Two Distinct Pseudomonas Effector Proteins Interact with the Pto Kinase and Activate Plant Immunity

Kim, Young Jin; Lin, Nai-Chun; Martin, Gregory B.

doi:10.1016/s0092-8674(02)00743-2

Cited by 269 publications

(240 citation statements)

References 40 publications

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“…Mutation of this residue to the smaller residue Ala (Figure 5A) or the charged residue Asp (Wu et al, 2004) greatly impairs its interaction with Pto. By contrast, the substitution L205I still interacted with AvrPtoB (Kim et al, 2002), presumably because Ile has a similar size to Leu. Asn-251 in Pto is involved in interaction with AvrPtoB but not with AvrPto.…”

Section: Discussionmentioning

confidence: 90%

“…Extensive mutational analysis and yeast two-hybrid (Y2H) studies have demonstrated that interaction between Pto and AvrPto or AvrPtoB is the molecular basis for pathogen recognition and activation of the immune response Tang et al, 1996;Kim et al, 2002). Prf, a protein with a nucleotide binding site and leucine-rich repeats, is required for Pto-mediated resistance to Pst (Salmeron et al, 1996), and Pto/Prf have been shown to occur in a complex in the plant cell (Salmeron et al, 1996;Mucyn et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

“…Interaction between Pto and AvrPto is highly specific; AvrPto does not interact with the Fen kinase, a closely related Pto family member that shares >80% sequence identity with Pto Tang et al, 1996;Jia et al, 1997;Frederick et al, 1998;Chang et al, 2001;Kim et al, 2002). The inability of Fen to interact with AvrPto stems from the fact that three residues, His-49, Val-51, and Thr-204, important for Pto recognition of AvrPto, are not conserved in Fen (Xing et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Crystal Structure of the Complex between Pseudomonas Effector AvrPtoB and the Tomato Pto Kinase Reveals Both a Shared and a Unique Interface Compared with AvrPto-Pto

et al. 2009

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Resistance to bacterial speck disease in tomato (Solanum lycopersicum) is activated upon recognition by the host Pto kinase of either one of two sequence-unrelated effector proteins, AvrPto or AvrPtoB, from Pseudomonas syringae pv tomato (Pst). Pto induces Pst immunity by acting in concert with the Prf protein. The recently reported structure of the AvrPto-Pto complex revealed that interaction of AvrPto with Pto appears to relieve an inhibitory effect of Pto, allowing Pto to activate Prf. Here, we present the crystal structure of the Pto binding domain of AvrPtoB (residues 121 to 205) at a resolution of 1.9Å and of the AvrPtoB121-205–Pto complex at a resolution of 3.3 Å. AvrPtoB121-205 exhibits a tertiary fold that is completely different from that of AvrPto, and its conformation remains largely unchanged upon binding to Pto. In common with AvrPto-Pto, the AvrPtoB-Pto complex relies on two interfaces. One of these interfaces is similar in both complexes, although the primary amino acid sequences from the two effector proteins are very different. Amino acid substitutions in Pto at the other interface disrupt the interaction of AvrPtoB-Pto but not that of AvrPto-Pto. Interestingly, substitutions in Pto affecting this unique interface also cause Pto to induce Prf-dependent host cell death independently of either effector protein.

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Section: Discussionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Crystal Structure of the Complex between Pseudomonas Effector AvrPtoB and the Tomato Pto Kinase Reveals Both a Shared and a Unique Interface Compared with AvrPto-Pto

et al. 2009

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“…oryzicola, which does not cause disease on maize, and the maize͞sorghum pathogen B. andropogonis. The ability of a single gene such as Rxo1 to confer resistance to two distantly related pathogen species is unusual but not unprecedented (33)(34)(35)(36). One possible explanation is that the Rxo1 gene recognizes the same avr gene products in both bacterial species.…”

Section: Resultsmentioning

confidence: 99%

A maize resistance gene functions against bacterial streak disease in rice

Zhao

Lin

Poland

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

226

151

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Although cereal crops all belong to the grass family (Poacea), most of their diseases are specific to a particular species. Thus, a given cereal species is typically resistant to diseases of other grasses, and this nonhost resistance is generally stable. To determine the feasibility of transferring nonhost resistance genes (R genes) between distantly related grasses to control specific diseases, we identified a maize R gene that recognizes a rice pathogen, Xanthomonas oryzae pv. oryzicola, which causes bacterial streak disease. Bacterial streak is an important disease of rice in Asia, and no simply inherited sources of resistance have been identified in rice. Although X. o. pv. oryzicola does not cause disease on maize, we identified a maize gene, Rxo1, that conditions a resistance reaction to a diverse collection of pathogen strains. Surprisingly, Rxo1 also controls resistance to the unrelated pathogen Burkholderia andropogonis, which causes bacterial stripe of sorghum and maize. The same gene thus controls resistance reactions to both pathogens and nonpathogens of maize. Rxo1 has a nucleotide-binding siteleucine-rich repeat structure, similar to many previously identified R genes. Most importantly, Rxo1 functions after transfer as a transgene to rice, demonstrating the feasibility of nonhost R gene transfer between cereals and providing a valuable tool for controlling bacterial streak disease.disease resistance ͉ nonhost resistance ͉ Xanthomonas

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“…Intact AvrPtoB elicits immunity-associated PCD on Ptoexpressing tomato plants (RG-PtoR); however, AvrPtoB does not elicit PCD on the susceptible RG-pto11 or RG-prf3 tomato lines (18) (Fig. 3B; and see Fig.…”

Section: Identification Of a Domain In The Avrptob C Terminus Requirementioning

confidence: 99%

Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity

Abramovitch

Janjusevic

Stebbins

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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207

160

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Microbial pathogens of both plants and animals employ virulence factors that suppress the host immune response. The tomato pathogen Pseudomonas syringae injects the AvrPtoB type III effector protein into the plant cell to suppress programmed cell death (PCD) associated with plant immunity. AvrPtoB also inhibits PCD in yeast, indicating that AvrPtoB manipulates a conserved component of eukaryotic PCD. To identify host targets of AvrPtoB, we performed a yeast two-hybrid screen and identified tomato ubiquitin (Ub) as a strong AvrPtoB interactor. AvrPtoB is ubiquitinated in vitro and exhibits E3 Ub ligase activity in the presence of recombinant E1 activating enzyme and specific E2 Ub-conjugating enzymes. The C terminus of AvrPtoB is sufficient for both anti-PCD and E3 Ub ligase activities, suggesting the two functions are associated. Indeed, mutation of AvrPtoB lysine residues in the C terminus, between K512 and K529, disrupts AvrPtoB-Ub interactions, decreases AvrPtoB-mediated anti-PCD activity, and abrogates P. syringae pathogenesis of susceptible tomato plants. Remarkably, quantitative decreases in AvrPtoB anti-PCD activity are correlated with decreases in AvrPtoB ubiquitination and E3 Ub ligase activity. Overall, these data reveal a unique bacterial pathogenesis strategy, where AvrPtoB manipulates the host Ub system and requires intrinsic E3 Ub ligase activity to suppress plant immunity.pathogenesis ͉ plant disease ͉ programmed cell death ͉ ubiquitin ͉ Pseudomonas

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Two Distinct Pseudomonas Effector Proteins Interact with the Pto Kinase and Activate Plant Immunity

Cited by 269 publications

References 40 publications

Crystal Structure of the Complex between Pseudomonas Effector AvrPtoB and the Tomato Pto Kinase Reveals Both a Shared and a Unique Interface Compared with AvrPto-Pto

Crystal Structure of the Complex between Pseudomonas Effector AvrPtoB and the Tomato Pto Kinase Reveals Both a Shared and a Unique Interface Compared with AvrPto-Pto

A maize resistance gene functions against bacterial streak disease in rice

Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity

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