A Bacterial Tyrosine Phosphatase Inhibits Plant Pattern Recognition Receptor Activation

Macho, Alberto P.; Schwessinger, Benjamin; Ntoukakis, Vardis; Brutus, Alexandre; Segonzac, Cécile; Roy, Sonali; Kadota, Yasuhiro; Oh, Man‐Ho; Sklenář, Jan; Derbyshire, Paul; Lozano‐Durán, Rosa; Malinovsky, Frederikke Gro; Monaghan, Jacqueline; Menke, Frank L.H.; Huber, Steven C.; He, Sheng Yang; Zipfel, Cyril

doi:10.1126/science.1248849

Cited by 161 publications

(171 citation statements)

References 25 publications

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“…The ROS burst peaks at 5e10 min in plants triggered by flg22 [12,14,21], at 10e20 min by elongation factor Tu (EF-Tu) [25], and at 35e40 min by Pseudomonas syringae [26]. In our study, the accumulation of H 2 O 2, as a main form of ROS, peaks at 5 min in tomato leaves triggered by PopW (Fig.…”

Section: Discussionsupporting

confidence: 49%

PopW activates PAMP-triggered immunity in controlling tomato bacterial spot disease

Tian

Wang

Zhou

et al. 2015

Biochemical and Biophysical Research Communications

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Section: Discussionsupporting

confidence: 49%

PopW activates PAMP-triggered immunity in controlling tomato bacterial spot disease

Tian

Wang

Zhou

et al. 2015

Biochemical and Biophysical Research Communications

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“…1C and D). Furthermore, we also mutated Tyr-5 and Tyr-110 to glutamate (E), alone or in conjunction with ␤C1-2D, to generate triple mutants (␤C1-2D-Y5E and ␤C1-2D-Y110E) or a quadruple mutant (␤C1-2D-Y5E/Y110E [␤C1-2D/2E]) and examined Tyr-5 and Tyr-110 in TYLCCNB-␤C1 in N. benthamiana plants by immunoprecipitation, followed by antibody against phosphorylated tyrosine as described previously (32). As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Mimic Phosphorylation of a βC1 Protein Encoded by TYLCCNB Impairs Its Functions as a Viral Suppressor of RNA Silencing and a Symptom Determinant

Zhong

Wang

Xiao

et al. 2017

J Virol

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Phosphorylation of the ␤C1 protein encoded by the betasatellite of tomato yellow leaf curl China virus (TYLCCNB-␤C1) by SNF1-related protein kinase 1 (SnRK1) plays a critical role in defense of host plants against geminivirus infection in Nicotiana benthamiana. However, how phosphorylation of TYLCCNB-␤C1 impacts its pathogenic functions during viral infection remains elusive. In this study, we identified two additional tyrosine residues in TYLCCNB-␤C1 that are phosphorylated by SnRK1. The effects of TYLCCNB-␤C1 phosphorylation on its functions as a viral suppressor of RNA silencing (VSR) and a symptom determinant were investigated via phosphorylation mimic mutants in N. benthamiana plants. Mutations that mimic phosphorylation of TYLCCNB-␤C1 at tyrosine 5 and tyrosine 110 attenuated disease symptoms during viral infection. The phosphorylation mimics weakened the ability of TYLCCNB-␤C1 to reverse transcriptional gene silencing and to suppress posttranscriptional gene silencing and abolished its interaction with N. benthamiana ASYMMETRIC LEAVES 1 in N. benthamiana leaves. The mimic phosphorylation of TYLCCNB-␤C1 had no impact on its protein stability, subcellular localization, or self-association. Our data establish an inhibitory effect of phosphorylation of TYLCCNB-␤C1 on its pathogenic functions as a VSR and a symptom determinant and provide a mechanistic explanation of how SnRK1 functions as a host defense factor. IMPORTANCE Tomato yellow leaf curl China virus (TYLCCNV), which causes a severe yellow leaf curl disease in China, is a monopartite geminivirus associated with the betasatellite (TYLCCNB). TYLCCNB encodes a single pathogenicity protein, ␤C1 (TYLCCNB-␤C1), which functions as both a viral suppressor of RNA silencing (VSR) and a symptom determinant. Here, we show that mimicking phosphorylation of TYLCCNB-␤C1 weakens its ability to reverse transcriptional gene silencing, to suppress posttranscriptional gene silencing, and to interact with N. benthamiana ASYMMETRIC LEAVES 1. To our knowledge, this is the first report establishing an inhibitory effect of phosphorylation of TYLCCNB-␤C1 on its pathogenic functions as both a VSR and a symptom determinant and to provide a mechanistic explanation of how SNF1-related protein kinase 1 acts as a host defense factor. These findings expand the scope of phosphorylation-mediated defense mechanisms and contribute to further understanding of plant defense mechanisms against geminiviruses.KEYWORDS TYLCCNB-␤C1, Nicotiana benthamiana, SnRK1, geminivirus, host defense factor, posttranscriptional gene silencing, protein phosphorylation, transcriptional gene silencing

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“…As the direct target proteins for both T3Es are still not known, it is possible that both T3Es could directly or indirectly associate with the UPS to modulate proteasome activity. The Tyr phosphatase HopAO1 targets the Arabidopsis receptor kinases EF-TU RECEPTOR and FLS2, reducing their Tyr phosphorylation and thus inhibiting PTI activation (Macho et al, 2014). Because the phosphorylation of certain proteasome subunits is crucial to activate its assembly and also induce its activity (Satoh et al, 2001), it might be possible that HopAO1 could target components of the proteasome to reduce their phosphorylation status.…”

Section: Discussionmentioning

confidence: 99%

The Proteasome Acts as a Hub for Plant Immunity and Is Targeted by Pseudomonas Type III Effectors

et al. 2016

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A Bacterial Tyrosine Phosphatase Inhibits Plant Pattern Recognition Receptor Activation

Cited by 161 publications

References 25 publications

PopW activates PAMP-triggered immunity in controlling tomato bacterial spot disease

PopW activates PAMP-triggered immunity in controlling tomato bacterial spot disease

Mimic Phosphorylation of a βC1 Protein Encoded by TYLCCNB Impairs Its Functions as a Viral Suppressor of RNA Silencing and a Symptom Determinant

The Proteasome Acts as a Hub for Plant Immunity and Is Targeted by Pseudomonas Type III Effectors

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