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The role of plant chitinases in protecting plants against a variety of fungal pathogens is well established. In the present study, a cDNA clone containing a class I chitinase (Chi-1) gene, designated as PgChi-1, has been isolated from the oriental medicinal plant Panax ginseng. PgChi-1 is predicted to encode a protein of 34.9 kDa consisting of 323 amino acid residues. PgChi-1 was found to be expressed constitutively in all of the studied organs of ginseng plant. Under various abiotic stress treatments including Cu, H2O2, mannitol, SA, JA, and NaCl, the expression of PgChi-1 in plantlets and hairy roots increased significantly compared to the control. When different parts of root were analyzed, maximum level was observed in taproot. In addition, levels of PgChi-1 expression were compared between healthy root and fungal, bacterial, and nematode infected root. Significant increase of PgChi-1 was noticed in pathogen infected roots than healthy roots. This study revealed that PgChi-1 may protect the P. ginseng under both biotic and abiotic stress conditions.
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http://dx.doi.org/10.1007/s11033-010-0082-6 | DOI Listing |
Mol Biol Rep
September 2025
Department of Agronomy, Faculty of Agriculture and Environment, The Islamia University of Bahawalpur, Bahawalpur, 63100, Pakistan.
Chitinases, enzymes responsible for hydrolyzing chitin, a significant component of fungal cell walls, play a crucial role in plant defense mechanisms, growth, symbiotic relationships, and stress resistance. In this study, we identified 27 chitinase genes in chickpeas (CaChi) and classified them into five classes based on phylogenetic analysis. Overall, chitinase genes are clustered on eight chromosomes.
View Article and Find Full Text PDFFEBS Open Bio
August 2025
Department of Biomedical Engineering, Faculty of Engineering, Osaka Institute of Technology, Japan.
A class I chitinase from the carnivorous sundew plant Drosera adelae was successfully expressed in the methylotrophic yeast Pichia pastoris and efficiently purified using a chitin affinity column. Enzymatic activity assays revealed that the enzyme showed a specific activity of 235.3 ± 10.
View Article and Find Full Text PDFPest Manag Sci
August 2025
Co-Innovation Centre for Sustainable Forestry in Southern China, Nanjing Forestry University, Nanjing, China.
Background: Pine wilt disease (PWD), caused by the pinewood nematode Bursaphelenchus xylophilus, poses a severe threat to coniferous forests, particularly impacting Pinus massoniana. Chitinases, essential defense-related enzymes, degrade chitin in pathogen cell walls to inhibit infection. However, their roles in conifer resistance against nematodes remain poorly understood.
View Article and Find Full Text PDFPlanta
July 2025
Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki, Sakyo-Ku, Kyoto, 606-8585, Japan.
The feeding assay revealed growth-retardation effects of class V chitinase of Ficus carica on Spodoptera litura larvae and these effects were retained in its chitinase-inactive mutants. This study investigated the anti-insect activity of the class V chitinase (FcChiC) from latex of the fig tree (Ficus carica, Moraceae). The feeding of radish cotyledons, transiently producing FcChiC, to larvae of Spodoptera litura (Lepidoptera), resulted in significant growth reduction.
View Article and Find Full Text PDFThe incredibly narrow protein fold bottleneck, which separates the billions of unique proteins on one side to deliver diverse biological functions on the other, arises from folds that tolerate mutations during evolution. One such fold, called the β-trefoil, is present in functionally diverse proteins including cytokines involved in the immune system such as interleukin-1. The unrecognizable sequence-level diversity, even among paralogs of interleukin-1 within the same chromosomal locus, suggests the resilience of this fold to mutational onslaught.
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