Purification and characterization of chitinase enzymes from healthy and Verticillium albo-atrum-infected tomato plants, and from V. albo-atrum

Pegg, G. F.; Young, David H.

doi:10.1016/0048-4059(82)90074-1

Cited by 86 publications

(45 citation statements)

References 22 publications

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“…For this reason, Abeles et al (1) proposed that chitinase functions as a defense against chitin-containing pathogens. This hypothesis is supported by studies which indicate that chitinase levels are increased in response to pathogen attack (19,20,24,25). In vitro studies have demonstrated further that plant chitinases are capable of hydrolyzing the cell walls ofplant pathogenic fungi (30) and releasing elicitors ofdefense reactions (14).…”

supporting

confidence: 61%

Regulation of a Chitinase Gene Promoter by Ethylene and Elicitors in Bean Protoplasts

Roby

Broglie²,

Gaynor³

et al. 1991

Plant Physiol.

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Chitinase gene expression has been shown to be transcriptionally regulated by a number of inducers, including ethylene, elicitors, and pathogen attack. To investigate the mechanism(s) responsible for induction of chitinase gene expression in response to various stimuli, we have developed a transient gene expression system in bean (Phaseolus vulgaris) protoplasts that is responsive to ethylene and elicitor treatment. This system was used to study the expression of a chimeric gene composed of the 5' flanking sequences of a bean endochitinase gene fused to the reporter gene ,-glucuronidase linked to a 3' fragment from nopaline synthase. Addition of 1-aminocyclopropane-1-carboxylic acid, the direct precursor of ethylene, or elicitors such as chitin oligosaccharides or cell wall fragments derived from Colletotrichum lagenarium, to transformed protoplasts resulted in a rapid and marked increase in the expression of the chimeric gene. The kinetics and dose response for these treatments were similar to those observed for the native gene in vivo. Analyses of 5' deletion mutants in the protoplast system indicated that DNA sequences located between -305 and -236 are important for both ethylene and elicitor induction of the reporter gene.Chitinase, a lytic enzyme found in most higher plants (1, 3), catalyzes the hydrolysis of chitin, a A-( 1,4)-linked polymer of 2-acetamido-2-deoxy-13-D-glucose. Although no endogenous substrate for this enzyme has been found in plants, chitin is a major component of the cell walls of many fungi (31). For this reason, Abeles et al. (1) proposed that chitinase functions as a defense against chitin-containing pathogens. This hypothesis is supported by studies which indicate that chitinase levels are increased in response to pathogen attack (19,20,24,25). In vitro studies have demonstrated further that plant chitinases are capable of hydrolyzing the cell walls ofplant pathogenic fungi (30) and releasing elicitors ofdefense reactions (14). In addition, plants treated with the phytohormone ethylene (1, 3) or elicitors such as isolated fungal cell walls (7,21,22), endogenous plant cell walls (21), or chitin oligosaccharides (14, 23), have also been shown to contain

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supporting

confidence: 61%

Regulation of a Chitinase Gene Promoter by Ethylene and Elicitors in Bean Protoplasts

Roby

Broglie²,

Gaynor³

et al. 1991

Plant Physiol.

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“…The induction and greater accumulation of PR-1 in 'GCTCV-218' after Foc infection could play a role in the successful containment of the pathogen. This is consistent with the study of Pegg and Young (1982), who reported that the release of β-1-3 glucanase and chitinase might serve to inhibit Foc in banana. PR-1 proteins are the only family members for which no biochemical function is known.…”

Section: Discussionsupporting

confidence: 82%

Genes Up-Regulated in Tolerant Cavendish Banana Roots in Response to Fusarium Oxysporum F. Sp. Cubense Infection

et al. 2009

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Fusarium wilt of banana, caused by Fusarium oxysporum f. sp. cubense (Foc), is regarded as one of the most devastating diseases. Cavendish cultivars (AAA genome) are highly susceptible to race 4 of the pathogen. The regulation of defencerelated genes in 'GCTCV-218', a Fusarium wilt-tolerant Cavendish selection, was studied. A cDNA library, enriched for genes up-regulated in 'GCTCV-218' after Foc infection when compared to susceptible Cavendish cultivar 'Williams', was previously constructed using suppression subtractive hybridisation (SSH) and screened using DNA micro-array technology. Potentially induced clones (334) were selected and sequenced. Four defence-associated genes (catalase 2, pectin acetyl esterase (PAE), PR-1 and PR-3) were selected for expression profile analysis using real-time reverse transcriptase PCR (RT-PCR). 'GCTCV-218' showed significantly lower disease severity and incidence than the susceptible 'Williams' in replicated greenhouse and field trials. Several defence-related transcripts were identified by BLASTX searches, including genes coding for PR-1, PAE, xylanase inhibitor, peroxidase, catalase 2, metallothionein, response regulator 6 and tripsin inhibitor. Inverse Northern dot blot data indicated that all of the above-mentioned transcripts were up-regulated in 'GCTCV-218' 6 hours post inoculation (hpi) compared to 'Williams'. Quantitative RT-PCR results confirmed that all four genes were differentially expressed in 'GCTCV-218' 3 and 6 hpi, confirming SSH results. PR-1 and PAE were induced very early (3 hpi) in 'GCTCV-218', while PR-3 and catalase 2 followed with a significant induction 6 hpi. This study concluded that 'GCTCV-218' is able to respond rapidly to Foc infection by activating both a biochemical and structural defence mechanism. The tolerance of 'GCTCV-218' was further linked to a significant increase in the induction cell wall-associated phenolic compounds.

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“…Among the proteins induced are chitinase and p-1,3-glucanase, lytic enzymes that catalyze the hydrolysis of the chitin and p-1,3-glucan components, respectively, of the fungal cell wall. Chitinases have been purified from a variety of sources, including a number of economically important crop plants (Molano et al, 1979;Pegg and Young, 1982;Bolleret al, 1983;Leah et al, 1987;Legrand et al, 1987;Shinshi et al, 1987;Fink et al, 1988;Nasser et al, 1988). In bean plants, the major chitinase activity is known to be associated with a basic, 30-kD protein that is localized in the vacuolar compartment (Boller et al, 1983;Boller and Vogeli, 1984).…”

Section: Introductionmentioning

confidence: 99%

Activation of a Bean Chitinase Promoter in Transgenic Tobacco Plants by Phytopathogenic Fungi

Roby¹,

Broglie²,

Cressman³

et al. 1990

The Plant Cell

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The temporal and spatial expression of a bean chitinase promoter has been investigated in response to fungal attack. Analysis of transgenic tobacco plants containing a chimeric gene composed of a 1.7-kilobase fragment carrying the chitinase 5B gene promoter fused to the coding region of the gus A gene indicated that the chitinase promoter is activated during attack by the fungal pathogens Botrytis cinerea, Rhizoctonia solani, and Sclerotium rolfsii. Although induction of 8-glucuronidase activity was observed in tissues that had not been exposed to these phytopathogens, the greatest induction occurred in and around the site of fungal infection. The increase in 8-glucuronidase activity closely paralleled the increase in endogenous tobacco chitinase activity produced in response to fungal infection. Thus, the chitinase 5B-gus A fusion gene may be used to analyze the cellular and molecular details of the activation of the host defense system during pathogen attack.

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Purification and characterization of chitinase enzymes from healthy and Verticillium albo-atrum-infected tomato plants, and from V. albo-atrum

Cited by 86 publications

References 22 publications

Regulation of a Chitinase Gene Promoter by Ethylene and Elicitors in Bean Protoplasts

Regulation of a Chitinase Gene Promoter by Ethylene and Elicitors in Bean Protoplasts

Genes Up-Regulated in Tolerant Cavendish Banana Roots in Response to Fusarium Oxysporum F. Sp. Cubense Infection

Activation of a Bean Chitinase Promoter in Transgenic Tobacco Plants by Phytopathogenic Fungi

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