with their pathogenicity (Li et al ., ).Our results also proved that acetylation modification of AflO at K241 and K384 plays critical roles in the pathogenicity of A. flavus .…”

Section: Discussionmentioning

confidence: 99%

Lysine acetylation contributes to development, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus

Guang

Yue

Ren

et al. 2019

Environmental Microbiology

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Summary Aspergillus flavus is a pathogenic fungus that produces carcinogenic aflatoxins, posing a great threat to crops, animals and humans. Lysine acetylation is one of the most important reversible post‐translational modifications and plays a vital regulatory role in various cellular processes. However, current information on the extent and function of lysine acetylation and aflatoxin biosynthesis in A. flavus is limited. Here, a global acetylome analysis of A. flavus was performed by peptide pre‐fractionation, pan‐acetylation antibody enrichment and liquid chromatography–mass spectrometry. A total of 1313 high‐confidence acetylation sites in 727 acetylated proteins were identified in A. flavus. These acetylation proteins are widely involved in glycolysis/gluconeogenesis, pentose phosphate pathway, citric acid cycle and aflatoxin biosynthesis. AflO (O‐methyltransferase), a key enzyme in aflatoxin biosynthesis, was found to be acetylated at K241 and K384. Deletion of aflO not only impaired conidial and sclerotial developments, but also dramatically suppressed aflatoxin production and pathogenicity of A. flavus. Further site‐specific mutations showed that lysine acetylation of AflO could also result in defects in development, aflatoxin production and pathogenicity, suggesting that acetylation plays a vital role in the regulation of the enzymatic activity of AflO in A. flavus. Our findings provide evidence for the involvement of lysine acetylation in various biological processes in A. flavus and facilitating in the elucidation of metabolic networks.

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Section: Discussionmentioning

confidence: 99%

Lysine acetylation contributes to development, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus

Guang

Yue

Ren

et al. 2019

Environmental Microbiology

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“…oryzae and F . graminearum , respectively (Yi et al, 2009; Liu et al, 2017). The sequences of the known proteins were used to conduct a BLAST search of F .…”

Section: Resultsmentioning

confidence: 99%

“…graminearum , and S . cerevisiae (Yam et al, 2005; Yi et al, 2009; Liu et al, 2017). However, no effort has been made to elucidate Hsp70s in F .…”

Section: Discussionmentioning

confidence: 99%

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The ER Lumenal Hsp70 Protein FpLhs1 Is Important for Conidiation and Plant Infection in Fusarium pseudograminearum

Chen

Geng

et al. 2019

Front. Microbiol.

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Heat shock protein 70s (Hsp70s) are a class of molecular chaperones that are highly conserved and ubiquitous in organisms ranging from microorganisms to plants and humans. Hsp70s play key roles in cellular development and protecting living organisms from environmental stresses such as heat, drought, salinity, acidity, and cold. However, their functions in pathogenic fungi are largely unknown. Here, a total of 14 FpHsp70 genes were identified in Fusarium pseudograminearum , including 3 in the mitochondria, 7 in the cytoplasm, 2 in the endoplasmic reticulum (ER), 1 in the nucleus, and 1 in the plastid. However, the exon–intron boundaries and protein motifs of the FpHsp70 have no consistency in the same subfamily. Expression analysis revealed that most FpHsp70 genes were up-regulated during infection, implying that FpHsp70 genes may play important roles in F . pseudograminearum pathogenicity. Furthermore, knockout of an ER lumenal Hsp70 homolog FpLhs1 gene reduced growth, conidiation, and pathogenicity in F . pseudograminearum . These mutants also showed a defect in secretion of some proteins. Together, FpHsp70s might play essential roles in F . pseudograminearum and FpLhs1 is likely to act on the development and virulence by regulating protein secretion.

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“…Recent studies suggest that intracellular trafficking including endocytosis, exocytosis, retrograde trafficking and ESCRT pathway are all important for the development, pathogenicity, and production of DON in F . graminearum [ 9 – 14 ].…”

Section: Introductionmentioning

confidence: 99%

Small GTPase Rab7-mediated FgAtg9 trafficking is essential for autophagy-dependent development and pathogenicity in Fusarium graminearum

et al. 2018

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Fusarium graminearum is a fungal pathogen that causes Fusarium head blight (FHB) in wheat and barley. Autophagy is a highly conserved vacuolar degradation pathway essential for cellular homeostasis in which Atg9 serves as a multispanning membrane protein important for generating membranes for the formation of phagophore assembly site. However, the mechanism of autophagy or autophagosome formation in phytopathogens awaits further clarifications. In this study, we identified and characterized the Atg9 homolog (FgAtg9) in F. graminearum by live cell imaging, biochemical and genetic analyses. We find that GFP-FgAtg9 localizes to late endosomes and trans-Golgi network under both nutrient-rich and nitrogen starvation conditions and also show its dynamic actin-dependent trafficking in the cell. Further targeted gene deletion of FgATG9 demonstrates that it is important for growth, aerial hyphae development, and pathogenicity in F. graminearum. Furthermore, the deletion mutant (ΔFgatg9) shows severe defects in autophagy and lipid metabolism in response to carbon starvation. Interestingly, small GTPase FgRab7 is found to be required for the dynamic trafficking of FgAtg9, and co-immunoprecipitation (Co-IP) assays show that FgAtg9 associates with FgRab7 in vivo. Finally, heterologous complementation assay shows that Atg9 is functionally conserved in F. graminearum and Magnaporthe oryzae. Taken together, we conclude that FgAtg9 is essential for autophagy-dependent development and pathogenicity of F. graminearum, which may be regulated by the small GTPase FgRab7.

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The FgSsb‐FgZuo‐FgSsz complex regulates multiple stress responses and mycotoxin production via folding the soluble SNARE Vam7 and β2‐tubulin in Fusarium graminearum

Cited by 19 publications

References 107 publications

Lysine acetylation contributes to development, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus

Lysine acetylation contributes to development, aflatoxin biosynthesis and pathogenicity in Aspergillus flavus

The ER Lumenal Hsp70 Protein FpLhs1 Is Important for Conidiation and Plant Infection in Fusarium pseudograminearum

Small GTPase Rab7-mediated FgAtg9 trafficking is essential for autophagy-dependent development and pathogenicity in Fusarium graminearum

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