Abstract
We determined the primary structure of a tobacco β-1,3-glucanase gene. The β-1,3-glucanase gene has a single large intron, and the intron separates coding regions of the signal peptide and the mature enzyme. Analysis of the 5′-flanking region sequence revealed an 11 bp GC-rich element with perfect homology to the putative regulatory sequence of tobacco chitinase genes. RNA blot analysis showed that levels of mRNAs of β-1,3-glucanase and chitinase are coordinately increased in response to ethylene and salicylic acid. Accumulation of β-1,3-glucanase mRNA in suspension-cultured cells is rapidly induced at late logarithmic growth phase. Members of the tobacco β-1,3-glucanase gene families are classified into two subfamilies. One of the subfamilies appeared to be transcriptionally inactive.
References
Boller T: Hydrolytic enzymes in plant disease resistance. In: Kosuge T, Nester EW (eds) Molecular and Genetic Perspective, vol. 2, Plant-microbe interactions, pp. 395–414. Macmillan, New York (1987).
Broglelie KE, Biddle P, Gressman R, Broglie RM: Functional analysis of DNA sequence responsible for ethylene regulation of a bean chitinase gene in transgenic tobacco. Plant Cell 1: 599–607 (1989).
Brown JWS: A catalogue of splice junctions and putative branch point sequences from plant introns. Nucleic Acids Res 14: 9549–9559 (1986).
Cordes S, Deikman J, Margossian L, Fisher RL: Interaction of a developmentally regulated DNA-binding factor with sites flanking two different fruit-ripening genes from tomato. Plant Cell 1: 1025–1034 (1989).
Cornelissen BJC, Horowitz J, Van Kan JAL, Goldberg RB, Bol JF: Structure of tobacco genes encoding pathogenesis-related proteins from the PR-1 group. Nucleic Acids Res 15: 6797–6811 (1987).
Deikman J, Fisher RL: Interaction of DNA binding factor with the 5′-flanking region of an ethylene-responsive fruit ripening gene from tomato. EMBO J 7: 3316–3320 (1988).
De Loose M, Alliotte T, Gheysen G, Genetello C, Gielen J, Soetaert P, Van Montagu M, Inzé: Primary structure of a hormonally regulate β-1,3-glucanase of Nicotiana plumbaginifolia. Gene 70: 13–23 (1988).
Fukuda Y, Ohme M, Shinshi H: Gene structure and expression of a tobacco endochitinase gene in suspension cultured tobacco cells. Plant Mol Biol in press (1990).
Goodall GJ, Filipowicz W: The AU-rich sequence present in the introns of plant nuclear pre-mRNAs are required for splicing. Cell 58: 473–483 (1989).
Hooft van Huijsduijnen RAM, Van Loon LC, Bol JF: cDNA cloning of six mRNAs induced by TMV infection of tobacco and a characterization of their translation products. EMBO J 5: 2057–2061 (1986).
Logemann J, Shell J, Willmitzer L: Improved method for the isolation of RNA from plant tissues. Anal Biochem 173: 16–20 (1987).
Mauch F, Staehelin LA: Functional implications of the subcellular location of ethylene-induced chitinase and β-1,3-glucanase activity. Plant Cell 1: 447–457 (1989).
Memelink J, Linthorst HJM, Schilperoort RA, Hoge JHC: Tobacco genes encoding acidic and basic isoforms of pathogenesis-related proteins display different expression patterns. Plant Mol Biol 14: 119–126 (1990).
Mohnen D, Shinshi H, Felix G, Meins FJr: Hormonal regulation of β-1,3-glucanase messenger RNA levels in cultured tobacco tissues. EMBO J 4: 1631–1635 (1985).
Murashige T, Skoog F: A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol Plant 15: 473–497 (1962).
Payne G, Ahl P, Moyer M, Harper A, Beck J, Meins FJr, Ryals J: Isolation of complementary DNA clones encoding pathogenesis-related proteins P and Q, two acidic chitinase from tobacco. Proc Natl Acad Sci (USA) 87: 98–102 (1990).
Pelham H: Activation of heat-shock genes in eukaryotes. Trends Genet 1: 31–35 (1985).
Pfitzner UM, Pfitzner AJP, Goodman HM: DNA sequence analysis of a PR-1a gene from tobacco: Molecular relationship of heat shock and pathogen responses in plants. Mol Gen Genet 212: 290–295 (1988).
Shinshi H, Mohnen D, Meins FJr: Regulation of a plant pathogenesis-related enzyme: inhibition of chitinase and chitinase mRNA accumulation in cultured tobacco tissues by auxin and cytokinin. Proc Natl Acad Sci (USA) 84: 89–93 (1987).
Shinshi H, Neuhans J-M, Ryals J, Meins FJr: Structure of a tobacco endochitinase gene: Evidence that different chitinase genes can arise by transposition of sequence encoding cystein-rich domain. Plant Mol Biol 14: 357–368 (1990).
Shinshi H, Wenzler H, Neuhaus J-M, Felix G, Hofsteenge J, Meins FJr: Evidence for N- and C-terminal processing of a plant defenese-related enzyme: Primary structure of tobacco prepro-β-1,3-glucanase. Proc Natl Acad Sci (USA) 85: 5541–5545 (1988).
Somssich IE, Schmelzer E, Kawalleck P, Hahlbrock K: Gene structure and in situ transcript localization of pathogenesis-related protein in parsley. Mol Gen Genet 213: 93–98 (1988).
Stanford A, Bevan M, Northcote D: Differential expression within a family of novel wound-induced genes in potato. Mol Gen Genet 215: 200–208 (1989).
Taylor JL, Frintzemeier K-H, Häuser I, Kombrink E, Frauke R, Schröder M, Strittmatter G, Hahlbrock K: Structural analysis and activations by fungal infection of a gene encoding a pathogenesis-related protein in potato. Mol Plant-Microbe Interact 3: 72–77 (1990).
Watson MEE: Compilation of published signal sequences. Nucleic Acids Res 13: 5155–5164 (1984).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Ohme-Takagi, M., Shinshi, H. Structure and expression of a tobacco β-1,3-glucanase gene. Plant Mol Biol 15, 941–946 (1990). https://doi.org/10.1007/BF00039434
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00039434