Molecular cloning and primary sequence analysis of a gene encoding a putative chitinase gene in Brassica oleracea var. capitata

Cell Research

Volumn 6, Issue 1, 1996, Pages 65-73

  Tang, Guo Qing ^a   Bai, Yong Yan ^a   Loo, Shi Wei ^a  

^a INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Cabbage; Chitinase gene; Cloning; Sequence

Indexed keywords

BETA VULGARIS SUBSP. VULGARIS; BRASSICA; BRASSICA OLERACEA VAR. CAPITATA; CAPITATA; PHASEOLUS (ANGIOSPERM); ZEA MAYS;

EID: 3142592659     PISSN: 10010602     EISSN: None     Source Type: Journal    
DOI: 10.1038/cr.1996.8     Document Type: Article

References (27)

1. 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.
2. 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.
3. 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.
4. Broekaert WF, Peumans WJ. Pectic polysaccharides elicit chitinase accumlation in tobacco. Physiol Plant 1988; 74:740-4.
5. 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.
6. Bartnicki-Garcia S. Cell wall chemistry, Morphogenesis and taxonomy of fungi. Annu Rev Microbiol 1968; 22:87-108.
7. Roberys WK, Selitrennikoff CP. Plant and bacterial chitinase differ in antifungal activity. J Gen Microbiol 1988; 134:169-76.
8. 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.
9. 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.
10. Sambrook J, Fritsch EF, Maniatis T. Molecular Cloning, a laboratory manual, second edition, 1989; Cold Spring Harbr Laboratroy Press.
11. Henikoffs. Unidirectional digestion with exonuclease III creates targeted break points for DNA sequencing. Gene 1984; 28:351-9.
12. Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 1977; 74:5463-8.
13. Lutcke HA, Chow KG, Mickel FS, Moss KA, Kern HF, Scheele G A. Selection of AUG initiation codons differs in plants and animals. EMBO J 1987; 6:43-8.
14. Breathnach R, Chambon P. Organization and expression of eukaryotic split genes coding for protein. Annu Rev Biochem 1986; 50:349-83.
15. Hart G M, 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.
16. Lois R, Dietrich A, Hahlbrock K, Schulz W. A phenylalamine ammonia-lyase gene from parsley: structure, regulation and indentification of elicitor and light response cisacting elements. EMBO J 1984; 8:1641-8.
17. 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
18. 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.
19. 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
20. Joshi CP. Putative polyadenylation signals in nuclear genes for higher plants: compilation and analysis. Nucl Acids Res 1987; 15:9627-40.
21. Von Heijne G. Patterns of amino acids near signal sequence cleavage sites. Eur J Biochem 1983; 133:17-21.
22. Broglie KE, Gaynor JJ, Broglie RM. Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phascolus vulgaris. Proc Natl Acad Sci USA 1986; 83:6820-4.
23. Gaynor JJ. Primary structure of an endochitinase mRNA from Solarium tuberosum. Nucl Acids Res 1988; 16:5210.
24. Samac DA, Hironaka CM, Yallay PE, Shah DM. Isolation and characterization of the genes encoding basic and acidic chitinase in Arabidopsis thailana. Plant physiol 1990; 93:907-14.
25. 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.
26. 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.
27. 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