Biologia plantarum 48:185-191, 2004 | DOI: 10.1023/B:BIOP.0000033443.60872.f1

Transformation of Tobacco Plants with cDNA Encoding Honeybee Royal Jelly MRJP1

J. Júdová1, R. Šutka1, J. Klaudiny1, D. Lišková1, D.W. Ow2, J. Šimúth1,*
1 Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovak Republic
2 USDA Plant Gene Expression Center, Albany, USA

For expression of MRJP1 - the most abundant protein of honeybee royal jelly - in plants, plasmid carrying the expression cassette composed of CaMV 35S RNA promoter, cDNA encoding MRJP1 with its native signal peptide, and nos3' as transcription terminator in binary vector pBin19 was prepared. The plasmid was introduced into tobacco (Nicotiana tabacum L. cv. Wi38) plants by Agrobacterium tumefaciens-mediated transformation. Transgenic F1 and F2 generation was grown from the seeds of the primary obtained transgenic tobacco plants. Immunoblot analyses of protein leaf extracts from transgenic plants showed expression of MRJP1.

Keywords: Agrobacterium tumefaciens; major royal jelly protein; Nicotiana tabacum; recombinant protein; transgenic plant
Subjects: Agrobacterium-mediated transformation; Agrobacterium tumefaciens; auxins; immunoblot; Nicotiana tabacum; polymerase chain reaction (PCR); protein, major royal gelly; recombinant protein; tobacco, transformation, honeybee royal jelly; transformation, Agrobacterium-mediated; transgenic plants

Published: June 1, 2004Show citation

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Júdová, J., Šutka, R., Klaudiny, J., Lišková, D., Ow, D.W., & Šimúth, J. (2004). Transformation of Tobacco Plants with cDNA Encoding Honeybee Royal Jelly MRJP1. Biologia plantarum, 48(2), 185-191. doi: 10.1023/B:BIOP.0000033443.60872.f1.
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    References

    1. Albert, Š., Bhattacharya, D., Klaudiny, J., Schmitzová, J., Šimúth, J.: The family of major royal jelly proteins and its evolution.-J. mol. Evol. 49: 290-297, 1999b. Go to original source...
    2. Albert, Š., Klaudiny, J., Šimúth, J.: Newly discovered features of updated sequence of royal jelly protein RJP57-1; longer repetitive region on C-terminus and homology to Drosophila melanogaster yellow protein.-J. apic. Res. 35: 63-68, 1996. Go to original source...
    3. Albert, Š., Klaudiny, J., Šimúth, J.: Molecular characterization of MRJP, highly polymorphic protein of honeybee (Apis mellifera) royal jelly.-Insect Biochem. mol. Biol. 29: 427-434, 1999a.
    4. Ausubel, M.F., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K.: Current Protocols in Molecular Biology. Vol. 2.-John Wiley & Sons, New York 1996.
    5. Becker, D., Brettschneider, R., Lorz, H.: Fertile transgenic wheat from microprojectile bombardment of scutellar tissue.-Plant J. 5: 299-307, 1994. Go to original source...
    6. Bellucci, M., Alpini, A., Arcioni, S.: Zein accumulation in forage species (Lotus corniculatus and Medicago saliva) and co-expression of the gamma-zein: KDEL and beta-zein: KDEL polypeptides in tobacco leaf.-Plant Cell Rep. 20: 848-856, 2002. Go to original source...
    7. Bevan, M.W.: Binary Agrobacterium vectors for plant transformation.-Nucl. Acids Res. 22: 8711-8721, 1984. Go to original source...
    8. Bíliková, K., Hanes, J., Nordhoff, E., Saenger, W., Klaudiny, J., Šimúth, J.: Apisimin, a new serine valin-rich peptide from honeybee (Apis mellifera L.) royal jelly: purification and molecular characterization.-FEBS Lett. 528, 125-129, 2002. Go to original source...
    9. Bogorad, L.: Engineering chloroplasts: an alternative site for foreign genes, proteins, reactions and products.-TIBTECH 18: 257-263, 2000. Go to original source...
    10. Chrispeels, M.J., Faye, L.: The production of recombinant glycoproteins with defined non-immunogenic glycans.-In: Owen, M.R.L., Pen, J. (ed): Transgenic Plants: A Production System for Industrial and Pharmaceutical Proteins. Pp. 99-113. John Wiley & Sons, New York 1996.
    11. Christou, P., Ford, T.L., Kofron, M.: Production of transgenic rice (Oryza sativa L.) plants from agronomically important indica and japonica varieties via electric discharge particle acceleration of exogenous DNA into immature zygotic embryos.-Bio/Technology 9: 957-962, 1991. Go to original source...
    12. Dale, E.C., Ow, D.W.: Gene transfer with subsequent removal of the selection gene from the host genome.-Proc. nat. Acad. Sci. USA 88: 10558-10562, 1991. Go to original source...
    13. Daniell, H., Lee, S.B., Panchal, T., Wiebe, P.O.: Expression of the native cholera toxin B subunit gene and assembly of functional oligomers in transgenic tobacco chloroplasts.-J. mol. Biol. 311: 1001-1009, 2001. Go to original source...
    14. Dellaporta, S.L., Wood, J., Hicks, J.B.: A plant DNA minipreparation: version 2.-Plant mol. Biol. Rep. 1: 19-22, 1983. Go to original source...
    15. Ditta, G., Stanfield, S., Corbin, D., Helinski, D.R.: Broad host range DNA cloning system for Gram-negative bacteria: Construction of a gene bank in Rhizobium meliloti.-Proc. nat. Acad. Sci. USA 77: 7347-7351, 1980. Go to original source...
    16. Hanes, J., Šimúth, J.: Identification and partial characterization of the major royal jelly protein of the honey bee (Apis mellifera L.).-J. apic. Res. 31: 22-26, 1992. Go to original source...
    17. Harlow, E., Lane, D.: Purification of antibodies by using a DEAE matrix (batch).-In: Antibodies: a Laboratory Manual. Pp. 302-303. Cold Spring Harbor Laboratory Press, Cold Spring Harbor 1988.
    18. He, P.H., Zhang, D.B., Liang, W.Q., Yao, Q.H., Zhang, R.X.: Expression of choline oxidase gene (codA) enhances salt tolerance of the tobacco.-Acta biochim. biophys. sin. 33: 519-524, 2001.
    19. Horsch, R.B., Fry, J.E., Hoffmann, N.L., Eichholtz, D., Rogers, S.G., Fraley, R.T.: A simple and general method for transferring genes into plants.-Science 227: 1229-1231, 1985.
    20. Júdová, J., Klaudiny, J., Šimúth, J.: Preparation of recombinant most abundant protein MRJP1 of royal jelly.-Biologia 53: 777-784, 1998.
    21. Keinonen-Mettälä, K., Pappinen, A., von Weissenberg, K.: Comparisons of the efficiency of some promoters in silver birch (Betula pendula).-Plant Cell Rep. 17: 356-361, 1998.
    22. Kimura, Y., Washino, N., Yonekura, M.: N-linked sugar chains of 350 kDa royal jelly glycoprotein.-Biosci. Biotech. Biochem. 59: 507-509, 1995. Go to original source...
    23. Klaudiny, J., Hanes, J., Kulifajová, J., Albert, Š., Šimúth, J.: Molecular cloning of two cDNAs from the head of the nurse honey bee (Apis mellifera L.) for coding related proteins of royal jelly.-J. apic. Res. 33: 105-111, 1994. Go to original source...
    24. Krasnyanski, S.F., Sandhu, J., Domier, L.L., Buetow, D.E., Korban, S.S.: Effect of an enhanced CaMV 35S promoter and fruit-specific promoter on UIDA gene expression in transgenic tomato plants.-In Vitro cell. dev. Biol. Plant 37: 427-433, 2001. Go to original source...
    25. Kucharski, R., Maleszka, R.: A royal jelly protein is expressed in a subset of Kenyon cells in the mushroom bodies of the honey bee brain.-Naturwissenschaften 85: 343-346, 1998. Go to original source...
    26. Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4.-Nature 227: 680-685, 1970. Go to original source...
    27. Lee, S.I., Kim, H.U., Lee, Y.H., Suh, S.C., Lim, Y.P., Lee, H.Y., Kim, H.I.: Constitutive and seed-specific expression of a maize lysine-feedback insensitive dihydrodipicolinate synthase gene leads to increased free lysine levels in rice seeds.-Mol. Breed. 8: 75-84, 2001. Go to original source...
    28. Malecová, B., Ramser, J., O'Brien, J.K., Janitz, M., Júdová, J., Lehrach, H., Šimúth, J.: Honeybee (Apis mellifera L.) mrjp gene family: computational analysis of putative promoters and genomic structure of mrjp, the gene coding for the most abundant protein of larval food.-Gene 303: 165-175, 2003. Go to original source...
    29. Matsui, T., Ykiyoshi, A., Doi, S., Sugimoto, H., Yamada, H., Matsumoto, K.: Gastrointestinal enzyme production of bioactive peptides from royal jelly protein and their antihypertensive activity.-J. nutr. Biochem. 13: 80-86, 2002. Go to original source...
    30. Morgan, M.K., Ow, D.W.: Polyethylene glycol-mediated transformation of tobacco leaf mesophyll protoplasts: an experiment in the study of Cre-lox recombination.-In: Maliga, P., Klessig, D., Cashmore, A., Gruissem, W., Varner, J., (ed.): Methods in Plant Molecular Biology, a Laboratory Manual. Pp. 1-17. Cold Spring Harbor Laboratory Press, Cold Spring Harbor 1995.
    31. Murashige, T., Skoog, F.: A revised medium for rapid growth and bioassays with tobacco cultures.-Physiol. Plant. 15: 473-497, 1962. Go to original source...
    32. Ohashi, K., Natori, S., Kubo, T.: Change in the mode of gene expression of the hypopharyngeal gland cells with an age-dependent role change of the worker honeybee Apis mellifera L.-Eur. J. Biochem. 249: 797-802, 1997. Go to original source...
    33. Oka, H., Emori, Y., Kobayashi, N., Hayashi, Y., Nomoto, K.: Supression of allergic reactions by royal jelly in association with restoration of macrophage function and the improvement of Th1/Th2 cell response.-Int. Immunopharmacol. 1: 521-532, 2001. Go to original source...
    34. Schmitzová, J., Klaudiny, J., Albert, Š., Schröder, W., Schreckengost, W., Hanes, J., Júdová, J., Šimúth, J.: A family of major royal jelly proteins of the honey bee (Apis mellifera L.).-J. cell. mol. Life Sci. 54: 1020-1030, 1998. Go to original source...
    35. Schroeder, H.E., Khan, M.R.I., Knibb, W.R., Spencer, D., Higgins, T.J.V.: Expression of a chicken ovalbumin gene in three lucerne cultivars.-Aust. J. Plant Physiol. 18: 495-505, 1991.
    36. Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, M.D., Provenzano, E.K., Fujimoto, E.K., Goeke, N.M., Olson, B.J., Klenk, D.C.: Bicinchoninic acid protein assay.-Anal. Biochem. 150: 76, 1985. Go to original source...
    37. Šimúth, J.: Some properties of the main protein of honeybee (Apis mellifera) royal jelly.-Apidologie 32: 69-80, 2001. Go to original source...
    38. Tabe, L., Higgins, T.J.V.: Engineering plant protein composition for improved nutrition.-Trends Plant Sci. 3: 282-286, 1998. Go to original source...
    39. Tu, H.M., Godfrey, L.W., Sun, S.S.M.: Expression of the Brazil nut methionine-rich protein and mutants with increased methionine in transgenic potato.-Plant mol. Biol. 37: 829-838, 1998. Go to original source...

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