Biological function of ‘pathogenesis-related’ proteins: four PR proteins of tobacco have 1,3-β-glucanase activity

Kauffmann, Serge; Legrand, Michel; Geoffroy, Philippe; Fritig, Bernard

doi:10.1002/j.1460-2075.1987.tb02637.x

Cited by 468 publications

(253 citation statements)

References 31 publications

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“…When the extracts of TMVtreated leaves were fractionated on denaturing SDS-PAGE the polypeptides of each PR protein class migrated at the following apparent molecular masses; PR-la, lb, lc at 19.5 kD; PR-2,N,O at 34 kD and PR-P,Q at 25 kD (Fig. 1B) (15,17,23). When all three antisera were applied simultaneously to the immunoblot ( Fig.…”

Section: Immunoblot Analysis Of Pr Proteins Induction By Tmvmentioning

confidence: 97%

“…Specificity of Antisera to PR proteins Acidic Isoforms PR protein classes have acidic and basic counterparts that appear to cross react immunologically (15,17). It is important to distinguish between them because readily detectable constitutive levels of mRNA and enzymatic activity of both the basic chitinase and basic (1-3)-,B-glucanases are present in tobacco leaves (22,28,31).…”

Section: Immunoblot Analysis Of Pr Proteins Induction By Tmvmentioning

confidence: 99%

“…The de novo synthesis of PR2 proteins is a ubiquitous reaction of monocot (10,23,33) and dicot plants (2,15) to pathogen attack. Originally characterized in relation to the hypersensitive response induced by TMV in tobacco plants containing the N gene (30), they appear to be part of a nonspecific host response to pathogens (22).…”

mentioning

confidence: 99%

“…The enzymatic functions of two groups of PR proteins have been described. One group, consisting of acidic and basic PR proteins, has (1 -3)-fl-glucanase activity (15); the acidic polypeptides of this group are PR-2, N and 0. A second group consisting of two basic and two acidic proteins has 2 Abbreviations: PR, pathogenesis-related; AVG, -aminoethoxyvinylglycine; STS, silver thiosulfate; TMV, tobacco mosaic virus.…”

mentioning

confidence: 99%

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Xylanase, a Novel Elicitor of Pathogenesis-Related Proteins in Tobacco, Uses a Non-Ethylene Pathway for Induction

Lotan¹,

Fluhr²

1990

Plant Physiol.

140

105

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Antisera to acidic isoforms of pathogenesis-related proteins were used to measure the induction of these proteins in tobacco (Nicotiana tabacum) leaves. Endo-(1-4)-i-xylanase purified from culture filtrates of Trichoderma viride was a strong elicitor of pathogenesis-related protein synthesis in tobacco leaves. The synthesis of these proteins was localized to tissue at the area of enzyme application. The inhibitors of ethylene biosynthesis and ethylene action, 1-aminoethoxyvinylglycine and silver thiosulfate, inhibited accumulation of pathogenesis-related proteins induced by tobacco mosaic virus and a-aminobutyric acid, but did not inhibit elicitation by xylanase. Likewise, the induction of these proteins by the tobacco pathogen Pseudomonas syringae pv. tabaci was not affected by the inhibitors of ethylene biosynthesis and action. The leaf response to tobacco mosaic virus and aaminobutyric acid was dependent on light in normal and photosynthetically incompetent leaves. In contrast, the response of leaves to xylanase was independent of light. Tobacco mosaic virus and a-aminobutyric acid induced concerted accumulation of pathogenesis-related proteins. However, xylanase elicited the accumulation of only a subset of these proteins. Specifically, the plant (1-3)-,6-glucanases, which are normally a part of the concerted response, were underrepresented. These experiments have revealed the presence of a novel ethylene-independent pathway for pathogenesis-related protein induction that is activated by xylanase.The de novo synthesis of PR2 proteins is a ubiquitous reaction of monocot (10,23,33)

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Section: Immunoblot Analysis Of Pr Proteins Induction By Tmvmentioning

confidence: 97%

Section: Immunoblot Analysis Of Pr Proteins Induction By Tmvmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Xylanase, a Novel Elicitor of Pathogenesis-Related Proteins in Tobacco, Uses a Non-Ethylene Pathway for Induction

Lotan¹,

Fluhr²

1990

Plant Physiol.

140

105

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“…[ 3 H]Laminarin, an algal ␤-1,3-glucan known to be digested by all ␤-1,3-glucanase isoforms (Kauffmann et al, 1987;Beffa et al, 1993), was utilized for the ␤-1,3-glucanase assays and [ 3 H]chitin as a substrate for chitinase. The reduced forms of these substrates were used, making the activities measured specific for the endo-type isoforms of these enzymes.…”

Section: Coordinate Accumulation Of ␤-13-glucanase and Chitinase In mentioning

confidence: 99%

Class I β-1,3-Glucanase and Chitinase Are Expressed in the Micropylar Endosperm of Tomato Seeds Prior to Radicle Emergence

et al. 2001

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β-1,3-Glucanase (EC 3.2.1.39) and chitinase (EC 3.2.1.14) mRNAs, proteins, and enzyme activities were expressed specifically in the micropylar tissues of imbibed tomato (Lycopersicon esculentum Mill.) seeds prior to radicle emergence. RNA hybridization and immunoblotting demonstrated that both enzymes were class I basic isoforms. β-1,3-Glucanase was expressed exclusively in the endosperm cap tissue, whereas chitinase localized to both endosperm cap and radicle tip tissues. β-1,3-Glucanase and chitinase appeared in the micropylar tissues of gibberellin-deficient gib-1tomato seeds only when supplied with gibberellin. Accumulation of β-1,3-glucanase mRNA, protein and enzyme activity was reduced by 100 μM abscisic acid, which delayed or prevented radicle emergence but not endosperm cap weakening. In contrast, expression of chitinase mRNA, protein, and enzyme activity was not affected by abscisic acid. Neither of these enzymes significantly hydrolyzed isolated tomato endosperm cap cell walls. Although both β-1,3-glucanase and chitinase were expressed in tomato endosperm cap tissue prior to radicle emergence, we found no evidence that they were directly involved in cell wall modification or tissue weakening. Possible functions of these hydrolases during tomato seed germination are discussed.

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Engineering Pathogen Resistance in Crop Plants

Campbell

Fitzgerald

Ronald

2004

Handbook of Plant Biotechnology

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As the world population continues to increase, food supplies must also grow to meet nutritional requirements. One means of ensuring the stability and plentitude of the food supply is to mitigate crop loss caused by plant pathogens. Strategies for combating disease include traditional technologies such as plant breeding and chemical applications; current technologies such as generating transgenic plants that express components of known defense signaling pathways; and the adaptation of newer technologies such as RNA silencing of pathogen and plant transcripts. Breeding has been used to pyramid resistance (R) genes into many different plants including rice. Chemical strategies include application of salicylic acid (SA) analogs to stimulate systemic acquired resistance (SAR) responses. Genetic screens in Arabidopsis have identified genes controlling SAR and these genes have been manipulated and used to engineer crop plants. The diseases caused by plant viruses are being thwarted through the initiation of endogenous RNA silencing mechanisms. Many of these strategies show great promise, some limitations, and exciting opportunities to develop many new tools for combating plant pests.

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Biological function of ‘pathogenesis-related’ proteins: four PR proteins of tobacco have 1,3-β-glucanase activity

Cited by 468 publications

References 31 publications

Xylanase, a Novel Elicitor of Pathogenesis-Related Proteins in Tobacco, Uses a Non-Ethylene Pathway for Induction

Xylanase, a Novel Elicitor of Pathogenesis-Related Proteins in Tobacco, Uses a Non-Ethylene Pathway for Induction

Class I β-1,3-Glucanase and Chitinase Are Expressed in the Micropylar Endosperm of Tomato Seeds Prior to Radicle Emergence

Engineering Pathogen Resistance in Crop Plants

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