Induction and characterization of chitinase isoforms in cucumber (Cucumis sativus L.): effect of elicitors, wounding and pathogen inoculation

Zhang, Yeyan; Punja, Zamir K.

doi:10.1016/0168-9452(94)90171-6

Cited by 19 publications

(12 citation statements)

References 24 publications

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“…In general, PR-like proteins were reported to be induced by several abiotic stresses, e.g. ozone (Schraudner et al, 1992;Yalpani et al, 1994), UV irradiation (Didierjean et al, 1996;Rakwal et al, 1999), heat stress (Margis-Pinheiro et al, 1994), wounding (Zhang and Punja, 1994;Ruperti et al, 2002), heavy metals (Edreva, 1990;Jacobsen et al, 1992;Rakwal et al, 1999), and during salt (Esaka et al, 1994) and cold adaptation (Antikainen et al, 1996;Hiilovaara-Teijo et al, 1999). Mn-induced expression of PR-like proteins was observed in tobacco (Edreva, 1990) and sunflower leaves (Jung et al, 1995), whereas several PR-proteins were also induced by a physiological, non-pathogenic disorder (Edreva, 1990), mercury, and UV light (Jung et al, 1995).…”

Section: Other Proteins In the Apoplast That Are Induced By Mn Stressmentioning

confidence: 99%

Effect of Manganese Toxicity on the Proteome of the Leaf Apoplast in Cowpea

et al. 2003

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Excess manganese (Mn) supply causes formation of visible brown depositions in the cell walls of leaves of cowpea (Vigna unguiculata), which consist of oxidized Mn and oxidized phenols. Because oxidation of Mn and phenolic compounds in the leaf apoplast was proposed to be catalyzed by apoplastic peroxidases (PODs), induction of these enzymes by Mn excess was investigated. POD activity increased upon prolonged Mn treatment in the leaf tissue. Simultaneously, a significant increase in the concentration of soluble apoplastic proteins in "apoplastic washing fluid" was observed. The identity of the released proteins was systematically characterized by analysis of the apoplast proteome using two-dimensional gel electrophoresis and liquid chromatography-tandem mass spectrometry. Some of the identified proteins exhibit sequence identity to acidic PODs from other plants. Several other proteins show homologies to pathogenesis-related proteins, e.g. glucanase, chitinase, and thaumatin-like proteins. Because pathogenesis-related-like proteins are known to be induced by various other abiotic and biotic stresses, a specific physiological role of these proteins in response to excess Mn supply remains to be established. The specific role of apoplastic PODs in the response of plants to Mn stress is discussed.For a wide range of plant species, formation of brown spots is part of a characteristic development of Mn toxicity symptoms in older leaves. The subsequent development of chlorosis and necrosis and finally leaf shedding occurs before a reduction in vegetative growth on the whole plant level (Horst, 1988; El-Jaoul and Cox, 1998). Analysis of the Mninduced formation of brown spots revealed the presence of oxidized Mn and oxidized phenols, especially in the cell wall of the epidermis layer (Horiguchi, 1987;Wissemeier and Horst, 1992). The formation of visible Mn toxicity symptoms is accompanied by the spatial formation of callose in the area of brown spots (Wissemeier and Horst, 1987). The physiological role of callose formation in response to toxic Mn levels in the tissue is unknown, but its detection serves as an additional sensitive parameter for Mn-induced injury of the leaf tissue. In cowpea (Vigna unguiculata), the leaf apoplast has been proposed to be the most important compartment for the defense of Mn stress (Horst et al., 1999 (Horst, 1988). This hypothesis is supported by a close relationship between the Mn-induced formation of brown spots, activation of constitutive apoplastic POD, and Mn-induced release of POD into the apoplast (Fecht-Christoffers et al., 2003). Among the existing information about the physiological functions of POD in plant tissue, its activation in response to a broad range of biotic and abiotic factors plays a particularly important role (Greppin et al., 1986;Obinger et al., 1996). POD activity is often used as a physiological marker for plant stress response as part of a complex cascade of reactions with an apparent lack of specificity. However, some specific relationships between horseradis...

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Section: Other Proteins In the Apoplast That Are Induced By Mn Stressmentioning

confidence: 99%

Effect of Manganese Toxicity on the Proteome of the Leaf Apoplast in Cowpea

et al. 2003

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“…Similar proteins, endo-P-1,3-glucanases, endochitinases, and TLPs, are known to be related to the mechanism for plant disease resistance (Carr and Klessig, 1989;Bol et al, 1990;Collinge et al, 1993;Stintzi et al, 1993) and are therefore classified as PR proteins. Proteins similar to PR proteins are also induced by other conditions unrelated to pathogen induction, such as ethylene (Boller et al, 1983), UV light (Yalpani et al, 1994), ozone (Ernst et al, 1992;Karenlampi et al, 1994;Yalpani et al, 1994), high salt (Esaka et al, 1994), heat (Margis-Pinheiro et al, 1994), phytotoxic metals (Jacobsen et al, 1992), and wounding (Zhang and Punja, 1994). Cold-induced accumulation of chitinase has been observed in barley (Tronsmo et al, 1993) and bermudagrass (Gatschet et al, 1996).…”

mentioning

confidence: 99%

Immunolocalization of Antifreeze Proteins in Winter Rye Leaves, Crowns, and Roots by Tissue Printing

et al. 1996

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During cold acclimation, antifreeze proteins (AFPs) that are similar to pathogenesis-related proteins accumulate in the apoplast of winter rye (Secale cereale L. cv Musketeer) leaves. AFPs have the ability to modify the growth of ice. To elucidate the role of AFPs in the freezing process, they were assayed and immunolocalized in winter rye leaves, crowns, and roots. Each of the total soluble protein extracts from cold-acclimated rye leaves, crowns, and roots exhibited antifreeze activity, whereas no antifreeze activity was observed in extracts from nonacclimated rye plants. Antibodies raised against three apoplastic rye AFPs, corresponding to a glucanase-like protein (CLP, 32 kD), a chitinase-like protein (CLP, 35 kD), and a thaumatin-like protein (TLP, 25 kD), were used in tissue printing to show that the AFPs are localized in the epidermis and in cells surrounding intercellular spaces in cold-acclimated plants. Although GLPs, CLPs, and TLPs were present in nonacclimated plants, they were found in different locations and did not exhibit antifreeze activity, which suggests that different isoforms of pathogenesis-related proteins are' produced at low temperature. The location of rye AFPs may prevent secondary nucleation of cells by epiphytic ice or by ice propagating through the xylem. l h e distributions of pathogenesis-induced and cold-accumulated CLPs, CLPs, and TLPs are similar and may reflect the common pathways by which both pathogens and ice enter and propagate through plant tissues.

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“…Previously, a chitinase (30.8 kDa) with antifungal activity has been isolated from mung bean (Phaseolus mungo) seeds (Wang et al, 2005), whereas two 28-kDa chitinases designated chitinase A and chitinase B also exhibiting antifungal activity were characterized in maize (Zea mays) seeds (Huynh et al, 1992). For comparison, 8 chitinase isoforms were identified in tobacco (Pan et al, 1992), 3 chitinase isoforms in cucumber (Zhang and Punja 1994). In celery, two chitinases were strongly induced by fungi (Krebs and Grumet 1991).…”

Section: Figurementioning

confidence: 99%

Wheat Pathogen Resistance and Chitinase Profile

Gregorová¹,

Socha²,

Maglovski³

et al. 2015

J microb biotech food sci

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The powdery mildew and leaf rust caused by Blumeria graminis and Puccinia recondita (respectively) are common diseases of wheat throughout the world. These fungal diseases greatly affect crop productivity. Incorporation of effective and durable disease resistance is an important breeding objective for wheat improvement. We have evaluated resistance of four bread wheat (Triticum aestivum) and four spelt wheat (Triticum spelta) cultivars. Chitinases occurrence as well as their activity was determined in leaf tissues. There was no correlation between resistance rating and activity of chitinase. The pattern of chitinases reveals four isoforms with different size in eight wheat cultivars. A detailed understanding of the molecular events that take place during a plant–pathogen interaction is an essential goal for disease control in the future.

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Induction and characterization of chitinase isoforms in cucumber (Cucumis sativus L.): effect of elicitors, wounding and pathogen inoculation

Cited by 19 publications

References 24 publications

Effect of Manganese Toxicity on the Proteome of the Leaf Apoplast in Cowpea

Effect of Manganese Toxicity on the Proteome of the Leaf Apoplast in Cowpea

Immunolocalization of Antifreeze Proteins in Winter Rye Leaves, Crowns, and Roots by Tissue Printing

Wheat Pathogen Resistance and Chitinase Profile

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