Heavy-metal-responsive genes in maize: identification and comparison of their expression upon various forms of abiotic stress

Didierjean, Luc; Frendo, Pierre; Nasser, William; Génot, Geneviève; Marivet, Jocelyne; Burkard, G.

doi:10.1007/bf00196874

Cited by 65 publications

(34 citation statements)

References 27 publications

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“…The highest number of bands is 16 and 15 bands which were recorded in the 15 and 30 days old Pisum seedlings respectively irrigated with water collected from Mostourd station. It was known that plants respond to heavy metals stress by the synthesis of phytoclelatins, peptide and related proteins (Didierjean et al, 1996). These proteins might have helped for encountering the heavy metal inhibitory effects.…”

Section: Resultsmentioning

confidence: 99%

Effects of Industrial Effluents Polluting the Ismailia Water Canal on Growth and Metabolic Responses of Pisum sativum Seedlings

Ahmed

Hanafy

2017

Egypt. J. Bot.

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T HE AIM of this work was to evaluate the impact of sources of waste water pollution on Ismailia canal and irrigated plants. The industrial sources along Ismailia canal produce large wastes that disturb the environmental balance. This study was based on investigating the growth and biochemical characteristics of Pisum sativum seedlings irrigated with industrial waste water collected from three selected stations of Ismailia canal. Results revealed an enrichment of organic matter and heavy metals in polluted water. Irrigation of plants using waste water affected germination, physiological, biochemical and growth characteristics of Pisum sativum. Irrigation with polluted water reduced photosynthetic pigments, total nitrogen and proteins in plant. Uptake and translocation of heavy metals and metal ions were higher in the polluted Pisum sativum which produced more metabolites to combat metal toxicity. High activity of antioxidant enzymes (Catalase, peroxidase and polyphenol oxidase), the contents of soluble sugars, anthocyanine, proline and new protein bands were induced.

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Section: Resultsmentioning

confidence: 99%

Effects of Industrial Effluents Polluting the Ismailia Water Canal on Growth and Metabolic Responses of Pisum sativum Seedlings

Ahmed

Hanafy

2017

Egypt. J. Bot.

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“…A survey of Arabidopsis chitinases did not include the genes of PR4 endochitinases or the exo enzymes (Passarinho and de Vries 2002). Of the 27 maize endochitinases described here only seven were described earlier: ChiI93771 and ChiI201 (Wu et al 1994), ChiIVA and ChiIVB (Huynh et al 1992), ChiII-PR4 (Bravo et al 2003), ChiII-drp (Chevalier et al 1995), and ChiIII-PRm3 (Didierjean et al 1996). The sequences for the other genes were present in EST and genomic databases, but were heretofore not studied.…”

Section: Discussionmentioning

confidence: 96%

Genome-wide identification, expression and chromosomal location of the genes encoding chitinolytic enzymes in Zea mays

Shoresh

Harman

2008

Mol Genet Genomics

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Chitinolytic enzymes are important pathogenesis and stress related proteins. We identiWed 27 putative genes encoding endochitinases in the maize genome via in silico techniques and four exochitinases. Only seven of the endochitinases and segments of the exochitinases were heretofore known. The endochitinases included members of family 19 chitinases (classes I-IV of PR3, II of PR4) and members of family 18 chitinases (class III of PR8). Some similar enzymes were detected on adjacent regions of the same chromosome, and seem to result from duplication events. Most of the genes expressed were identiWed from EST libraries from plants exposed to biotic or abiotic stresses but also from libraries from tissues not exposed to stresses. We isolated proteins from seedlings of maize in the presence or absence of the symbiotic root colonizing fungus Trichoderma harzianum strain T22, and analyzed the activity of chitinolytic enzymes using an in-gel activity assay. The activity bands were identiWed by LC/MS/MS using the database from our in silico study. The identities of the enzymes changed depending on whether or not T22 was present. One activity band of about 95 kDa appeared to be a heterodimer between an exochitinase and any of several diVerent endochitinases. The identity of the endochitinase component appeared to be dependent upon treatment.

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“…Furthermore, the U. maydis-induced cell wall autofluorescence spread from the site of infection to the surrounding epidermal cells as well as to mesophyll cells below ( Figures 2C and 2D). In addition, transcriptional induction of the two SA-dependent genes pr1 and pr5 (van Loon et al, 2006) as well as the stress-induced marker prm6b (Nasser et al, 1990;Cordero et al, 1994;Didierjean et al, 1996) were monitored via qRT-PCR ( Figure 2E). In the cc9-silenced plants, expression of pr1, pr5, and prm6b was significantly induced in response to U. maydis infection when compared with BMV/YFPsi control plants ( Figure 2E).…”

Section: Identification Of Cystatin-9 As a Compatibility Factormentioning

confidence: 99%

A Maize Cystatin Suppresses Host Immunity by Inhibiting Apoplastic Cysteine Proteases

et al. 2012

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Ustilago maydis is a biotrophic pathogen causing maize (Zea mays) smut disease. Transcriptome profiling of infected maize plants indicated that a gene encoding a putative cystatin (CC9) is induced upon penetration by U. maydis wild type. By contrast, cc9 is not induced after infection with the U. maydis effector mutant Dpep1, which elicits massive plant defenses. Silencing of cc9 resulted in a strongly induced maize defense gene expression and a hypersensitive response to U. maydis wild-type infection. Consequently, fungal colonization was strongly reduced in cc9-silenced plants, while recombinant CC9 prevented salicylic acid (SA)-induced defenses. Protease activity profiling revealed a strong induction of maize Cys proteases in SA-treated leaves, which could be inhibited by addition of CC9. Transgenic maize plants overexpressing cc9-mCherry showed an apoplastic localization of CC9. The transgenic plants showed a block in Cys protease activity and SA-dependent gene expression. Moreover, activated apoplastic Cys proteases induced SA-associated defense gene expression in naïve plants, which could be suppressed by CC9. We show that apoplastic Cys proteases play a pivotal role in maize defense signaling. Moreover, we identified cystatin CC9 as a novel compatibility factor that suppresses Cys protease activity to allow biotrophic interaction of maize with the fungal pathogen U. maydis.

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Heavy-metal-responsive genes in maize: identification and comparison of their expression upon various forms of abiotic stress

Cited by 65 publications

References 27 publications

Effects of Industrial Effluents Polluting the Ismailia Water Canal on Growth and Metabolic Responses of Pisum sativum Seedlings

Effects of Industrial Effluents Polluting the Ismailia Water Canal on Growth and Metabolic Responses of Pisum sativum Seedlings

Genome-wide identification, expression and chromosomal location of the genes encoding chitinolytic enzymes in Zea mays

A Maize Cystatin Suppresses Host Immunity by Inhibiting Apoplastic Cysteine Proteases

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