Chitinases in root nodules

Santos, Procópio Miguel dos; Fortunato, Ana S.; Ribeiro, Ana Isabel; Pawlowski, Katharina

doi:10.5511/plantbiotechnology.25.299

Cited by 31 publications

(19 citation statements)

References 78 publications

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“…3) Some plant chitinases are involved in plant defense mechanisms against fungal and bacterial pathogens through lytic action against chitin and peptidoglycan (lysozymic action), respectively, 4,5) and show in vitro antifungal properties against several phytopathogenic fungi, inhibiting both spore germination and hyphal growth either alone or synergistically with other pathogenesis-related proteins; [6][7][8] while other chitinases and chitinase isoforms play important roles in the growth and development of plants, as in embryonic development, pollination, and sexual reproduction. [9][10][11] Some plant chitinases are reported to play roles in the protection of plants against environmental stress. 11) Chitinases have immense potential for biotechnological applications, as in preparing pharmaceutically important chitooligosaccharides and N-acetyl D-glucosamine, which are promising antibacterial agents, lysozyme-inducing elicitors, and immunoenhancers; the production of single-cell proteins; protoplast isolation from fungi and yeasts; the development of bio-control agents for pests and pathogens, and disease resistant transgenic plants; the control of mosquitoes to interfere with or block the transmission of diseases such as yellow fever, dengue, and malaria; and chitinous waste management.…”

mentioning

confidence: 99%

Characterization of a yam class IV chitinase produced by recombinant Pichia pastoris X-33

Akond

Matsuda

Ishimaru

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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A yam (Dioscorea opposita Thunb) class IV chitinase, whose genomic DNA was cloned by Mitsunaga et al. (2004), was produced by the recombinant Pichia pastoris X-33 in high yields such as 66 mg/L of culture medium. The chitinase was purified by column chromatography after Endoglycosidase H treatment and then characterized. It showed properties similar to the original chitinase E purified from the yam tuber reported by Arakane et al. (2000). This Pichia-produced chitinase also showed strong lytic activity against Fusarium oxysporum and Phytophthora nicotianae, wide pH and thermal stability, optimum activity at higher temperature such as 70 °C, and high substrate affinity, indicating that one can use this Pichia-produced yam chitinase as a bio-control agent.

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mentioning

confidence: 99%

Characterization of a yam class IV chitinase produced by recombinant Pichia pastoris X-33

Akond

Matsuda

Ishimaru

et al. 2014

Bioscience, Biotechnology, and Biochemistry

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“…Chitinases belong to the GH18 family including class III and V chitinases (Takenaka et al, 2009). The GH19 family is exclusively composed of the chitinases of class I, II, and IV members (Santos et al, 2008). Different structure and roles of plant chitinases had been found during plant evolution.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and expression of drought-induced protein 3 (DIP3) encoding a class III chitinase in upland rice

Guo

Bai²,

Su³

et al. 2013

Genet. Mol. Res.

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ABSTRACT.A drought-induced gene, DIP3, encoding a chitinase III protein was isolated from the roots of upland rice by reverse transcriptionpolymerase chain reaction (RT-PCR). Sequence analysis demonstrated that the cDNA and deduced protein showed high identity to Oryza sativa class III chitinase. The deduced protein contained a signal peptide sequence in the N-terminal region of 21aa and a conserved glycosyl hydrolase (GH) 18 domain. The secondary and 3D structures were analyzed and showed that it contained α-helix, β-sheets, extended strand and random coil structures and that it was approximately spheroidal. Real-time quantitative PCR analysis revealed that expression levels accumulated rapidly under different forms of abiotic stress (drought, salt and low temperature), peaked at different times and then decreased. These results implied that as a member of class III chitinases, DIP3 may function as a stress-induced protein involved in the regulation of plant stress response.

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“…The putative CgCHI1 protein consisted of 318 amino acids, presenting sequence characteristics of chitin hydrolases (Asensio et al 2000) and a C-terminal extension motif (GNGLVDTM) similar to that of a tobacco chitinase (Neuhaus et al 1991) and a class I chitinase from Elaeagnus umbellata root nodules (EuNOD-CHT2; Kim and An 2002), which is necessary and sufficient for vacuolar targeting (Neuhaus et al 1991). In fact, previous phylogenetic studies (Santos et al 2008) showed that CgCHI1 groups with actinorhizal chitinases, EuNOD-CHT1 and -CHT2 (Kim and An 2002). Although CgChi1 expression levels were not significantly affected by external stimuli in nodules and roots, transcript levels increased significantly in leaves after SA treatment (Fig.…”

Section: Cgchi1mentioning

confidence: 93%

“…These three sequences were also retrieved from NCBI. Sequence analyses were performed as described in Santos et al (2008) using ClustalX for multiple alignment neighbor-joining analysis.…”

Section: Sequence and Phylogenetic Analysesmentioning

confidence: 99%

Characterization of four defense-related genes up-regulated in root nodules of Casuarina glauca

et al. 2009

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Actinorhizal plants are capable of high rates of nitrogen fixation, due to their capacity to establish a rootnodule symbiosis with N 2 -fixing actinomycetes of the genus Frankia. Nodulation is an ontogenic process which requires a sequence of highly coordinated events. One of these mechanisms is the induction of defense-related events, whose precise role during nodulation is largely unknown. In order to contribute to the clarification of the involvement of defense-related genes during actinorhizal root-nodule symbiosis, we have analysed the differential expression of several genes with putative defense-related functions in Casuarina glauca nodules versus noninoculated roots. Four genes encoding a chitinase (CgChi1), a glutathione S-transferase (CgGst), a hairpin-inducible protein (CgHin1) and a peroxidase (CgPox4) were found to be up-regulated in mature nodules compared to roots. In order to find out to which extend were the encoded proteins involved in nodule protection, development or both, gene regulation studies in response to SA and wounding as well as phylogenetic analysis of the protein sequences were performed. These were further characterized through expression studies after SA-treatment and wounding, and by phylogenetic analysis. We suggest that CgChi1 and CgGst are involved in defense or microsymbiont control and CgPox4 is involved in nodule development. For CgHin1 the question "defense, development or both" remains open.

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Chitinases in root nodules

Cited by 31 publications

References 78 publications

Characterization of a yam class IV chitinase produced by recombinant Pichia pastoris X-33

Characterization of a yam class IV chitinase produced by recombinant Pichia pastoris X-33

Molecular cloning and expression of drought-induced protein 3 (DIP3) encoding a class III chitinase in upland rice

Characterization of four defense-related genes up-regulated in root nodules of Casuarina glauca

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