chitinase/oryza sativa

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Distribution, structure, organ-specific expression, and phylogenic analysis of the pathogenesis-related protein-3 chitinase gene family in rice (Oryza sativa L.).

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Rice (Oryza sativa L.) pathogenesis-related (PR)-3 chitinases, like other PR proteins, are each coded by one of the genes of a multigene family in the plant genome. We assembled the database information about rice PR-3 chitinase sequences. A total of 12 PR-3 chitinase loci (Cht1 to Cht12) were found

Chitinases in Oryza sativa ssp. japonica and Arabidopsis thaliana.

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Chitinases (EC3.2.1.14), found in a wide range of organisms, catalyze the hydrolysis of chitin and play a major role in defense mechanisms against fungal pathogens. The alignment and typical domains were analyzed using basic local alignment search tool (BLAST) and simple modular architecture

[A study on introduction of chitinase gene and beta-1,3-glucanase gene into restorer line of dian-type hybrid rice (Oryza sativa L.) and enhanced resistance to blast (Magnaporthe grisea)].

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Plasmid pBLGC containing chitinase gene from Phaseolus limensis and beta-1,3-glucanase gene from Nicotiana tabacum was bombarded into the restorer line "Nan29" of Dian-type hybrid rice (Oryza sativa L. ssp. japonica) from Yunnan province of South-west China. 93 regenerants were obtained from the

Structure, heterologous expression, and properties of rice (Oryza sativa L.) family 19 chitinases.

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We identified four new family 19 chitinases in Oryza sativa L. cv. Nipponbare: one class I (OsChia1d), two class II (OsChia2a and OsChia2b), and one class IV (OsChia4a). OsChia2a resembled (about 60% identity) the catalytic domains of class I chitinases, but OsChia2b was almost identical (95%

Family 19 chitinase from rice (Oryza sativa L.): substrate-binding subsites demonstrated by kinetic and molecular modeling studies.

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A family 19 chitinase (OsChia1c, class I) from rice, Oryza sativa L., and its chitin-binding domain-truncated mutant (OsChia1c deltaCBD, class II) were produced by the Pichia expression system, and the hydrolytic mechanism toward N-acetylglucosamine hexasaccharide [(GlcNAc)6] was investigated by

Flower-predominant expression of a gene encoding a novel class I chitinase in rice (Oryza sativa L.).

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A flower-predominant cDNA for a gene, termed OsChia 1;175, was isolated from a cDNA library of rice pistils. Northern blot and RT-PCR analyses revealed that the OsChia 1;175 gene is highly expressed in floral organs (pistils, stamens and lodicules at the heading stage) but not or at an extremely low

Regulation, expression and function of a new basic chitinase gene in rice (Oryza sativa L.).

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A new basic chitinase gene, designated RC24, was isolated from a rice genomic library. The predicted RC24 protein contains 322 amino acid residues and exhibits 68% to 95% amino acid identity with known class I rice chitinases. RC24 protein expressed in Escherichia coli exhibited chitinase activity

A secreted chitinase-like protein (OsCLP) supports root growth through calcium signaling in Oryza sativa.

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Chitinases belong to a conserved protein family and play multiple roles in defense, development and growth regulation in plants. Here, we identified a secreted chitinase-like protein, OsCLP, which functions in rice growth. A T-DNA insertion mutant of OsCLP (osclp) showed significant retardation of

A novel class I Chitinase from Hippophae rhamnoides: Indications for participating in ICE-CBF cold stress signaling pathway.

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Plant chitinases are the members of PR (Pathogenesis related) proteins family and protect plants from biotic and abiotic stress. A novel chitinase HrCHI1 (Accession number JQ289153) of 954bp ORF encoding 317 amino acids protein was cloned, expressed and characterized from seabuckthorn, a cold/freeze

Rice chitinases: sugar recognition specificities of the individual subsites.

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Sugar recognition specificities of class III (OsChib1a) and class I (OsChia1cDeltaChBD) chitinases from rice, Oryza sativa L., were investigated by analyzing (1)H- and (13)C-nuclear magnetic resonance spectra of the enzymatic products from partially N-acetylated chitosans. The reducing end residue

Isolation and characterization of a rice gene encoding a basic chitinase.

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Chitinase, which catalyzes the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages of the fungal cell wall polymer chitin, is involved in inducible defenses of plants. A basic chitinase genomic sequence was isolated from a rice (Oryza sativa L.) genomic library using a bean chitinase gene

Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes.

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Hydrolytic mechanisms of family 18 chitinases from rice (Oryza sativa L.) and Bacillus circulans WL-12 were comparatively studied by a combination of HPLC analysis of the reaction products and theoretical calculation of reaction time-courses. All of the enzymes tested produced beta-anomers from

Molecular cloning of Indian jujube (Zizyphus mauritiana) allergen Ziz m 1 with sequence similarity to plant class III chitinases.

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Indian jujube (Zizyphus mauritiana) is a sweet fruit that is abundantly cultivated in Taiwan. We have previously identified 42 and 30 kDa allergens that are cross-reactive with latex allergen from crude Indian jujube extract. This study aimed to clone the 30 kDa Ziz m 1 Z. mauritiana allergen. The

Elicitation of Diterpene Biosynthesis in Rice (Oryza sativa L.) by Chitin.

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Cell-free extracts of UV-irradiated rice (Oryza sativa L.) leaves have a much greater capacity for the synthesis from geranylgeranyl pyrophosphate of diterpene hydrocarbons, including the putative precursors of rice phytoalexins, than extracts of unstressed leaves (KA Wickham, CA West [1992] Arch

Co-transformation of canola by chimeric chitinase and tlp genes towards improving resistance to Sclerotinia sclerotiorum.

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Canola (Brassica napus) plants were co-transformed with two pathogenesis-related protein genes expressing a Trichoderma atroviride chitinase with a chitin-binding domain (chimeric chitinase) and a thaumatin-like protein (tlp) from Oryza sativa conferring resistance to phytopatogenic fungi by

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