Abstract
Chitinase, which catalyzes the hydrolysis of the β-1, 4-acetyl-D-glucosamine linkages of the fungal cell wall polymer chitin, is involved in inducible plants defense system. By construction of cabbage (Brassica oleracea var. capitata) genomic library and screening the library with pRCH8, a probe of rice chitinase gene fragment, a chitinase genomic sequence was isolated. The complete nucleotide sequence of the putative cabbage chitinase gene (cabch29) was determined, with its longest open reading frame (ORF)encoding a polypeptide of 413 aa. This polypeptide consists of a 21 aa N-terminal signal peptide, two chitin-binding domains different from those of other classes of plant chitinases, and a catalytic domain. Homology analysis illustrated that this cabch29 gene has 58.8% identity at the nucleotide level with the pRCH8 ORF probe and has 50% identity at the amino acid level with the catalytic domains of chitinase from bean,maize and sugar beet. Meanwhile,several kinds of cis-elements, such as TATA box, CAAT box, GATA motif, ASF-1 binding site, wound-response elements and AATAAA, have also been discovered in the flanking region of cabch29 gene.
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References
Loon V . Stress proteins in infected plants. In Kosuge T, Nester EW, eds, Plant-Microbe Interactions. 1989; Vol. 3 McGraw-Hill, New York, pp.198–237.
Kombrink E, Schroder M, Hahlbrock K . Several “pathogenesis - related” proteins in potato are 1, 3-β-glucanases and chitinase. Proc Natl Acad Sci USA 1988; 85:782–6.
Mauch F, Hadwiger LE, Boller T . Ethylene: Symptom, not signal for the induction of chitinase and β-1, 3-glucanase in pea pods by pathogens and elicitors. Plant physiology 1984; 76:607–11.
Broekaert WF, Peumans WJ . Pectic polysaccharides elicit chitinase accumlation in tobacco. Physiol Plant 1988; 74:740–4.
Legrand M, Kauffmann S, Geoffroy P . Fritig B . Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinase. Proc Natl Acad Sci USA 1987; 88:6750–4.
Bartnicki-Garcia S . Cell wall chemistry, Morphogenesis and taxonomy of fungi. Annu Rev Microbiol 1968; 22:87–108.
Roberys WK, Selitrennikoff CP . Plant and bacterial chitinase differ in antifungal activity. J Gen Microbiol 1988; 134:169–76.
Mauch F, Mauch-Mani B, Boller T . Antifungal hydrolases in pea tissue II. Inhibition of fungal growth by combinations of chitinase and β-1, 3-glucanase. Plant Physiol 1988; 88:936–42.
Tuzun S, Nageswara R, Vgeli U, Schardl C, Kuc J . Induced systemic resistance to blue mold: Early induction and accumulation of β-1, 3-glucanase, chitinase and other pathogenesis-related proteins (b-proteins) in immunized tobacco. Phytopathology 1989; 79:979–83.
Sambrook J, Fritsch EF, Maniatis T . Molecular Cloning, a laboratory manual, second edition, 1989; Cold Spring Harbr Laboratroy Press.
Henikoffs . Unidirectional digestion with exonuclease III creates targeted break points for DNA sequencing. Gene 1984; 28:351–9.
Sanger F, Nicklen S, Coulson AR . DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 1977; 74:5463–8.
Lutcke HA, Chow KC, Mickel FS, Moss KA, Kern HF, Scheele GA . Selection of AUG initiation codons differs in plants and animals. EMBO J 1987; 6:43–8.
Breathnach R, Chambon P . Organization and expression of eukaryotic split genes coding for protein. Annu Rev Biochem 1986; 50:349–83.
Hart CM, Nagy F, Meins F Jr . A 61 bp enhancer element of tobacco β-1, 3-glucanase B gene intereacts with one or more regulated nuclear proteins. Plant Mol Biol 1993; 21:121–9.
Lois R, Dietrich A, Hahlbrock K, Schulz W . A phenylalamine ammonia-lyase gene from parsley: structure, regulation and indentification of elicitor and light response cis-acting elements. EMBO J 1984; 8:1641–8.
Holdsworth MJ, Laties GG . Site-specific binding of a nuclear factor to the carrot extensin gene is influenced by both ethylene and wounding. Planta 1989; 180:74–81
Lam E, Chua NH . ASF-2: A factor that binds to the cauliflower mosaic virus 35S promoter and conserved GATA motif in cab promoter. The Plant Cell 1989; 1:1147–56.
Datta N, Cashmore AR . Binding of a pea nuclear protein to promoters of certain photoregulated genes is modulated by phosphorylation. The Plant Cell 1989; 1:1069–77
Joshi CP . Putative polyadenylation signals in nuclear genes for higher plants: compilation and analysis. Nucl Acids Res 1987; 15:9627–40.
Von Heijne G . Patterns of amino acids near signal sequence cleavage sites. Eur J Biochem 1983; 133:17–21.
Broglie KE, Gaynor JJ, Broglie RM . Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris. Proc Natl Acad Sci USA 1986; 83:6820–4.
Gaynor JJ . Primary structure of an endochitinase mRNA from Solanum tuberosum. Nucl Acids Res 1988; 16:5210.
Samac DA, Hironaka CM, Yallay PE, Shah DM . Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thaliana. Plant physiol 1990; 93:907–14.
Shinshi H, Neuhaus JM, Ryals J, Meins F . Structure of a tobacco endochitinase gene: evidence that different chitinase genes can arise by transposition of sequences encoding cysteine-rich domain. Plant Mol Biol 1990; 14:357–68.
Huang JK, Wen L, Swegle M, Tran HC, Thin TH, Naylor HM, Muthukrishnan S, Reeck CR . Nucleotide sequence of a rice genomic clone that encodes a class I endochitinase. Plant Mol Biol 1991; 16:479–80.
Newhaus JM, Sticher L, Meins F, Boller T . A short terminal sequence is necessary and sufficient for the targeting of chitinase to the plant vacuole. Proc Natl Acad Sci USA 1992; 88:10362–6
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Tang, G., Bai, Y. & Loo, S. Molecular cloning and primary sequence analysis of a gene encoding a putative chitinase gene in Brassica oleracea vat. capitata. Cell Res 6, 65–73 (1996). https://doi.org/10.1038/cr.1996.8
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DOI: https://doi.org/10.1038/cr.1996.8


