Ethylene Biosynthesis-Inducing Protein from Cellulysin Is an Endoxylanase

Fuchs, Yoram; Saxena, Abha; Gamble, H. Ray; Anderson, James D.

doi:10.1104/pp.89.1.138

Cited by 97 publications

(58 citation statements)

References 24 publications

(27 reference statements)

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“…Because many of these chemicals (except salicylic acid) trigger ethylene biosynthesis, chemical elicitation of PR protein accumulation may be via ethylene. Recently, an endoxylanase has been purified from culture filtrates of Trichoderma viride and has been identified as the ethylene-inducing factor in Cellulysin (a commercial cellulase-containing product) (13). Here we show that this enzyme induces synthesis of PR proteins when applied directly to tobacco leaves.…”

mentioning

confidence: 74%

“…Experiments involving ethylene evolution have been carried out on leaf discs (6,13). We wished to confirm the biosynthesis ofethylene and its inhibition in our experimental system, i.e.…”

Section: -Ethylene-and Non-ethylene-dependent Pathways In Pr-pq Inmentioning

confidence: 99%

“…Purified (I-4)-j3-endoxylanase from T. viridi cultures has been shown to elicit ethylene production in tobacco leaf discs (13). Since ethylene has been correlated with induction of PR proteins, we tested the ability of xylanase to induce the accumulation of PR proteins.…”

Section: Immunoblot Analysis Of Pr Proteins Induction By Tmvmentioning

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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mentioning

confidence: 74%

“…Experiments involving ethylene evolution have been carried out on leaf discs (6,13). We wished to confirm the biosynthesis ofethylene and its inhibition in our experimental system, i.e.…”

Section: -Ethylene-and Non-ethylene-dependent Pathways In Pr-pq Inmentioning

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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“…The 22-kD fungal protein ethylene-inducing xylanase (EIX; Fuchs et al, 1989) induces ethylene biosynthesis, electrolyte leakage, pathogensis-related protein expression, and HR in specific plant species and/or varieties (Bailey et al, 1990(Bailey et al, , 1993Ron et al, 2000;Elbaz et al, 2002). Analysis of EIX mutants lacking enzymatic activity (b-1-4-endoxylanase) but retaining elicitation activity showed that the xylanase activity is not required for the HR elicitation process because the protein per se functions as the elicitor (Enkerli et al, 1999;FurmanMatarasso et al, 1999;Rotblat et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

The Receptor for the Fungal Elicitor Ethylene-Inducing Xylanase Is a Member of a Resistance-Like Gene Family in Tomato

2004

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An ethylene-inducing xylanase (EIX) is a potent elicitor of plant defense responses in specific cultivars of tobacco (Nicotiana tabacum) and tomato (Lycopersicon esculentum). The LeEix locus in tomatoes was characterized by map-based cloning, which led to the identification of a novel gene cluster from which two members (LeEix1 and LeEix2) were isolated. Similar to the tomato Ve resistance genes in tomato plants, the deduced amino acid sequences encoded by LeEix1 and LeEix2 contain a Leu zipper, an extracellular Leu-rich repeat domain with glycosylation signals, a transmembrane domain, and a C-terminal domain with a mammalian endocytosis signal. Silencing expression of the LeEix genes prevented the binding of EIX to cells of an EIX-responsive plant and thus inhibited the hypersensitive response. Overexpression of either LeEix1 or LeEix2 genes in EIX-nonresponsive tobacco plants enabled the binding of EIX, although only LeEix2 could transmit the signal that induced the hypersensitive response. Overexpressing LeEix2 in mammalian COS-7 cells enables binding of EIX, indicating physical interaction between the EIX elicitor and LeEix2 gene product. Structural analysis of the LeEix proteins suggests that they belong to a class of cell-surface glycoproteins with a signal for receptor-mediated endocytosis. Mutating the endocytosis signal in LeEix2 (Tyr 993 to Ala) abolished its ability to induce the hypersensitive response, suggesting that endocytosis plays a key role in the signal transduction pathway

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“…The enzyme apparently degrades P-1,4-xylan linkages in the plant cell wall and is an exceptionally potent inducer of chitinase accumulation. It also promotes ethylene evolution (Fuchs et al, 1989); nevertheless, ethylene is not required in its mode of action (Lotan and Fluhr, 1990b).…”

Section: Introductionmentioning

confidence: 99%

Calcium Requirement for Ethylene-Dependent Responses.

1992

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Ethylene, a gaseous plant hormone, plays a role in plant development, defense, and climactericfruit ripening. Both genetic and biochemical evidence suggest that the response of plants to ethylene is mediated by a specific ethylene receptor. The signal emanating from the receptor-effector complex is then presumably transduced via an unknown cascade pathway. We have used the plant pathogenesis response, exemplified by the induction of the pathogenesis-related gene chitinase, as a paradigm to investigate ethylene-dependent signal transduction in the plant cell. We showed that calcium is necessarily involved in the ethylene-mediated pathogenesis response. Blocking calcium fluxes with chelators inhibited ethylene-dependent induction of chitinase accumulation, but not ethylene independent induction. Artificially increasing cytosolic calcium levels by treatments with the calcium ionophore ionomycin or the calcium pump blocker thapsigargin stimulated chitinase accumulation. Plants grown in calcium-poor soil showed a 10-fold reduction in leaf extractable calcium. Their leaves exhibited a reduced pathogenesis reaction to ethylene and were impaired in another hormone response mediated by calcium, i.e., abscisic acid-controlled closure of guard cells. The addition of calcium to leaves excised from calcium-deficient plants rsstored their sensitivity to ethylene. Ethylene participates in the control of seedling growth, promoting the so-called "triple response" that results in distinct morphological development, such as hypocotyl hook formation. This effect, similar to the ethylene-promoted pathogenesis response, was found to be calcium dependent. The results indicate that calcium is required for a variety of ethylene-dependent processes.

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Ethylene Biosynthesis-Inducing Protein from Cellulysin Is an Endoxylanase

Cited by 97 publications

References 24 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

The Receptor for the Fungal Elicitor Ethylene-Inducing Xylanase Is a Member of a Resistance-Like Gene Family in Tomato

Calcium Requirement for Ethylene-Dependent Responses.

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