cDNA cloning and characterization of a putative 1,3-?-D-glucanase transcript induced by fungal elicitor in bean cell suspension cultures

Edington, Brent V.; Lamb, Christopher J.; Dixon, Richard A.

doi:10.1007/bf00017919

Cited by 52 publications

(28 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[29,301, Glycine max [34], Phuseolus vulgaris [35], Lycopevsicon esculentum (unpublished) and Arabidopsis thaliana [36]. Positional identity values within the range of 44.7-49.5% are observed between the barley enzyme and the (1 +3)-fbglucanases from dicotyledonous plants, with a standard deviation of 1.34% about a mean of 46.5%.…”

Section: Dlscussionmentioning

confidence: 91%

Purification, characterization and gene structure of (1→3)‐β‐glucanase isoenzyme GIII from barley (Hordeum vulgare)

Wang¹,

Xu²

1992

European Journal of Biochemistry

View full text Add to dashboard Cite

A new member of the barley (1 +3)-P-glucan glucanohydrolase family of enzymes has been purified from extracts of germinated grain and young seedlings by fractional precipitation with ammonium sulphate, ion-exchange chromatography, chromatofocussing and gel-filtration chromatography. The enzyme, which has been designated (1 +3)-P-glucanase isoenzyme GIII, is a basic protein with an apparent molecular mass of 32 000 Da. Oligosaccharide products released by the enzyme during hydrolysis of the (1+3)-P-glucan, laminarin, indicate that the enzyme is an endohydrolase. A 2349-bp fragment of barley genomic DNA has been isolated and identified as the gene encoding the (1 +3)-P-glucanase isoenzyme GIII. The open reading frame encoding the isoenzyme is interrupted by a single intron of 180 bp that splits a codon in the putative signalpeptide region. Northern-blot analyses with gene-specific probes indicate that the (1 +3)-P-glucanase isoenzyme GI11 mRNA accumulates in developing leaves; no mRNA transcripts were detected in the aleurone or scutellum of germinated grain, or in mature vegetative tissues. Although plant (1 +3)-Pglucanases are generally classified as 'pathogenesis-related' proteins, the physiological function of the barley (1 +3)-P-glucanase isoenzyme GI11 is unclear.During the germination of barley, hydrolytic enzymes depolymerize the starch and storage-protein reserves of the starchy endosperm into low-molecular-mass products that are translocated to the embryo where they support seedling growth. The hydrolases originate principally in the alcurone and scutellum, although some pre-exist in the starchy endosperm of ungerminated grain [I]. The most abundant enzymes in germinated barley include a-amylases, P-amylases, (1 + 3,l -.4)-p-glucanases, xylanases, carboxypeptidases and endopeptidases [2 -81. These enzymes participate in the degradation of storage polymers or in the removal of cell walls that separate the secreted hydrolases from their substrates within the cells of the starchy endosperm.High levels of (1 +3)-P-glucan endohydrolase activity are also found in the endosperm of germinated barley [9, lo], but the function of these enzymes is not so obvious. It has been suggested that they may participate in cell-wall degradation through an ability to hydrolyse regions of contiguous (1 +3)-fi-linked glucosyl residues in wall (1 +3,1-+4)-P-glucan [ll], but no regions of adjacent (1 +3)-P linkages have been conclusively demonstrated in this polysaccharide [I] and purified (1 + 3)-P-glucanases are unable to hydrolyse 40 "C water-soluble barley (1 +3,1+4)-B-glucans [12]. Another potential function of the (1 -+3)-~-glucanases in the germinating grain relates to the small deposits of (1 +3)-@-glucan that are scattered through the starchy endosperm 113 -151. The (1 +3)-Pglucanases might play a role in the recovery of glucose from these polysaccharides as an energy source for the young seedling. However, (1 +3)-b-glucanase levels are higher than those required to depolymerize these (1 +3)-P-glucan deposits. A possibl...

show abstract

Section: Dlscussionmentioning

confidence: 91%

Purification, characterization and gene structure of (1→3)‐β‐glucanase isoenzyme GIII from barley (Hordeum vulgare)

Wang¹,

Xu²

1992

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…RT-PCR and qRT-PCR were conducted as described previously (Ryu et al, 2004a). To detect expression levels of PR-2, LOX, and Actin genes, adequate primers were obtained from Edington et al (1991;PR-2), Meier et al (1993;LOX), and Maffei et al (2006;Actin) and were as follows: PvPR-2 (forward, 5#-GCCACAAATGCCGACACTGC-3#; reverse, 5#-GGACT-CACTTCATTGCCAACTGC-3#), PvLOX (forward, 5#-GTGAGAGGCGATG-GAAGTGGAG-3#; reverse, 5#-TGCGAGGGTAAGGTAAGGTAGAAC-3#), and PlActin (forward, 5#-AGGCTCCTCTTAACCCCAAG-3#; reverse, 5#-GTGGGAGAGCATAACCCTCA-3#).…”

Section: Rt-pcr and Qrt-pcrmentioning

confidence: 99%

Airborne Induction and Priming of Plant Defenses against a Bacterial Pathogen

Heil²,

et al. 2009

View full text Add to dashboard Cite

Herbivore-induced plant volatiles affect the systemic response of plants to local damage and hence represent potential plant hormones. These signals can also lead to "plant-plant communication," a defense induction in yet undamaged plants growing close to damaged neighbors. We observed this phenomenon in the context of disease resistance. Lima bean (Phaseolus lunatus) plants in a natural population became more resistant against a bacterial pathogen, Pseudomonas syringae pv syringae, when located close to conspecific neighbors in which systemic acquired resistance to pathogens had been chemically induced with benzothiadiazole (BTH). Airborne disease resistance induction could also be triggered biologically by infection with avirulent P. syringae. Challenge inoculation after exposure to induced and noninduced plants revealed that the air coming from induced plants mainly primed resistance, since expression of PATHOGENESIS-RELATED PROTEIN2 (PR-2) was significantly stronger in exposed than in nonexposed individuals when the plants were subsequently challenged by P. syringae. Among others, the plant-derived volatile nonanal was present in the headspace of BTH-treated plants and significantly enhanced PR-2 expression in the exposed plants, resulting in reduced symptom appearance. Negative effects on growth of BTH-treated plants, which usually occur as a consequence of the high costs of direct resistance induction, were not observed in volatile organic compound-exposed plants. Volatile-mediated priming appears to be a highly attractive means for the tailoring of systemic acquired resistance against plant pathogens.

show abstract

“…culaire des Plantes du CNRS, Strasbourg, France). The pG101 class I β-1,3-glucanase (Edington, Lamb & Dixon, 1991) was from Dr R. A. Dixon (The Samuel Roberts Noble Foundation, Ardmore, OK, USA), and pCHS1, encoding chalcone synthase, (Ryder et al, 1984) pPAL5, coding for phenylalanine ammonia-lyase (Edwards et al, 1985) and pH1, a cDNA clone encoding a constitutively expressed gene of unknown function (Lawton & Lamb, 1987), were from Dr C. J. Lamb (The Salk Institute for Biological Studies, La Jolla, CA, USA).…”

Section: Source Of Cdna Probesmentioning

confidence: 99%

Plant defence genes are induced in the pathogenic interaction between bean roots and Fusarium solani, but not in the symbiotic interaction with the arbuscular mycorrhizal fungus Glomus mosseae

et al. 1998

View full text Add to dashboard Cite

Plant roots enter symbiotic as well as pathogenic interactions with fungi in the rhizosphere. We studied the response of bean (Phaseolus vulgaris L. cv. Saxa) roots to infection by the arbuscular mycorrhizal fungus Glomus mosseae (Nicol. & Gerd.) Gerdemann & Trappe and the pathogen Fusarium solani (Mart.) Sacc. f. sp. phaseoli (Burkholder) Snyder & Hansen. In a time‐course study of the symbiotic interaction between bean roots and G. mosseae, covering all stages of mycorrhiza development, we detected little change in the expression of the defence‐related genes chitinase, β‐1,3‐glucanase and phenylalanine ammonia‐lyase compared with non‐mycorrhizal control roots. The only difference observed was a transient increase in chalcone synthase transcripts at later stages of mycorrhizal root colonization. In interactions with the pathogen, a marked induction of chitinase and phenylalanine ammonia‐lyase expression was observed at the level of both the transcripts and enzyme activities. Class I β‐1,3‐glucanase levels strongly increased at the transcript level, but there was little change in the overall β‐1,3‐glucanase enzyme activity. In the non‐host interaction between common bean and Fusarium solani (Mart.) Sacc. f. sp. pisi (Linford) Snyder & Hansen defence responses increased only slightly and transiently, if at all.

show abstract

cDNA cloning and characterization of a putative 1,3-?-D-glucanase transcript induced by fungal elicitor in bean cell suspension cultures

Cited by 52 publications

References 33 publications

Purification, characterization and gene structure of (1→3)‐β‐glucanase isoenzyme GIII from barley (Hordeum vulgare)

Purification, characterization and gene structure of (1→3)‐β‐glucanase isoenzyme GIII from barley (Hordeum vulgare)

Airborne Induction and Priming of Plant Defenses against a Bacterial Pathogen

Plant defence genes are induced in the pathogenic interaction between bean roots and Fusarium solani, but not in the symbiotic interaction with the arbuscular mycorrhizal fungus Glomus mosseae

Contact Info

Product

Resources

About