Characterization of NtChitIV, a class IV chitinase induced by β-1,3-, 1,6-glucan elicitor from Alternaria alternata 102: Antagonistic effect of salicylic acid and methyl jasmonate on the induction of NtChitIV

Shinya, Tomonori; Hanai, Kazunari; Gàlis, Ivan; Suzuki, Kaoru; Matsuoka, Ken; Matsuoka, Hiroaki; Saito, Mikako

doi:10.1016/j.bbrc.2006.12.009

Cited by 20 publications

(13 citation statements)

References 35 publications

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“…Accordingly to them, exogenously applied SA slightly but rapidly stimulated levels of chitinase homologous gene transcripts from Mikania micrantha infected by Cuscuta campestris. In contrast, application of SA has been reported to suppress expression of a tobacco chitinase gene induced in response to treatment with a glucan elicitor from Alternaria alternata (Shinya et al 2007). In cotton plants infected with F. oxysporum, PR-3 expression has been reported to being increased at the later stages of infection (Dowd et al 2004).…”

Section: Introductionmentioning

confidence: 91%

Expression Analysis of Defense-Related Genes in Cotton (Gossypium hirsutum) after Fusarium oxysporum f. sp. vasinfectum Infection and Following Chemical Elicitation using a Salicylic Acid Analog and Methyl Jasmonate

et al. 2011

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Cotton (Gossypium hirsutum) wilt caused by Fusarium oxysporum f. sp. vasinfectum (Fov) is considered as a major threat for commercial cotton production worldwide. Relative expression ratios of two key pathogenesis-related (PR) genes (PR-3 and PR-10) and a detoxification gene (GST18) were compared between a fully susceptible ("LACTA") and a partially field-resistant ("EMERALD") cultivar after challenging with an Australian Fov isolate, as well as after pre-treatments with chemical inducers of defense such as BION® (a chemical analog of salicylic acid) and methyl-jasmonate (MeJA) prior to Fov inoculation. It was demonstrated that in both hypocotyls and roots of "EMERALD", all PR genes were over-expressed after inoculation with Fov but not in the fully susceptible cultivar. Fov inoculation did not significantly affect GST18 expression in both cultivars. Exogenous application of each defense elicitor, prior to Fov inoculation, resulted in up-regulation of the three genes in root tissues of the fully susceptible cultivar. BION® application did not influence PR-3 expression in hypocotyls of both cultivars, whereas MeJA application resulted in induction of PR-3 in both cultivars. Furthermore, in hypocotyls of "LACTA", over-expression of PR-10 was recorded after treatment with each chemical inducer. This pathogen exhibited different ability in eliciting oxidative burst in roots of the two cotton cultivars used in our analysis.

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Section: Introductionmentioning

confidence: 91%

Expression Analysis of Defense-Related Genes in Cotton (Gossypium hirsutum) after Fusarium oxysporum f. sp. vasinfectum Infection and Following Chemical Elicitation using a Salicylic Acid Analog and Methyl Jasmonate

et al. 2011

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“…Previous studies reported that chitinase gene expression is modified by various treatments, such as wounding, application of plant hormones, hot water, and various stress-inducing chemicals (Bailey et al 2005;Keulen et al 2008;Porat et al 2001;Shinya et al 2007;Wu and Bradford 2003;Xiao et al 2007). In this study, levels of accumulated Mmchi1 transcripts were modulated by mechanical wounding, ZnSO 4 , abscisic acid, salicylic acid, and high salt stress (Fig.…”

Section: Discussionmentioning

confidence: 59%

“…7e). In contrast, application of salicylic acid has been reported to suppress expression of NtChitIV, a tobacco chitinase gene induced in response to treatment of plants with a glucan elicitor from Alternaria alternata (Shinya et al 2007).…”

Section: Discussionmentioning

confidence: 93%

“…It has been reported that chitinases inhibit growth of chitin-containing fungi, both in vitro (Schlumbaum et al 1986;Mauch et al 1988b) and in vivo (Broglie et al 1991;Maximova et al 2006;Robert et al 2002;Xiao et al 2007). Expression of plant chitinase genes is often up-regulated either upon pathogen attack or in response to a variety of abiotic stress factors (Bailey et al 2005;Hong and Hwang 2002;Keulen et al 2008;Khan and Shih 2004;Porat et al 2001;Shinya et al 2007;Wu and Bradford 2003). Furthermore, some chitinase genes may also possess developmental and physiological functions, including processes related to somatic embryogenesis in carrot, spruce, and Arabidopsis (de Jong et al 1992(de Jong et al , 1995Dong and Dunstan 1997;Passarinho et al 2001), maturation of pea pods (Mauch et al 1988a, b), senescence of rapeseed leaves (Hanfrey et al 1996), and ripening of grape berries (Robinson et al 1997).…”

Section: Introductionmentioning

confidence: 97%

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Molecular Cloning and Characterization of a Chitinase-Homologous Gene from Mikania micrantha Infected by Cuscuta campestris

Staehelin

Wang

et al. 2009

Plant Mol Biol Rep

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Mmchi1, a putative chitinase gene from Mikania micrantha infected by the parasitic plant Cuscuta campestris, was cloned and characterized. Mmchi1 is predicted to encode a 35.42-kDa polypeptide with a isoelectric point of 5.69. The corresponding genomic sequence contains two introns (1,171 and 621 bp). Phylogenetic analysis showed that the predicted Mmchi1 protein is related to class I and class II chitinases (glycoside hydrolase family 19). Mmchi1 is likely a class II chitinase, as the protein sequence lacks a cysteine-rich hevein domain at its N terminus. Southern blot analysis suggests that sequences related to Mmchi1 exist in the genome of M. micrantha. Expression of Mmchi1 in different tissues was analyzed by semiquantitative reverse transcriptase-polymerase chain reaction (RT-PCR). Mmchi1 was constitutively expressed in shoots, whereas only low transcript levels were detected in other tissues. Transcript levels of Mmchi1 in shoots of M. micrantha infected by C. campestris, as analyzed by RT-PCR and real-time PCR, significantly increased after 2 days post infection but markedly decreased during the following days. Transcript levels of Mmchi1 determined by semiquantitative RT-PCR varied in noninfected shoots exposed to various stress factors. Elevated levels of Mmchi1 transcripts were accumulated in response to mechanical wounding and application of abscisic acid, salicylic acid, or ZnSO 4 , respectively. Under salt stress conditions, Mmchi1 transcripts accumulated at significant lower levels, however. Taken together, these data suggest that Mmchi1 is a stress-related gene of M. micrantha, which is stimulated in response to C. campestris infection at early post-penetration stage but significantly suppressed during later infection stages.

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“…Chitinases are kinds of these induced proteins, and play significant roles in the interaction between plants and pathogenic fungi. [1][2][3][4][5][6][7] Chitinases (EC 3.2.1.14) could hydrolyze chitin, a linear homopolymer of β-1,4-linked N-acetylglucosamine (GlcNAc) residues, to protect the plants from pathogen attacks. 8,9 In contrast to the roles of chitinases in defense, much less attention was paid to their non-defensive functions.…”

mentioning

confidence: 99%

High-capacity calcium-binding chitinase III from pomegranate seeds (Punica granatumLinn.) is located in amyloplasts

Masuda

Yang

et al. 2011

Plant Signaling & Behavior

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Characterization of NtChitIV, a class IV chitinase induced by β-1,3-, 1,6-glucan elicitor from Alternaria alternata 102: Antagonistic effect of salicylic acid and methyl jasmonate on the induction of NtChitIV

Cited by 20 publications

References 35 publications

Expression Analysis of Defense-Related Genes in Cotton (Gossypium hirsutum) after Fusarium oxysporum f. sp. vasinfectum Infection and Following Chemical Elicitation using a Salicylic Acid Analog and Methyl Jasmonate

Expression Analysis of Defense-Related Genes in Cotton (Gossypium hirsutum) after Fusarium oxysporum f. sp. vasinfectum Infection and Following Chemical Elicitation using a Salicylic Acid Analog and Methyl Jasmonate

Molecular Cloning and Characterization of a Chitinase-Homologous Gene from Mikania micrantha Infected by Cuscuta campestris

High-capacity calcium-binding chitinase III from pomegranate seeds (Punica granatumLinn.) is located in amyloplasts

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