Cloning of two genes from Bacillus circulans WL-12 which encode 1,3-β-glucanase activity

References

1. Abel P. P., Nelson R. S., Hoffman B. DE N., Rogers S. G., Fraley R. T., Beachy R. N. 1986; Delay of disease development in transgenic plants that express the tobacco mosaic virus coat protein gene. Science 232:738–743
   [Google Scholar]
2. Barry G. F. 1986; Permanent insertion of foreign genes into the chromosomes of soil bacteria. Bio/Technology 4:446–449
   [Google Scholar]
3. Barton K. A., Whiteley H. R., Young N. S. 1987; Bacillus thiringiensis δ-endotoxin expressed in transgenic Nicotiana tabacum provides resistance to lepidopteran insects. Plant Physiology 85:1103–1109
   [Google Scholar]
4. Bell A. A. 1981; Biochemical mechanisms of disease resistance. Annual Review of Plant Physiology 321:21–81
   [Google Scholar]
5. Birnboim H. C., Doly J. 1979; A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Research 1:1513–1524
   [Google Scholar]
6. Bradford M. M. 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Biochemistry 12:248–254
   [Google Scholar]
7. Borris R., Baumlein H., Hofemeister J. 1985; Expression in Escherichia coli of a cloned β-glucanase gene from Bacillus amyloliquefaciens . Applied Microbiology and Biotechnology 22:63–71
   [Google Scholar]
8. Cantwell B., Mcconnell D. J. 1983; Molecular cloning and expression of a Bacillus subtilis β-glucanase gene in Escherichia coli. Gene 23:211–219
   [Google Scholar]
9. Chesters C. G. C., Bull A. T. 1963; The enzymatic degradation of laminarin. 1. The distribution of laminarinase among microorganisms. Biochemical Journal 86:28–31
   [Google Scholar]
10. Deblock M., Botterman J., Vandewiele M., Dockx J., Thoen C., Gossele V., Movva N. R., Thompson C., Van Montagu M., Leemans J. 1987; Engineering herbicide resistance in plants by expression of a detoxifying enzyme. EMBO Journal 6:2513–2518
    [Google Scholar]
11. Doi K., Doi A., Fukui T. 1973; Purification and properties of lytic β-glucanase from an Arthrobacter bacterium. Agricultural and Biological Chemistry 37:1619–1627
    [Google Scholar]
12. Esteban R., Nebrada A. R., Villa T. G. 1984; Synthesis and regulation of Bacillus circulans WL-12 1,3-/β-d-glucanases. Journal of General Microbiology 130:2483–2487
    [Google Scholar]
13. Fischhoff D. A., Bowdish K. S., Perlak F. J., Marrone P. G., Mccormick S. M., Niedermeyer J. G., Dean D. A., Kusano-Kretzmer K., Mayer E. J., Rochester D. E., Rogers S. G., Fraley R. T. 1988; Insect tolerant transgenic tomato plants. Bio/Technology 5:807–813
    [Google Scholar]
14. Fuchs R. L., Mcpherson S. A., Drahos D. J. 1986; Cloning of a Serratia marcescens gene encoding chitinase. Applied and Environmental Microbiology 51:504–509
    [Google Scholar]
15. Hewick R. M., Hunkapiller M. W., Hood L. E., Dreyer W. J. 1981; A gas-liquid solid phase peptide and protein sequenator. Journal of Biological Chemistry 256:7990–7997
    [Google Scholar]
16. Horikoshi K., Atsukawa Y. 1973; β1,3-Glucanase produced by alkalophilic bacteria Bacillus no. K-12-5. Agricultural and Biological Chemistry 37:1449–1456
    [Google Scholar]
17. Kobayashi T., Tanaka H., Ogasawara N. 1974a; Concerted inductions of multiple (β-1,3 glucanases in Bacillus circulans WL-12 in response to three different substrates. Agricultural and Biological Chemistry 38:967–972
    [Google Scholar]
18. Kobayashi Y., Tanaka H., Ogasawara N. 1974b; Multiple β-1,3 glucanases in the lytic enzyme complex of Bacillus circulans WL-12. Agricultural and Biological Chemistry 38:959–965
    [Google Scholar]
19. Kobayashi Y., Tanaka H., Ogasawara N. 1974c; Purification and properties of F-1 a, a β-1,3 glucanase which is highly lytic toward cell walls of Piricularia oryzae P2. Agricultural and Biological Chemistry 38:973–978
    [Google Scholar]
20. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature; London: 227680–685
    [Google Scholar]
21. Mahasneh A. M., Stewart D. J. 1980; A medium for detecting β-1, 3 glucanase activity in bacteria. Journal of Applied Bacteriology 48:457–458
    [Google Scholar]
22. Maniatis T., Fritsch E. F., Sambrook J. 1982 Molecular Cloning, a Laboratory Manual Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
23. Manners D. J., Wilson G. 1973; Studies on β-glucanases: some properties of a bacterial endo-β(1→3)-glucanase system. Biochemical Journal 135:11–18
    [Google Scholar]
24. Martin D. F., Priest F. G., Todd C., Goodfellow M. 1980; Distribution of β-glucanases within the genus Bacillus . Applied and Environmental Microbiology 40:1136–1138
    [Google Scholar]
25. Miller J. H. 1972 Experiments in Molecular Genetics Cold Spring Harbor, NY: Cold Spring Harbor Laboratory;
    [Google Scholar]
26. Nichols E. J., Beckman J. M., Hadwiger L. A. 1980; Glycosidic enzyme activity in pea tissue and pea-Fusarium solani interactions. Plant Physiology 66:199–204
    [Google Scholar]
27. Nitzsche W. 1983; Chitinase as a possible resistance factor for higher plants. Theoretical and Applied Genetics 65:171–172
    [Google Scholar]
28. Okagbue R. N., Lewis M. J. 1985; Influence of mixed culture conditions on yeast-wall hydrolytic activity of Bacillus circulans WL- 12 and on extractability of astaxanthin from the yeast Phaffia rhodozyma . Journal of Applied Bacteriology 59:243–255
    [Google Scholar]
29. Robson L. M., Chambliss G. H. 1986; Cloning of the Bacillus subtilis DLG β-1,4-glucanase gene and its expression in E. coli and B. subtilis . Journal of Bacteriology 165:612–619
    [Google Scholar]
30. Rombouts F. M., Phaff H. J. 1976; Lysis of yeast cell walls: lytic β-(1,3)-glucanases from Bacillus circulans WL-12. European Journal of Biochemistry 63:121–130
    [Google Scholar]
31. Shah D. M., Horsch R. B., Klee H. J., Kishore G. M., Winter J. A., Tumer N. E., Hironaka C. M., Sanders P. R., Gasser C. S., Aykent S., Siegel N. R., Rogers S. G., Fraley R. T. 1986; Herbicide tolerance in transgenic plants. Science 233:478–481
    [Google Scholar]
32. Sietsma J. A., Wessels J. G. H. 1979; Evidence for covalent linkages between chitin and β-glucan in a fungal wall. Journal of General Microbiology 114:99–108
    [Google Scholar]
33. Skujins J. J., Potgieter H. J., Alexander M. 1965; Dissolution of fungal cells by a streptomycete chitinase and β-(1→)-glucanase. Archives of Biochemistry and Biophysics 111:358–364
    [Google Scholar]
34. Somogyi M. 1952; Notes on sugar determination. Journal of Biological Chemistry 195:19–23
    [Google Scholar]
35. Tanaka H., Phaff J. H. 1965; Enzymatic hydrolysis of yeast cell walls. I. Isolation of wall-decomposing organisms and separation and purification of lytic enzymes. Journal of Bacteriology 89:1570–1580
    [Google Scholar]
36. Tanaka H., Itakura K., Toda K. 1978; Concerted induction of β-glucanases of Bacillus circulans WL-12 in response to various yeast glucans. Agricultural and Biological Chemistry 42:1631–1636
    [Google Scholar]
37. Tanaka H., Kobayashi Y., Itakura K., Kamimiya S. 1981; Concerted induction of cell wall lytic enzymes in Bacillus circulans WL-12. Advances in Biotechnology 4:593–598
    [Google Scholar]
38. Tumer N. E., O’Connell K. M., Nelson R. S., Sanders P. R., Beachy R. N., Fraley R. T., Shah D. M. 1987; Expression of alfalfa mosaic virus coat protein confers cross-protection in transgenic tobacco and tomato plants. EMBO Journal 6:1181–1188
    [Google Scholar]
39. Usui T., Totani K., Totsuka A., Oguchi M. 1985; Purification of endo-(1→3)-β-d-glucanases lysing yeast cell walls from Rhizoctonia solani . Biochimica et Biophysica Acta 840:255–263
    [Google Scholar]
40. Vaeck M., Reynaerts A., Hofte H., Kansens S., De Beuckeleer M., Dean C., Zabeau M., Van Montagu J. 1987; Transgenic plants protected from insect attack. Nature; London: 32833–37
    [Google Scholar]
41. Wray W., Boulikas T., Wray V. P., Hancock R. 1981; Silver staining proteins in polyacrylamide gels. Analytical Biochemistry 118:197–203
    [Google Scholar]
42. Yamamoto S., Miyagi M., Nagasaki R. 1983; Amino acid residues involved in the action of endo-(1→3)-β-d-glucanase II from Flavobacterium dormitator var. glucanolyticae FA-5. Carbohydrate Research 114:137–145
    [Google Scholar]