Abstract
Plant pathogens secrete numerous effectors to promote host infection, but whether any of these toxic proteins undergoes phase separation to manipulate plant defence and how the host copes with this event remain elusive. Here we show that the effector FolSvp2, which is secreted from the fungal pathogen Fusarium oxysporum f. sp. lycopersici (Fol), translocates a tomato iron-sulfur protein (SlISP) from plastids into effector condensates in planta via phase separation. Relocation of SlISP attenuates plant reactive oxygen species production and thus facilitates Fol invasion. The action of FolSvp2 also requires K205 acetylation that prevents ubiquitination-dependent degradation of this protein in both Fol and plant cells. However, tomato has evolved a defence protein, SlPR1. Apoplastic SlPR1 physically interacts with and inhibits FolSvp2 entry into host cells and, consequently, abolishes its deleterious effect. These findings reveal a previously unknown function of PR1 in countering a new mode of effector action.
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Data availability
The LC–MS/MS raw data are publicly available via figshare (FolSvp2 peptides obtained from FolSvp2-GFP expressed in Fol, https://doi.org/10.6084/m9.figshare.24903507.v1 (ref. 60); target proteins obtained from the GFP or FolSvp2-GFP copurified, https://doi.org/10.6084/m9.figshare.24903546.v1 (ref. 61); FolSvp2 peptides obtained from FolSvp2-GFP expressed in tobacco leaves, https://doi.org/10.6084/m9.figshare.24903540.v1 (ref. 62); identification of FolSvp2 K205 acetylation, https://doi.org/10.6084/m9.figshare.25909660 (ref. 63)). Source data are provided with this paper.
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Acknowledgements
This work was financially supported by the National Natural Science Foundation of China (32272489 (J.L.), 32325043 (W.L.)), Key Research and Development Program of Shandong Province (2022CXGC020709) to W.L. and Taishan Scholar Construction Foundation of Shandong Province (tshw20130963) to W.L.
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Contributions
W.L. and J.L. conceived the idea and supervised the project. W.L., J.L. and L.Y. designed the experiments. J.L. and L.Y. performed most of the experiments and analysed data. S.D. and M.G. helped in making some constructs and Fusarium transformation and performed Y2H assays. Y.Y., G.Y. and Y.Z. helped in making constructs. J.L. and W.L. wrote the paper, and all authors contributed to revision.
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Nature Plants thanks Yet-Ran Chen, Yushi Luan and Lay-Sun Ma for their contribution to the peer review of this work.
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Extended data
Extended Data Fig. 1 Generation and analysis of FolSvp2 transformants.
a, Expression profile of FolSvp2 in Fol with or without two-week-old tomato root incubation. The data are presented as the means ± SEs of three independent replicates. b, Genomic DNA was analyzed via PCR to determine which strains were harboring GFP, FolSvp2-GFP, or a K205 mutant (FolSvp2Q-GFP and FolSvp2R-GFP) under the RP27 constitutive promoter. The Histone H4 (FOXG_09402) was used as a positive PCR control. c, Secretion of FolSvp2 in the presence or absence of tomato roots. Conidia of strains harboring FolSvp2-GFP were inoculated into 5% liquid YEPD in the presence or absence of tomato roots. Forty hours after inoculation, proteins were extracted from mycelia or culture supernatants and probed with α-GFP and α-Actin. Coomassie brilliant blue (CBB) or silver staining was used to determine protein loading in each lane. d, Functional validation of the secreted signal peptide (SP) of FolSvp2. The yeast strains were cultured on CMD-W or YPRAA medium for 3 days. TTC was added to the culture supernatant to measure the enzymatic activity for reducing TTC to the red TPF. e, Secretion of FolSvp2 proteins in the presence of tomato roots. Protein extraction and identification were performed as described in (c). f, Homologous recombination-based deletion of FolSvp2. g, PCR analysis to identify the ∆FolSvp2 (KO1, KO9, KO26 and KO37) knockout and wild-type (WT) strains with the primer pairs FolSvp2-out-F/R, FolSvp2-in-F/R and H4-qRT-F/R. h, PCR analysis to identify the WT, ∆FolSvp2, complementation (∆FolSvp2-C) and K205 mutant (∆FolSvp2-CQ, ∆FolSvp2-CR) strains with the native promoter. The primer pairs FolSvp2-pQB-F/R, FolSvp2-pQB-F/pYF11-cGFP-R, FolSvp2-out-F/R and H4-qRT-F/R were used as described above. i, Mycelial growth of the WT, ∆FolSvp2 (∆FolSvp2-KO1), ∆FolSvp2-C, ∆FolSvp2-CQ and ∆FolSvp2-CR mutant strains on the PDA media, complete media (CM), and minimal media (MM) after 5 days of cultivation. Scale bars = 2 cm. j, Mycelial diameter and conidial production of the indicated strains in the indicated media or at the indicated times. No significant difference (ns) was indicated according to multiple comparison tests (mean ± SEM, n = 3). The experiments were performed three times with similar results obtained.
Extended Data Fig. 2 Identification of the ubiquitinated sites in FolSvp2 expressed in Fol and in planta.
a, LC-MS/MS identification of FolSvp2 ubiquitination in Fol. After MG132 treatment for 2 hours, the immunoprecipitated FolSvp2R-GFP was subjected to LC‒MS/MS analysis. The coverage (as highlighted in bold) of the FolSvp2 protein sequence was 75.9%. The ubiquitinated residues identified are highlighted in blue. b, Spectra showing FolSvp2 ubiquitination at K107 and K215. The representative y21 and y10 ions represent the assignment of K107 and K215 ubiquitination, respectively. c, LC-MS/MS identification of FolSvp2 ubiquitination in N. benthamiana. After MG132 treatment for 4 hours, the immunoprecipitated FolSvp2-GFP was subjected to LC‒MS/MS analysis. The coverage (as highlighted in bold) of the FolSvp2 protein sequence was 82.7%. The ubiquitinated residues identified are highlighted in blue. d, Spectrum showing FolSvp2 ubiquitination at K215. The representative y2 ion represents the assignment of K215 ubiquitination.
Extended Data Fig. 3 Localization of FolSvp2 and phenotypic analysis of FolSvp2 overexpression tomato seedlings.
a, Subcellular localization of the WT and K205 mutant FolSvp2-GFP proteins with or without the native signal peptide (ΔSP) in tobacco. The indicated constructs were transiently expressed in nuclear (Nu) marker histone H2B-RFP-overexpressing N. benthamiana, and images were obtained at 3 DAI. The fluorescence intensity profiles of GFP and RFP were assessed along the transects shown as the green and magenta lines. Y-axis, fluorescence intensity (arbitrary units); X-axis, transect length (μm). Scale bars, 50 μm. b, Subcellular localization of GFP and FolSvp2-GFP in tomato. The FolSvp2-GFP protein were overexpressed in two tomato lines (FolSvp2-GFP-OE: #1, #3), and fluorescence was observed in the leaves and roots. The GFP were overexpressed (GFP-OE) in tomato as a control. Scale bars, 40 μm. c, Western blot analysis showing the protein expression described in (b). The extracted proteins were immunoblotted with α-GFP and α-actin. d, DAB staining showing H2O2 production in the indicated tomato root tissues infected with the Fol strain at 3 DAI (top). Microscopy observation of H2O2 accumulation after DAB staining in tomato roots (bottom). Scale bars = 100 µm. e, Quantification of H2O2 in the tomato roots in (d). The mean values (± SEM) of four replicates are shown. f, Resistance of WT, GFP-OE or FolSvp2-GFP-OE tomato seedlings to Fol strain infection at 14 DAI. g, Disease indices were scored at 14 DAI for the 14 plants in (f). (d) to (g) were generated as described in Fig. 5. All the experiments were performed three times with similar results obtained.
Extended Data Fig. 4 Subcellular localization of the WT and CP mutant FolSvp2-GFP proteins in tobacco leaves.
a, Schematic drawing of the WT and CP mutant FolSvp2 constructs without the native signal peptide (ΔSP). b, Subcellular localization of the WT and CP mutant FolSvp2-GFP proteins in N. benthamiana leaves. Images were taken at 3 DAI. Scale bars = 50 µm. c, Western blot analysis showing the expression of FolSvp2 protein in tobacco leaves in (b). Total proteins extracted were probed with α-GFP and α-actin. For (b) and (c), the experiments were repeated three times with similar observations.
Extended Data Fig. 5 Subcellular localization and functional analysis of SlISP in planta.
a, The SlISP-GFP or GFP construct was transiently expressed in N. benthamiana, and images were taken at 3 DAI. Scale bars, 20 μm. b, Western blot analysis showing the expression of the indicated proteins in (a). Total proteins extracted were probed with α-GFP. CBB staining was used to measure protein loading in each lane. c, Fluorescence observation of the roots of the GFP-ovexpressing (GFP-OE) or SlISP-GFP-overexpressing (SlISP-OE4) tomato line. Scale bars, 50 μm. d, Western blot analysis showing the expression of GFP or SlISP-GFP in (c). Total proteins and plastid proteins were extracted and probed with α-GFP and α-actin. Plastid proteins were immunoblotted with α-PetC to visualize the endogenous SlISP. e, Schematic of the WT SlISP target and the two selected guide RNA sequences (gRNA1 and gRNA2). The spacer sequence is shown in the dashed box. Three CRISPR-Cas9-induced SlISP mutants (Slisp-2, Slisp-5, and Slisp-10) in tomato plants were obtained through genetic transformation. The genotype of the mutation in Slisp-2 is based on base substitution and base deletion in the gRNA1 spacer sequence. The genotype of Slisp-5 is a 296-base deletion from positions 50 to 345 of the SlISP sequence. The genotype of Slisp-10 is a single-base deletion in the gRNA1 sequence, as shown by the dashed line. f, Western blot analysis showing the expression of SlISP proteins in the mutant lines. The extracted proteins were probed with anti-SlISP (α-PetC) and α-actin. g, Resistance of WT and CRISPR-Cas9-edited SlISP tomato seedlings to Fol infection. Disease indices of 10 plants were scored at 14 DAI. h, Western blot analysis showing GFP-overexpressing (GFP-OE) and three SlISP-GFP-overexpressing (SlISP-OE2, SlISP-OE4, and SlISP-OE21) tomato lines. Total proteins were extracted and probed with α-GFP and α-actin. i, Resistance of the indicated tomato seedlings to Fol infection. Disease indices (n=10) were scored as described in (g). All the experiments were repeated three times with similar observations.
Extended Data Fig. 6 BiFC assays showing the interaction of SlISP with the WT, IDR2 and CP mutant FolSvp2 proteins.
The indicated constructs were transiently expressed in N. benthamiana leaves for 3 days, after which images were taken. cYFP, C-terminal region of YFP; nYFP, N-terminal region of YFP. Scale bars = 20 µm. The experiments were repeated three times with similar observations.
Extended Data Fig. 7 Interaction of putative tomato PR1 proteins with FolSvp2.
a, Y2H assays showing the interaction of thirteen predicted PR1 proteins with FolSvp2. b, Amino acid sequence alignment of SlPR1 homologs in tomato using DNAMAN. The black line indicates the C-terminal CAPE peptide. The dashed box in red shows the CAPE cleavage motif. The three red asterisks indicate the N-terminal differential sites between SlPR1 and SlP14b. c, Y2H assays showing the interaction of WT and mutant (S101D, K114M and R116G) SlPR1 proteins with FolSvp2. SlP14b was used as the control. For (a) and (c), the experiments were performed three times with similar results.
Extended Data Fig. 8 BiFC assays showing the interaction of the full-length or truncated SlPR1 proteins with FolSvp2 containing the SP of SlPR1.
A schematic of the recombinant FolSvp2 and truncated SlPR1 constructs is shown (left). The indicated constructs were transiently expressed in N. benthamiana leaves for 3 days. Plasmolysis was visualized after treatment with 800 mM mannitol for 6 hours. Scale bars = 50 µm. Experiments were performed three times with similar results.
Extended Data Fig. 9 Interaction of SlPR1 with the WT and mutant FolSvp2 proteins.
a, Y2H assays showing the interaction of SlPR1 with the WT and mutant FolSvp2 proteins. b, Split-LUC assays (left) showing the interaction of SlPR1 with the WT and mutant FolSvp2 proteins without the native signal peptide. Scale bars = 1 cm. Western blot analysis (right) was performed to show the expression of the indicated proteins. Proteins extracted were probed with α-LUC and α-actin. c, Co-IP assays showing the interaction of SlPR1 with the WT and mutant SlPR1SPFolSvp2 proteins. The indicated constructs were transiently expressed in N. benthamiana leaves for 3 days, and the proteins copurified with GFP-Trap beads were probed with α-GFP and α-RFP. The input proteins were subjected to Western blotting with α-GFP, α-RFP and α-actin. All the experiments were repeated three times with similar observations.
Extended Data Fig. 10 Subcellular localization of SlPR1, SlP14b and FolSvp2 in tobacco leaves.
a, Fluorescence images of SlPR1-RFP, CAPE1 mutant SlPR1-RFP and SlP14b-RFP proteins. b, Fluorescence observation of GFP and SlPR1SPFolSvp2-GFP. For (a) and (b), the indicated constructs were transiently expressed in WT or H2B-RFP-overexpressing N. benthamiana leaves for 3 days. Plasmolysis was visualized after treatment with 800 mM mannitol for 6 hours. The experiments were performed three times with similar results. Scale bars = 50 µm.
Supplementary information
Supplementary Table 1
FolSvp2 peptides obtained from FolSvp2-GFP expressed in Fol after LC–MS/MS analysis.
Supplementary Table 2
Target proteins obtained from the GFP or FolSvp2-GFP copurified LC–MS/MS data.
Supplementary Table 3
FolSvp2 peptides obtained from FolSvp2-GFP expressed in tobacco leaves after LC–MS/MS analysis.
Supplementary Table 4
Annotation of 22 candidate FolSvp2-interacting proteins identified via Y2H screening.
Supplementary Table 5
Primers used in this study.
Supplementary Table 6
Synthesized genes used in Y2H study.
Supplementary Data 1
The source data for the charts or graphs.
Source data
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Li, J., Yang, L., Ding, S. et al. Plant PR1 rescues condensation of the plastid iron-sulfur protein by a fungal effector. Nat. Plants 10, 1775–1789 (2024). https://doi.org/10.1038/s41477-024-01811-y
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DOI: https://doi.org/10.1038/s41477-024-01811-y
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