Palmitoyl Transferase FonPAT2-Catalyzed Palmitoylation of the FonAP-2 Complex Is Essential for Growth, Development, Stress Response, and Virulence in Fusarium oxysporum f. sp.
            <i>niveum</i>

Xiong, Xiaoxing; Gao, Yizhou; Wang, Jiajing; Wang, Hui; Lou, Jiajun; Bi, Yan; Yan, Yuqing; Li, Dayong; Song, Fengming

doi:10.1128/spectrum.03861-22

Cited by 8 publications

(6 citation statements)

References 76 publications

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“…Thus, FonKin4 likely influences Fon pathogenicity by regulating its invasive growth within host plants, consistent with the observed deficiencies in vegetative growth and asexual reproduction ( Figure 4 ). This mechanism parallels findings for FonPUF1, FonNST2, and FonPAT2 in Fon pathogenicity ( Gao et al, 2022 , 2023 ; Xiong et al, 2023 ). Furthermore, FonKin4 participated in stress responses against multiple cell wall-perturbing agents and oxidative stress-inducing factors ( Figure 5 ).…”

Section: Discussionsupporting

confidence: 86%

“…This reduction in pathogenicity in the ΔFonPARP1 mutant primarily stemmed from a defect in invasive growth within watermelon plants ( Figures 1D – G ) rather than an impairment in its ability to penetrate the host ( Supplementary Figure S6 ). This pattern mirrors the functions of previously identified pathogenicity factors, including FonNst2, FonPAT2, and FonPUF1, whose deletion mutants exhibited reduced pathogenicity due to compromised in planta invasive growth and colonization within host plants ( Gao et al, 2022 , 2023 ; Xiong et al, 2023 ). Our study also revealed that FonPARP1 undergoes self-PARylation in vitro ( Figure 7A ), indicating its active PARP activity in Fon .…”

Section: Discussionsupporting

confidence: 85%

“…For instance, N -glycosylation, catalyzed by N -glycosyltransferase Gnt2, is indispensable for the morphogenesis and virulence of F. oxysporum ( Lopez-Fernandez et al, 2015 ). Additionally, palmitoyl transferase FonPAT2-catalyzed palmitoylation of the FonAP-2 complex influences the stability and interactions among core subunits of the complex, playing a vital role in growth, development, stress responses, and pathogenicity of F. oxysporum ( Xiong et al, 2023 ). Lysine acetyltransferase FolArd1-mediated acetylation regulates the stability of the effector FolSvp1, thereby implicating its role in the pathogenicity of F. oxysporum ( Li et al, 2022 ).…”

Section: Introductionmentioning

confidence: 99%

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The Ser/Thr protein kinase FonKin4-poly(ADP-ribose) polymerase FonPARP1 phosphorylation cascade is required for the pathogenicity of watermelon fusarium wilt fungus Fusarium oxysporum f. sp. niveum

Wang,

Gao,

Xiong

et al. 2024

Front. Microbiol.

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Poly(ADP-ribosyl)ation (PARylation), catalyzed by poly(ADP-ribose) polymerases (PARPs) and hydrolyzed by poly(ADP-ribose) glycohydrolase (PARG), is a kind of post-translational protein modification that is involved in various cellular processes in fungi, plants, and mammals. However, the function of PARPs in plant pathogenic fungi remains unknown. The present study investigated the roles and mechanisms of FonPARP1 in watermelon Fusarium wilt fungus Fusarium oxysporum f. sp. niveum (Fon). Fon has a single PARP FonPARP1 and one PARG FonPARG1. FonPARP1 is an active PARP and contributes to Fon pathogenicity through regulating its invasive growth within watermelon plants, while FonPARG1 is not required for Fon pathogenicity. A serine/threonine protein kinase, FonKin4, was identified as a FonPARP1-interacting partner by LC–MS/MS. FonKin4 is required for vegetative growth, conidiation, macroconidia morphology, abiotic stress response and pathogenicity of Fon. The S_TKc domain is sufficient for both enzyme activity and pathogenicity function of FonKin4 in Fon. FonKin4 phosphorylates FonPARP1 in vitro to enhance its poly(ADP-ribose) polymerase activity; however, FonPARP1 does not PARylate FonKin4. These results establish the FonKin4-FonPARP1 phosphorylation cascade that positively contributes to Fon pathogenicity. The present study highlights the importance of PARP-catalyzed protein PARylation in regulating the pathogenicity of Fon and other plant pathogenic fungi.

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Section: Discussionsupporting

confidence: 86%

Section: Discussionsupporting

confidence: 85%

Section: Introductionmentioning

confidence: 99%

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The Ser/Thr protein kinase FonKin4-poly(ADP-ribose) polymerase FonPARP1 phosphorylation cascade is required for the pathogenicity of watermelon fusarium wilt fungus Fusarium oxysporum f. sp. niveum

Wang,

Gao,

Xiong

et al. 2024

Front. Microbiol.

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“…Palmitoyl transferase FonPAT2 regulates the growth, development, stress response and virulence of F. oxysporum f. sp. niveum by palmitoylation of the FonAP‐2 Complex (Xiong et al., 2023 ).…”

Section: Identification and Pathogenicity Of Root Rot Pathogens In ...mentioning

confidence: 99%

Plant–pathogen interaction with root rot of Panax notoginseng as a model: Insight into pathogen pathogenesis, plant defence response and biological control

Li,

Ai,

Hou

et al. 2024

Molecular Plant Pathology

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Plant diseases are a major threat affecting the sustainability of global agriculture. Although the breeding of new resistant cultivars is considered to be the primary approach to prevent and control plant diseases, it is dependent on an in‐depth understanding of plant–pathogen interactions. At present, we have an in‐depth understanding of the interactions between model plants and pathogens, such as Arabidopsis thaliana and rice, but we are still in the beginning stage for more non‐model plants (e.g., medicinal plants). Panax notoginseng is the primary source of the high‐value active ingredient triterpenoid saponins. Root rot disease in P. notoginseng has attracted research attention because of its high destructiveness. Understanding the infection stages and strategies of pathogens, plant resistance mechanisms and induced plant defence against pathogens is essential to support agricultural sustainable development of P. notoginseng. Here, we review and summarize, with root rot of P. notoginseng as a model, the current knowledge of plant–pathogen interaction, and feasability of use of microorganisms and secondary metabolites as sources of biological control agents at a low cost. Finally, we also discuss the importance of plant–pathogen interactions in resistance breeding, thereby providing a new strategy to develop green agriculture for non‐model plants.

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“…Directed mutation of pat1, pat2 and pat4 showed that their palmitoyl transferase activity is dependent upon the presence of a cysteine residue in the DHHC motif. These three palmitoyl transferases have clear effects on growth, formation of asexual spores and conidia morphology, in addition to the response to the cell wall and metal ions stressing factors [135]. An important observation was the fact that the lack of Pat1, Pat2 or Pat4 reduces fungal virulence in plants probably by alteration of the formation of toxic metabolites [106,136].…”

Section: Protein Palmitoylation In Plant Pathogenic Fungi: the Cargo ...mentioning

confidence: 99%

Targeting of Specialized Metabolites Biosynthetic Enzymes to Membranes and Vesicles by Posttranslational Palmitoylation: A Mechanism of Non-Conventional Traffic and Secretion of Fungal Metabolites

Martín,

Liras

2024

IJMS

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In nature, the formation of specialized (secondary) metabolites is associated with the late stages of fungal development. Enzymes involved in the biosynthesis of secondary metabolites in fungi are located in distinct subcellular compartments including the cytosol, peroxisomes, endosomes, endoplasmic reticulum, different types of vesicles, the plasma membrane and the cell wall space. The enzymes traffic between these subcellular compartments and the secretion through the plasma membrane are still unclear in the biosynthetic processes of most of these metabolites. Recent reports indicate that some of these enzymes initially located in the cytosol are later modified by posttranslational acylation and these modifications may target them to membrane vesicle systems. Many posttranslational modifications play key roles in the enzymatic function of different proteins in the cell. These modifications are very important in the modulation of regulatory proteins, in targeting of proteins, intracellular traffic and metabolites secretion. Particularly interesting are the protein modifications by palmitoylation, prenylation and miristoylation. Palmitoylation is a thiol group-acylation (S-acylation) of proteins by palmitic acid (C16) that is attached to the SH group of a conserved cysteine in proteins. Palmitoylation serves to target acylated proteins to the cytosolic surface of cell membranes, e.g., to the smooth endoplasmic reticulum, whereas the so-called toxisomes are formed in trichothecene biosynthesis. Palmitoylation of the initial enzymes involved in the biosynthesis of melanin serves to target them to endosomes and later to the conidia, whereas other non-palmitoylated laccases are secreted directly by the conventional secretory pathway to the cell wall space where they perform the last step(s) of melanin biosynthesis. Six other enzymes involved in the biosynthesis of endocrosin, gliotoxin and fumitremorgin believed to be cytosolic are also targeted to vesicles, although it is unclear if they are palmitoylated. Bioinformatic analysis suggests that palmitoylation may be frequent in the modification and targeting of polyketide synthetases and non-ribosomal peptide synthetases. The endosomes may integrate other small vesicles with different cargo proteins, forming multivesicular bodies that finally fuse with the plasma membrane during secretion. Another important effect of palmitoylation is that it regulates calcium metabolism by posttranslational modification of the phosphatase calcineurin. Mutants defective in the Akr1 palmitoyl transferase in several fungi are affected in calcium transport and homeostasis, thus impacting on the biosynthesis of calcium-regulated specialized metabolites. The palmitoylation of secondary metabolites biosynthetic enzymes and their temporal distribution respond to the conidiation signaling mechanism. In summary, this posttranslational modification drives the spatial traffic of the biosynthetic enzymes between the subcellular organelles and the plasma membrane. This article reviews the molecular mechanism of palmitoylation and the known fungal palmitoyl transferases. This novel information opens new ways to improve the biosynthesis of the bioactive metabolites and to increase its secretion in fungi.

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Palmitoyl Transferase FonPAT2-Catalyzed Palmitoylation of the FonAP-2 Complex Is Essential for Growth, Development, Stress Response, and Virulence in Fusarium oxysporum f. sp. niveum

Abstract: Fusarium oxysporum f. sp. niveum ( Fon ), the causal agent of watermelon Fusarium wilt, is one of the most serious threats for the sustainable development of the watermelon industry worldwide. However, little is known about the underlying molecular mechanism of pathogenicity in Fon .

Cited by 8 publications

References 76 publications

The Ser/Thr protein kinase FonKin4-poly(ADP-ribose) polymerase FonPARP1 phosphorylation cascade is required for the pathogenicity of watermelon fusarium wilt fungus Fusarium oxysporum f. sp. niveum

The Ser/Thr protein kinase FonKin4-poly(ADP-ribose) polymerase FonPARP1 phosphorylation cascade is required for the pathogenicity of watermelon fusarium wilt fungus Fusarium oxysporum f. sp. niveum

Plant–pathogen interaction with root rot of Panax notoginseng as a model: Insight into pathogen pathogenesis, plant defence response and biological control

Targeting of Specialized Metabolites Biosynthetic Enzymes to Membranes and Vesicles by Posttranslational Palmitoylation: A Mechanism of Non-Conventional Traffic and Secretion of Fungal Metabolites

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