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Original Article

Isolation and Expression of a Barley β-1, 3-Glucanase Isoenzyme II Gene

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Pages 395-398 | Received 05 Mar 1999, Published online: 11 Jul 2009

References

  • Anuratha C. S., Zen K. C., Cole K. C., Mew T., Muthukrishnan S. Induction of chitinases and beta-1, 3-glucanases in Rhizoctonia solani-infected rice plants : Isolation of an infection-related chitinase cDNA clone. Physiol. Plant. 1996; 97: 39–46
  • Christensen A. H., Sharrock R. A., Quail P. H. Polyubiquitin genes: structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer to protoplasts by electroporation. Plant Mol. Biol. 1992; 18: 675–689
  • Boiler T. Hydrolytic enzymes in plant disease resistance. Plant-Microbe Interactions : Molecular and Genetic Perspectives Volume 2, T. Kosuge, E. W. Nester. Macmillan, New York 1987; 385–413
  • Burton R. A., Qi Z., Roulin S., Fincher G. B. Gene structure and a possible cytoplasmic location for (1–3)-β-glucanase isoenzyme GI from barley. (Hordeum vulgare). Plant Science 1998; 135: 39–47
  • Cordero M. J., Raventos D., Segundo B. S. Differential expression and induction of chitinases and β-1, 3-glucanases in response to fungal Infection during germination of maize seeds. Mol. Plant-Microbe Interact. 1994; 7: 23–31
  • Donath M, Mendel R., Cerff R., Martin W. Intron-dependent transient expression of the maize GapA1 gene. Plant Mol. Biol. 1995; 28: 667–676
  • Goodall G., Filipowicz W. The minimum functional length of pre-mRNA introns in monocots and dicots. Plant Mol. Biol. 1990; 14: 727–733
  • Goodall G., Filipowicz W. Different effects of intron nucleotide composition and secondary structure on pre mRNA splicing in monocot and dicot plants. EMBOJ 1991; 10: 2635–2644
  • Hoj P. B., Hartman D. J., Morrice N. A., Doan D. N.P., Fincher G. B. Purification of (l-3)-β-glucan endohydrolase isoenzyme II from germinated barley and determination of its primary structure from a cDNA clone. Plant Mol. Biol. 1989; 13: 31–42
  • Leah R., Tommerup H., Svendsen I., Mundy J. Biochemical and molecular characterization of three barley seed proteins with antifungal properties. J. Biol. Chem. 1991; 266: 1564–1573
  • Li C. D., Langridge P., Lance R. C.M., Xu P., Fincher G. B. Seven members of the (1–<3)-beta-glucanase gene family in barley (Hordeum vulgare) are clustered on the long arm of chromosome 3 (3HL). Theor. Appl. Genet. 1996; 92: 791–796
  • Linthorst H. J.M. Pathogenesis-reiated proteins of plants. Crit. Rev. Plant Sci. 1991; 10: 123–150
  • Luehrsen K. R., Walbot V. Intron enhancement of gene expression and the splicing efficiency of introns in maize cells. Mol. Gen. Genet. 1994; 225: 81–93
  • MacGregor A. W., Ballance G. M., Dushnicky L. Fluorescence microscopy studies on (1, 3)-β-D-glucan in barley endosperm. Food Microstructure 1989; 8: 235–244
  • Roulin S., Xu P., Brown A. H.D., Fincher G. B. Expression of specific (l-3)-beta-glucanase genes in leaves of near-isogenic resistant and susceptible barley lines infected with the leaf scald fungus. (Rhynchosporium secalis). Physiol. Molec. Plant Pathol. 1997; 50: 245–261
  • Saul M. W., Shillito R. D., Negrutiu I. Direct DNA transfer to protoplasts with and without electroporation. Plant Molecular Biology Manual, S. V. Gelvin, R. A. Schilperoort. Kluwer Academic Publishers, Dordrecht 1988; 1–16
  • Simpson C. G., Clark G., Davidson D., Smith P., Brown J. W.S. Mutation of putative branchpoint consensus sequences in plant introns reduces splicing efficiency. Plant J. 1996; 9: 369s–380
  • Wadsworth G. J., Redinbaugh M. G., Scandalios A. G. A procedure for the small-scale isolation of plant RNA suitable for RNA Blot analysis. Anal. Biochem. 1988; 172: 279–283
  • White O., Soderlund C, Shanmugan P., Fields C. Information contents and dinucleotide composition of plant intron sequences vary with evolutionary origin. Plant Mol. Biol. 1992; 19: 1057–1064
  • Wu S., Kriz A. L., Widholm J. M. Nucleotide sequence of a maize cDNA for a class II, acidic Beta-1, 3-glucanase. Plant Physiol. 1994; 106: 1709–1710

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