The molecular biology of disease resistance

Keen, N. T.

doi:10.1007/bf00015609

Cited by 161 publications

(39 citation statements)

References 126 publications

(127 reference statements)

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“…Metaperiodate and Glycosidase Treatments-Plasma membrane preparations (5 mg protein/ml) were incubated at 4°C for 16 h in the dark in binding buffer without sucrose but supplemented with 5 mM NaIO 4 and then used in binding experiments. In control experiments, the same concentration of NaIO 4 was added to plasma membrane preparations 30 s before initiation of 125 I-cryptogein binding, which lasted 90 min.…”

Section: Methodsmentioning

confidence: 99%

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Characterization of the Cryptogein Binding Sites on Plant Plasma Membranes

Bourque¹,

Binet²,

Ponchet³

et al. 1999

Journal of Biological Chemistry

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Cryptogein is a 98-amino acid proteinaceous elicitor of tobacco defense reactions. Specific binding of cryptogein to high affinity binding sites on tobacco plasma membranes has been previously reported (K d ‫؍‬ 2 nM; number of binding sites: 220 fmol/mg of protein). In this study, biochemical characterization of cryptogein binding sites reveals that they correspond to a plasma membrane glycoprotein(s) with an N-linked carbohydrate moiety, which is involved in cryptogein binding. Radiation inactivation experiments performed on tobacco plasma membrane preparations indicated that cryptogein bound specifically to a plasma membrane component with an apparent functional molecular mass of 193 kDa. Moreover, using the homobifunctional cross-linking reagent disuccinimidyl suberate and tobacco plasma membranes incubated with 125 I-cryptogein, we identified, after SDS-polyacrylamide gel electrophoresis and autoradiography, two 125 I-cryptogein linked N-glycoproteins of about 162 and 50 kDa. Similar results were obtained using Arabidopsis thaliana and Acer pseudoplatanus plasma membrane preparations, whereas cryptogein did not induce any effects on the corresponding cell suspensions. These results suggest that either cryptogein binds to nonfunctional binding sites, homologues to those present in tobacco plasma membranes, or that a protein involved in signal transduction after cryptogein recognition is absent or inactive in both A. pseudoplatanus and A. thaliana.Most often, the interaction between plants and microorganisms results in an incompatible interaction characterized by multicomponent defense responses such as phytoalexin production or reinforcement of plant cell walls and is sometimes associated with the collapse of the challenged plant cells in the so-called hypersensitive response (1). Such reactions are induced by elicitors, which either originate from the pathogens or are produced from plant cell walls by fungal hydrolytic enzymes (2).Pathogen recognition in cultivar-specific interaction can often be determined by a gene-for-gene relation. Race-specific elicitors, which are encoded directly or indirectly by pathogen avirulence genes, induce resistance in plants carrying the corresponding dominant R genes, whose products were assumed to be receptors for avirulence gene products (3, 4). Many such R genes have been identified (for review, see Ref. 5). Most of them encode cytoplasmic proteins that contain a central nucleotide binding site and a C-terminal domain with a variable number of leucine-rich repeats (5). The N-terminal region contains either leucine zipper motifs or shows homology with the cytoplasmic domain of the Drosophila Toll and mammalian interleukin-1 receptors (6). These nucleotide binding site leucine-rich repeats containing proteins show homologies to proteins regulating apoptosis in mammals and worms (7). Taken together, these results suggest that the corresponding proteins may be involved in a conserved pathway in the response of eukaryotes to pathogens (8), including the hypersensitive response...

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Section: Methodsmentioning

confidence: 99%

“…Race-specific elicitors, which are encoded directly or indirectly by pathogen avirulence genes, induce resistance in plants carrying the corresponding dominant R genes, whose products were assumed to be receptors for avirulence gene products (3,4). Many such R genes have been identified (for review, see Ref.…”

mentioning

confidence: 99%

Characterization of the Cryptogein Binding Sites on Plant Plasma Membranes

Bourque¹,

Binet²,

Ponchet³

et al. 1999

Journal of Biological Chemistry

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“…The second group comprises the race-specific elicitors encoded by Avr (avirulence) genes present in particular races of pathogens that elicit defense responses in plant hosts carrying the corresponding resistance genes. The interaction of these specific elicitors and the gene products underlies the classic gene-forgene interaction (3,4), and it has been postulated that the products of the resistance genes function as receptors for the race-specific elicitors (5).…”

mentioning

confidence: 99%

Sensitivity of Different Ecotypes and Mutants ofArabidopsis thaliana toward the Bacterial Elicitor Flagellin Correlates with the Presence of Receptor-binding Sites

Bauer

Gómez-Gómez

Boller

et al. 2001

Journal of Biological Chemistry

177

144

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“…A simple explanation for this gene-for-gene correspondence is that avr genes generate signals for which resistance genes encode the cognate receptors. A signal transduction pathway then carries the avr-generated signal to a set of target genes, which initiates the HR and other host defenses (1,3,4).…”

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confidence: 99%

“…A variety of avr genes have been cloned from bacterial and fungal phytopathogens (4) and, in at least two cases, gene-forgene interactions have been demonstrated at the molecular level by demonstrating that a purified avr-generated signal molecule will elicit a HR. In the best documented case, two avr genes from the tomato fungal pathogen Cladosporium fulvum, avr9 and avr4, were shown to encode precursors of elicitor peptides.…”

mentioning

confidence: 99%