Signal transduction in systemic acquired resistance.

Ryals, John; Lawton, Kay A.; Delaney, Terrence P.; Friedrich, Leslie; Keßmann, Helmut; Neuenschwander, Urs; Uknes, Scott; Vernooij, Bernard; Weymann, Kris

doi:10.1073/pnas.92.10.4202

Cited by 138 publications

(58 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…4A). However, mkk1/2 and mpk4 supported significantly less bacterial growth, whereas the positive controls NahG (Ryals et al, 1995) and atgsnor1-3 (Feechan et al, 2005) showed higher levels of bacterial growth. The resistance of mkk1/2 to Pst DC3000 can be partly attributed to the enhanced ET production of the double mutant but more obviously by its SA content, because both the mkk1/2/ein2 (ET insensitive) and the mkk1/2/sid2 (reduced SA production) triple mutants carried a greater bacterial load than mkk1/2 alone (Fig.…”

Section: Disease Responses Of Mkk1/2mentioning

confidence: 99%

Arabidopsis Mitogen-Activated Protein Kinase Kinases MKK1 and MKK2 Have Overlapping Functions in Defense Signaling Mediated by MEKK1, MPK4, and MKS1

et al. 2008

View full text Add to dashboard Cite

The Arabidopsis (Arabidopsis thaliana) MKK1 and MKK2 mitogen-activated protein kinase kinases have been implicated in biotic and abiotic stress responses as part of a signaling cascade including MEKK1 and MPK4. Here, the double loss-offunction mutant (mkk1/2) of MKK1 and MKK2 is shown to have marked phenotypes in development and disease resistance similar to those of the single mekk1 and mpk4 mutants. Because mkk1 or mkk2 single mutants appear wild type, basal levels of MPK4 activity are not impaired in them, and MKK1 and MKK2 are in part functionally redundant in unchallenged plants. These findings are confirmed and extended by biochemical and molecular analyses implicating the kinases in jasmonate-and salicylate-dependent defense responses, mediated in part via the MPK4 substrate MKS1. In addition, transcriptome analyses delineate overlapping and specific effects of the kinases on global gene expression patterns demonstrating both redundant and unique functions for MKK1 and MKK2.

show abstract

Section: Disease Responses Of Mkk1/2mentioning

confidence: 99%

Arabidopsis Mitogen-Activated Protein Kinase Kinases MKK1 and MKK2 Have Overlapping Functions in Defense Signaling Mediated by MEKK1, MPK4, and MKS1

et al. 2008

View full text Add to dashboard Cite

show abstract

“…In the last decade, particular attention has been turned toward understanding mechanisms that govern plant-microbe interactions and to unravel the processes that lead to plant resistance (Dixon et al, 1994;Jones, 1994;Ryan, 1994;Ryals et al, 1995;Staskawicz et al, 1995;Ji et al, 1998;Keen, 1999). However, the general molecular basis of plant-pathogen recognition controlling plant resistance remains to be elucidated.…”

Section: Introductionmentioning

confidence: 99%

Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

Osman¹,

Vauthrin²,

Mikeš

et al. 2001

MBoC

104

View full text Add to dashboard Cite

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionality. However, these proteins were strongly altered in their sterol-loading efficiency, specific binding to high-affinity sites, and activities on tobacco cells. Ligand replacement experiments strongly suggest that the formation of a sterol-elicitin complex is a requisite step before elicitins fasten to specific binding sites. This was confirmed with the use of two sterol-preloaded elicitins. Both more rapidly displaced labeled cryptogein from its specific binding sites than the unloaded proteins. Moreover, the binding kinetics of elicitins are related to their biological effects, which constitutes the first evidence that binding sites could be the biological receptors. The first event involved in elicitin-mediated cell responses is proposed to be the protein loading with a sterol molecule.

show abstract

“…Both responses are initiated at the site of attack but eventually involve mobile messengers that communicate a localized defense alert throughout naive regions of the plant (Malamy et al, 1990;Pearce et al, 1991;Ryals et al, 1995). Both responses involve the biosynthesis of toxic compounds such as phytoalexins, which presumably retard the invasion of microbes and macroscopic herbivores (Nicholson, 1992;Davis et al, 1993;Nojiri et al, 1996).…”

mentioning

confidence: 99%

Systemin Potentiates the Oxidative Burst in Cultured Tomato Cells1

et al. 1998

View full text Add to dashboard Cite

Plants that have been wounded by insects or other herbivores may be more susceptible to infection by adventitious microbes. Wound-induced signal molecules, which serve to induce responses in the plant that retard further feeding, might also act to prepare a plant for possible pathogen attack. We have examined the effect of a wound-generated systemic messenger (systemin) on a pathogen-stimulated defense-response marker, the oxidative burst. We observed that neither systemin nor its inactive analog (A-17) was able to directly induce H

show abstract

Signal transduction in systemic acquired resistance.

Cited by 138 publications

References 22 publications

Arabidopsis Mitogen-Activated Protein Kinase Kinases MKK1 and MKK2 Have Overlapping Functions in Defense Signaling Mediated by MEKK1, MPK4, and MKS1

Arabidopsis Mitogen-Activated Protein Kinase Kinases MKK1 and MKK2 Have Overlapping Functions in Defense Signaling Mediated by MEKK1, MPK4, and MKS1

Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

Systemin Potentiates the Oxidative Burst in Cultured Tomato Cells1

Contact Info

Product

Resources

About