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Plant growth and development influenced by transgenic insertion of bacterial chitinolytic enzymes

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Abstract

The role of the chitinolytic enzymes in plants is not necessarilyrestricted to plant defense. Tomato plants transformed with an endochitinaseand a chitobiosidase gene from Streptomyces albidoflavus andgrowth under greenhouse conditions showed a significant reduction in plantheight, and reduced time to flowering compared with the control(non-transformed) plants. The levels of chitobiosidase and endochitinaseactivity in the transgenic tomato plants were positively correlated with earlyflowering, and negatively correlated with plant height. We have not determinedwhether these effects are exclusively due to the expression of the transgenesof endochitinase and chitobiosidase from S. albidoflavus orthe additive effect of these 2 enzymes combined with the endogenouschitinolytic enzymes produced by the plants. However, when control plants were trimmed,early flowering was observed compared with the controls that were not trimmed, whichindicates that wound induced proteins such as chitinolytic enzymes affect thetime of flowering. In addition, the expression of the endochitinase andchitobiosidase genes significantly increased the number of flowers and fruit onthe plants, resulting in an increase in yield of fruit. One of the primarygoals of crop breeding programs is to increase the productivity of plants. These twogenes were directly associated with plant productivity, and should be studied further.

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References

  • Benhamou N. and Asselin A. 1989. Attempted localization of a substrate for chitinase in plant cell reveals abundant N-acetyl-D-glucosamine residues in secondary wall. Biol. Cell 67: 341-350.

    Google Scholar 

  • Benhamou N., Joosten M. and De Wit J.G.M. 1990. Subcellular localization of chitinase and of its potential substrate in tomato root tissues infected by Fusarium oxysporum f. sp. radicis-lycopersici. Plant Physiol. 92: 1108-1120.

    Google Scholar 

  • Boller T. 1987. Hydrolytic enzymes in plant disease resistance. In: Kosuge T. and Nestor E. (eds), Plant-Microbe Interaction. Vol. 2. Macmillan, New York, pp. 385-480.

    Google Scholar 

  • Broekaert W.F., Van Parijs J., Allen A.K. and Peumans W.J. 1988. Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat. Physiol. Mol. Plant Pathol. 33: 319-331.

    Google Scholar 

  • Broglie K., Chet I., Hollyday M., Cressman R., Biddle P., Knowlton S. et al. 1991. Transgenic plants with enhance resistance to the fungal pathogen Rhizoctonia solani. Science 245: 1194-1197.

    Google Scholar 

  • Cheung W.Y., Hubert N. and Laundry B.S. 1993. A simple and rapid DNA microextraction method for plant, animal, and insect suitable for RAPD and other PCR analysis. PCR Meth. Appl. 3: 69-70.

    Google Scholar 

  • Collinge D.B., Kragh K.M., Mikkelsen J.D., Nielsen K.K., Rasmussen U. and Vad K. 1993. Plant Chitinases. Plant J. 3: 31-40.

    Google Scholar 

  • Cote F. and Hahn M.G. 1994. Oligosaccharides: structures and signal transduction. Plant Mol. Biol. 26: 1379-1411.

    Google Scholar 

  • De Jong A.J., Cordewener J., Schiavo L.F., Terzi M., Vandekerckhove J., van Kammen A. et al. 1992. A carrot somatic embryo mutant is rescued by chitinase. Plant Cell 4: 425-433.

    Google Scholar 

  • Dong J.K. and Dunstan D.I. 1997. Endochitinase and B-1,3-glucanase genes are developmentally regulated during somatic embryogenesis in Picea glauca. Planta 201: 189-194.

    Google Scholar 

  • Flach J., Pilet P.E. and Jolles P. 1992. What's new in chitinase research? Experientia 48: 701-716.

    Google Scholar 

  • Fulton T.M., Chunwongse J. and Tansksley S.D. 1995. Micropep protocole for extraction of DNA from tomato and other herbaceous plants. Plant Mol. Biol. Rep. 13: 207-209.

    Google Scholar 

  • Gongora C.E., Wang S., Barbehenn R.V. and Broadway R.M. 2001. Chitinolytic enzymes from Streptomyces albidoflavus expresses in tomato plants: Effects on Trichoplusia ni (Lepidoptera: Noctuidae). Entomol. Exp. Appl. 99: 193-204.

    Google Scholar 

  • Hammond K.K. and Jones J. 1996. Resistance gene-dependent plant defense responses. Plant Cell 8: 1773-1791.

    Google Scholar 

  • Hanfrey C., Fife M. and Buchanan-Wollaston V. 1996. Leaf senescence in Brassica napus: expression of genes encoding pathogenesis-related proteins. Plant Mol. Biol. 30: 597-609.

    Google Scholar 

  • Harikrishna K., Jampates B.R., Milligan S.B. and Gasser C.S. 1996. An endochitinase gene expressed at high levels in the stylar transmitting tissue of tomatoes. Plant Mol. Biol. 30: 899-911.

    Google Scholar 

  • Heese-Peck A., Cole R.N., Borkhsenious O.N., Hart G.H. and Raikhel N.V. 1995. Plant nuclear pore complex proteins are modified by novel oligossacharides with terminal N-acetylglucosamine. Plant Cell 7: 1459-1471.

    Google Scholar 

  • Hughes R.K. and Dickerson A.G. 1991. Modulation of elicitor-induced chitinase and b-1,3-glucanase activity by hormones in Phaseolus vulgaris. Plant Cell Physiol. 32: 853-861.

    Google Scholar 

  • Karban R. and Myers J.H. 1989. Induce plant response to herbivory. Annu. Rev. Ecol. Syst. 20: 331-348.

    Google Scholar 

  • Leung D.W. 1992. Involvement of plant chitinase in sexual reproduction of higuer plants. Phytochemistry 31: 1899-1900.

    Google Scholar 

  • Lin W., Anuratha C.J., Datta K., Potrykus I., Muthukrishnan S. and Datta S.K. 1995. Genetic engineering of rice for resistance to sheath blight. Biotechnology 13: 686-691.

    Google Scholar 

  • Mauch F., Mauch-Mani B. and Boller T. 1988. Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and b-1,3-glucanses. Plant Physiol. 88: 936-942.

    Google Scholar 

  • McCormick S., Niedermeyer J., Fry J., Barnason A., Horsch R. and Fraley R. 1986. Leaf disc transformation of cultivated tomato (L. esculentum) using Agrobacterium tumefaciens. Plant cell report 5: 81-84.

    Google Scholar 

  • Neale A.D., Wahleithner J.A., Lund M., Bonnett H.T., Kelly A., Meeks-Wagner D.R. et al. 1990. Chitinase, b-1,3-glucanase, osmotin, and extensin are expressed in tobacco explants during flower formation. Plant Cell 2: 673-684.

    Google Scholar 

  • Nishizawa Y., Nishio Z., Nakazono K., Soma M., Nakajima E., Ugaki M. et al. 1999. Enhanced resistance to blast (Magnaporthe grisea) in transgenic Japonica rice by constitutive expression of rice chitinase. TAG 99: 383-390.

    Google Scholar 

  • Patil V.R. and Widholm J.M. 1997. Possible correlation between increased vigour and chitinase activity espression in tobacco. J. Exp. Bot. 48: 1943-1950.

    Google Scholar 

  • Pierard D., Jacqmard A., Bernier J. and Salmon J. 1980. Appearance and disappearance of proteins in the shoot apical meristem of Sinapis alba in transition to flowering. Planta 150: 397-405.

    Google Scholar 

  • Roberts W.K. and Selitrennikoff C.P. 1988. Plant and bacterial chitinases differ in antifungal activity. J. Gen. Micro. 134: 169-176.

    Google Scholar 

  • Robinson S.P., Jacobs A.K. and Dry I.B. 1997. A class IV chitinase is highly expressed in grape berries during ripening. Plant Physiol. 114: 771-778.

    Google Scholar 

  • Roby D. and Esquerre-Tugaye M.T. 1987. Induction of chitinases and of translatable mRNA for these enzymes in melon plants infected with Colletotrichum lagenarium. Plant Sci. 52: 175-185.

    Google Scholar 

  • Schickler H. and Chet I. 1997. Heterologous chitinase gene expression to improve plant defense against phytopathogenic fungi. J. Industrial Microbiol. Biotechnol. 19: 196-201.

    Google Scholar 

  • Schlumbaum A., Mauch F., Vogeli U. and Boller T. 1986. Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365-367.

    Google Scholar 

  • Sela-Buurlage M.B., Ponstein A.S., Bres-Vloemans S.A., Melchers L.S., Van den Elzen P.J. and Cornelissen B.J. 1993. Only specific tobacco (Nicotiana tabacum) chitinases and B-1,3-glucanases exhibit antifungal activity. Plant Physiol. 101: 857-863.

    Google Scholar 

  • Spaink H.P., Wijfjes A.H., van Vilet T.B., Kijne L.W. and Lugtenberg J.J. 1993. Rhizobial lipo-oligosaccharide signals and their role in plant morphogenesis: are analogous lipophilic chitin derivatives produced by the plant? Aust. J. Plant Physiol. 20: 381-392.

    Google Scholar 

  • Tabei Y., Kitade S., Nishizawa Y., Kikuchi N., Kayano T., Hibi T. et al. 1998. Transgenic cucumber plants harboring a rice chitinase gene exhibit enhance resistance to gray mold (Botrytis cinerea). Plant Cell Report 17: 159-164.

    Google Scholar 

  • van Hengel A.J., Guzzo F., van Kammen A. and de Vries S. 1998. Expression pattern of the carrot EP3 endochitinase genes in suspension culture and in developing seeds. Plant Physiol. 117: 43-53.

    Google Scholar 

  • Varner J.E. and Lin L.S. 1989. Plant cell wall architecture. Cell 56: 231-239.

    Google Scholar 

  • Vogeli-Lange R., Frundt C., Hart C.M., Beffa R., Nagy F. and Meins F. 1994. Evidence for a role of B-1,3-glucanase in dicot seed germination. Plant J. 5: 273-278.

    Google Scholar 

  • Vogelsang R. and Barz W. 1990. Elicitation of b-1,3-glucanase and chitinase activities in cell suspension cultures of Ascochyta rabiei resistant and susceptible cultivars of chickpea (Cicer arietinum). Z. Naturforsch. 45c: 233-239.

    Google Scholar 

  • Wu S., Kriz A.L. and Widholm J.M. 1994. Molecular analysis of two cDNA clones encoding acidic class I chitinase in maize. Plant Physiol. 105: 1097-1105.

    Google Scholar 

  • Xue B., Gonsalves C., Provvidenti R., Slightom J.L., Fuchs M. and Gonsalves D. 1994. Development of transgenic tomato expressing a high level of resistance to cucumber mosaic virus strains of subgroups I and II. Plant Dis. 78: 1038-1041.

    Google Scholar 

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Correspondence to Carmenza E. Gongora.

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Gongora, C.E., Broadway, R.M. Plant growth and development influenced by transgenic insertion of bacterial chitinolytic enzymes. Molecular Breeding 9, 123–135 (2002). https://doi.org/10.1023/A:1026732124713

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