The Pseudomonas AvrPto Protein Is Differentially Recognized by Tomato and Tobacco and Is Localized to the Plant Plasma Membrane

Shan, Libo; Thara, Venkatappa K.; Martin, Gregory B.; Zhang, Jianmin; Tang, Xiaoyan

doi:10.2307/3871232

Cited by 58 publications

(111 citation statements)

References 9 publications

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“…Two non-NBS-LRR R proteins with PK activity, FEN and PTO, are myristoylated in tomato (6,80). Both these proteins are induced by avrPto, a myristoylated secreted protein from bacteria (81). MYR appears to be involved in the R mechanisms of many higher plants (see also Refs.…”

Section: Transduction Pathways Involve a Large Number Of N-myristoylamentioning

confidence: 99%

Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote

Boisson¹,

Giglione

Meinnel

2003

Journal of Biological Chemistry

143

157

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N-Myristoylation is an irreversible modification that affects the membrane binding properties of crucial cytoplasmic proteins from signal transduction cascades. We characterized the two putative N-myristoyltransferases of Arabidopsis thaliana as a means of investigating the entire N-myristoylation proteome (N-myristoylome) in a higher eukaryote. AtNMT1 compensated for the nmt1 defect in yeast, whereas AtNMT2 and chimeras of the two genes did not. Only AtNMT1 modified known N-myristoylated proteins in vitro. AtNMT1 is therefore responsible for the A. thaliana N-myristoylome, whereas AtNMT2 does not seem to have usual myristoylation activity. We began with the whole set of N-myristoylated G proteins in the A. thaliana proteome. We then used a reiterative approach, based on the in vitro N-myristoylation of more than 60 different polypeptides, to determine the substrate specificity of AtNMT1. We found that the positive charge on residue 7 of the substrate was particularly important in substrate recognition. The A. thaliana N-myristoylome consists of 437 proteins, accounting for 1.7% of the complete proteome. We demonstrated the N-myristoylation of several unexpected protein families, including innate immunity proteins, thioredoxins, components of the protein degradation pathway, transcription factors, and a crucial regulatory enzyme of glycolysis. The role of N-myristoylation is discussed in each case; in particular, this process may underlie the "guard" hypothesis of innate immunity.

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Section: Transduction Pathways Involve a Large Number Of N-myristoylamentioning

confidence: 99%

Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote

Boisson¹,

Giglione

Meinnel

2003

Journal of Biological Chemistry

143

157

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“…Myristoylation is a eukaryotic-specific posttranslational modification that often is used in combination with palmitoylation to target proteins to the plasma membrane (49). Multiple P. syringae T3Es acylated and localized to the plasma membrane once delivered into plant cell by the type III secretion system (50)(51)(52)(53)(54).…”

Section: Hr Triggered By Avrxv3 In Tomato Is Also Dependent On Its Pumentioning

confidence: 99%

Pseudomonas syringae type III effector HopAF1 suppresses plant immunity by targeting methionine recycling to block ethylene induction

Washington

Mukhtar

Finkel

et al. 2016

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

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HopAF1 is a type III effector protein of unknown function encoded in the genomes of several strains of Pseudomonas syringae and other plant pathogens. Structural modeling predicted that HopAF1 is closely related to deamidase proteins. Deamidation is the irreversible substitution of an amide group with a carboxylate group. Several bacterial virulence factors are deamidases that manipulate the activity of specific host protein substrates. We identified Arabidopsis methylthioadenosine nucleosidase proteins MTN1 and MTN2 as putative targets of HopAF1 deamidation. MTNs are enzymes in the Yang cycle, which is essential for the high levels of ethylene biosynthesis in Arabidopsis. We hypothesized that HopAF1 inhibits the host defense response by manipulating MTN activity and consequently ethylene levels. We determined that bacterially delivered HopAF1 inhibits ethylene biosynthesis induced by pathogenassociated molecular patterns and that Arabidopsis mtn1 mtn2 mutant plants phenocopy the effect of HopAF1. Furthermore, we identified two conserved asparagines in MTN1 and MTN2 from Arabidopsis that confer loss of function phenotypes when deamidated via site-specific mutation. These residues are potential targets of HopAF1 deamidation. HopAF1-mediated manipulation of Yang cycle MTN proteins is likely an evolutionarily conserved mechanism whereby HopAF1 orthologs from multiple plant pathogens contribute to disease in a large variety of plant hosts.

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“…When delivered to or expressed in plant cells, a large number of bacterial effectors localize to the plasma membrane through their N-myristoylation motifs, including Pst effectors AvrB, AvrRpm1, AvrPphB, AvrPto, and HopF2 (Göhre et al, 2008;Nimchuk et al, 2000;RobertSeilaniantz et al, 2006;Shan et al, 2000;Xiang et al, 2008). XopR also localizes to the plasma membrane in plant cells.…”

Section: Discussionmentioning

confidence: 99%

A Xanthomonas oryzae pv. oryzae effector, XopR, associates with receptor-like cytoplasmic kinases and suppresses PAMP-triggered stomatal closure

Wang

Sun

Fan

et al. 2016

Sci. China Life Sci.

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Receptor-like kinases (RLKs) play important roles in plant immunity signaling; thus, many are hijacked by pathogen effectors to promote successful pathogenesis. Xanthomonas oryzae pv. oryzae (Xoo) is the causal agent of rice leaf blight disease. The strain PXO99A has 18 non-TAL (transcription activation-like) effectors; however, their mechanisms of action and host target proteins remain largely unknown. Although the effector XopR from the Xoo strain MAFF311018 was shown to suppress PAMP-triggered immune responses in Arabidopsis, its target has not yet been identified. Here, we show that PXO99A XopR interacts with BIK1 at the plasma membrane. BIK1 is a receptor-like cytoplasmic kinase (RLCK) belonging to the RLK family of proteins and mediates PAMP-triggered stomatal immunity. In turn, BIK1 phosphorylates XopR. Furthermore, XopR suppresses PAMP-triggered stomatal closure in transgenic Arabidopsis expressing XopR. In addition, XopR is able to associate with RLCKs other than BIK1. These results suggest that XopR likely suppresses plant immunity by targeting BIK1 and other RLCKs. Xanthomonas, effector, XopR, BIK1, immunity Citation:Wang, S., Sun, J., Fan, F., Tan, Z., Zou, Y., and Lu, D. (2016). A Xanthomonas oryzae pv. oryzae effector, XopR, associates with receptor-like cytoplasmic kinases and suppresses PAMP-triggered stomatal closure. Sci China Life Sci 59, 897 -905.

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The Pseudomonas AvrPto Protein Is Differentially Recognized by Tomato and Tobacco and Is Localized to the Plant Plasma Membrane

Cited by 58 publications

References 9 publications

Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote

Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote

Pseudomonas syringae type III effector HopAF1 suppresses plant immunity by targeting methionine recycling to block ethylene induction

A Xanthomonas oryzae pv. oryzae effector, XopR, associates with receptor-like cytoplasmic kinases and suppresses PAMP-triggered stomatal closure

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