메뉴 건너뛰기




Volumn 48, Issue 2, 2004, Pages 185-191

Transformation of tobacco plants with cDNA encoding honeybee royal jelly MRJP1

Author keywords

Agrobacterium tumefaciens; major royal jelly protein; Nicotiana tabacum; recombinant protein; transgenic plant

Indexed keywords

AGROBACTERIUM; AGROBACTERIUM TUMEFACIENS; APIS MELLIFERA; EMBRYOPHYTA; EUKARYOTA; NICOTIANA; NICOTIANA OBTUSIFOLIA; NICOTIANA TABACUM; RHIZOBIUM;

EID: 3142694824     PISSN: 00063134     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:BIOP.0000033443.60872.f1     Document Type: Article
Times cited : (13)

References (39)
  • 2
    • 0030366727 scopus 로고    scopus 로고
    • 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
    • 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.
    • (1996) J. Apic. Res. , vol.35 , pp. 63-68
    • Albert, Š.1    Klaudiny, J.2    Šimúth, J.3
  • 3
    • 0033136389 scopus 로고    scopus 로고
    • Molecular characterization of MRJP, highly polymorphic protein of honeybee (Apis mellifera) royal jelly
    • 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.
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 427-434
    • Albert, Š.1    Klaudiny, J.2    Šimúth, J.3
  • 5
    • 0028369233 scopus 로고
    • Fertile transgenic wheat from microprojectile bombardment of scutellar tissue
    • Becker, D., Brettschneider, R., Lorz, H.: Fertile transgenic wheat from microprojectile bombardment of scutellar tissue. - Plant J. 5: 299-307, 1994.
    • (1994) Plant J. , vol.5 , pp. 299-307
    • Becker, D.1    Brettschneider, R.2    Lorz, H.3
  • 6
    • 0036185318 scopus 로고    scopus 로고
    • 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
    • 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.
    • (2002) Plant Cell Rep. , vol.20 , pp. 848-856
    • Bellucci, M.1    Alpini, A.2    Arcioni, S.3
  • 7
    • 0021771482 scopus 로고
    • Binary Agrobacterium vectors for plant transformation
    • Bevan, M.W.: Binary Agrobacterium vectors for plant transformation. - Nucl. Acids Res. 22: 8711-8721, 1984.
    • (1984) Nucl. Acids Res. , vol.22 , pp. 8711-8721
    • Bevan, M.W.1
  • 8
    • 0037174146 scopus 로고    scopus 로고
    • Apisimin, a new serine valin-rich peptide from honeybee (Apis mellifera L.) royal jelly: Purification and molecular characterization
    • 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.
    • (2002) FEBS Lett. , vol.528 , pp. 125-129
    • Bíliková, K.1    Hanes, J.2    Nordhoff, E.3    Saenger, W.4    Klaudiny, J.5    Šimúth, J.6
  • 9
    • 0034213006 scopus 로고    scopus 로고
    • Engineering chloroplasts: An alternative site for foreign genes, proteins, reactions and products
    • Bogorad, L.: Engineering chloroplasts: an alternative site for foreign genes, proteins, reactions and products. - TIBTECH 18: 257-263, 2000.
    • (2000) TIBTECH , vol.18 , pp. 257-263
    • Bogorad, L.1
  • 10
    • 0002471977 scopus 로고    scopus 로고
    • The production of recombinant glycoproteins with defined non-immunogenic glycans
    • Owen, M.R.L., Pen, J. (ed): John Wiley & Sons, New York
    • 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.
    • (1996) Transgenic Plants: A Production System for Industrial and Pharmaceutical Proteins , pp. 99-113
    • Chrispeels, M.J.1    Faye, L.2
  • 11
    • 14744291338 scopus 로고
    • 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
    • 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.
    • (1991) Bio/Technology , vol.9 , pp. 957-962
    • Christou, P.1    Ford, T.L.2    Kofron, M.3
  • 12
    • 0025840490 scopus 로고
    • Gene transfer with subsequent removal of the selection gene from the host genome
    • 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.
    • (1991) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 10558-10562
    • Dale, E.C.1    Ow, D.W.2
  • 13
    • 0035979785 scopus 로고    scopus 로고
    • Expression of the native cholera toxin B subunit gene and assembly of functional oligomers in transgenic tobacco chloroplasts
    • 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.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1001-1009
    • Daniell, H.1    Lee, S.B.2    Panchal, T.3    Wiebe, P.O.4
  • 15
    • 1842349188 scopus 로고
    • Broad host range DNA cloning system for Gram-negative bacteria: Construction of a gene bank in Rhizobium meliloti
    • 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.
    • (1980) Proc. Nat. Acad. Sci. USA , vol.77 , pp. 7347-7351
    • Ditta, G.1    Stanfield, S.2    Corbin, D.3    Helinski, D.R.4
  • 16
    • 21144477712 scopus 로고
    • Identification and partial characterization of the major royal jelly protein of the honey bee (Apis mellifera L.)
    • 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.
    • (1992) J. Apic. Res. , vol.31 , pp. 22-26
    • Hanes, J.1    Šimúth, J.2
  • 17
    • 0003448569 scopus 로고
    • Purification of antibodies by using a DEAE matrix (batch)
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • 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.
    • (1988) Antibodies: A Laboratory Manual , pp. 302-303
    • Harlow, E.1    Lane, D.2
  • 18
    • 20444410843 scopus 로고    scopus 로고
    • Expression of choline oxidase gene (codA) enhances salt tolerance of the tobacco
    • 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.
    • (2001) Acta Biochim. Biophys. Sin. , vol.33 , pp. 519-524
    • He, P.H.1    Zhang, D.B.2    Liang, W.Q.3    Yao, Q.H.4    Zhang, R.X.5
  • 20
    • 17744408947 scopus 로고    scopus 로고
    • Preparation of recombinant most abundant protein MRJP1 of royal jelly
    • Júdová, J., Klaudiny, J., Šimúth, J.: Preparation of recombinant most abundant protein MRJP1 of royal jelly. - Biologia 53: 777-784, 1998.
    • (1998) Biologia , vol.53 , pp. 777-784
    • Júdová, J.1    Klaudiny, J.2    Šimúth, J.3
  • 21
    • 0031947199 scopus 로고    scopus 로고
    • Comparisons of the efficiency of some promoters in silver birch (Betula pendula)
    • 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.
    • (1998) Plant Cell Rep. , vol.17 , pp. 356-361
    • Keinonen-Mettälä, K.1    Pappinen, A.2    Von Weissenberg, K.3
  • 22
    • 0029269727 scopus 로고
    • N-linked sugar chains of 350 kDa royal jelly glycoprotein
    • Kimura, Y., Washino, N., Yonekura, M.: N-linked sugar chains of 350 kDa royal jelly glycoprotein. - Biosci. Biotech. Biochem. 59: 507-509, 1995.
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 507-509
    • Kimura, Y.1    Washino, N.2    Yonekura, M.3
  • 23
    • 0028002024 scopus 로고
    • Molecular cloning of two cDNAs from the head of the nurse honey bee (Apis mellifera L.) for coding related proteins of royal jelly
    • 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.
    • (1994) J. Apic. Res. , vol.33 , pp. 105-111
    • Klaudiny, J.1    Hanes, J.2    Kulifajová, J.3    Albert, Š.4    Šimúth, J.5
  • 24
    • 0034792503 scopus 로고    scopus 로고
    • Effect of an enhanced CaMV 35S promoter and fruit-specific promoter on UIDA gene expression in transgenic tomato plants
    • 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.
    • (2001) In Vitro Cell. Dev. Biol. Plant , vol.37 , pp. 427-433
    • Krasnyanski, S.F.1    Sandhu, J.2    Domier, L.L.3    Buetow, D.E.4    Korban, S.S.5
  • 25
    • 0031875965 scopus 로고    scopus 로고
    • A royal jelly protein is expressed in a subset of Kenyon cells in the mushroom bodies of the honey bee brain
    • 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.
    • (1998) Naturwissenschaften , vol.85 , pp. 343-346
    • Kucharski, R.1    Maleszka, R.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. - Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0034776257 scopus 로고    scopus 로고
    • Constitutive and seed-specific expression of a maize lysine-feedback insensitive dihydrodipicolinate synthase gene leads to increased free lysine levels in rice seeds
    • 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.
    • (2001) Mol. Breed. , vol.8 , pp. 75-84
    • Lee, S.I.1    Kim, H.U.2    Lee, Y.H.3    Suh, S.C.4    Lim, Y.P.5    Lee, H.Y.6    Kim, H.I.7
  • 28
    • 0037448609 scopus 로고    scopus 로고
    • 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
    • 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.
    • (2003) Gene , vol.303 , pp. 165-175
    • Malecová, B.1    Ramser, J.2    O'Brien, J.K.3    Janitz, M.4    Júdová, J.5    Lehrach, H.6    Šimúth, J.7
  • 29
    • 0036144704 scopus 로고    scopus 로고
    • Gastrointestinal enzyme production of bioactive peptides from royal jelly protein and their antihypertensive activity
    • 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.
    • (2002) J. Nutr. Biochem. , vol.13 , pp. 80-86
    • Matsui, T.1    Ykiyoshi, A.2    Doi, S.3    Sugimoto, H.4    Yamada, H.5    Matsumoto, K.6
  • 30
    • 0002320412 scopus 로고
    • Polyethylene glycol-mediated transformation of tobacco leaf mesophyll protoplasts: An experiment in the study of Cre-lox recombination
    • Maliga, P., Klessig, D., Cashmore, A., Gruissem, W., Varner, J., (ed.): Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • 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.
    • (1995) Methods in Plant Molecular Biology, a Laboratory Manual , pp. 1-17
    • Morgan, M.K.1    Ow, D.W.2
  • 31
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco cultures
    • Murashige, T., Skoog, F.: A revised medium for rapid growth and bioassays with tobacco cultures. - Physiol. Plant. 15: 473-497, 1962.
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 32
    • 0030695026 scopus 로고    scopus 로고
    • 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.
    • 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.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 797-802
    • Ohashi, K.1    Natori, S.2    Kubo, T.3
  • 33
    • 0035096386 scopus 로고    scopus 로고
    • Supression of allergic reactions by royal jelly in association with restoration of macrophage function and the improvement of Th1/Th2 cell response
    • 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.
    • (2001) Int. Immunopharmacol. , vol.1 , pp. 521-532
    • Oka, H.1    Emori, Y.2    Kobayashi, N.3    Hayashi, Y.4    Nomoto, K.5
  • 37
    • 0035109783 scopus 로고    scopus 로고
    • Some properties of the main protein of honeybee (Apis mellifera) royal jelly
    • Šimúth, J.: Some properties of the main protein of honeybee (Apis mellifera) royal jelly. - Apidologie 32: 69-80, 2001.
    • (2001) Apidologie , vol.32 , pp. 69-80
    • Šimúth, J.1
  • 38
    • 0032127583 scopus 로고    scopus 로고
    • Engineering plant protein composition for improved nutrition
    • Tabe, L., Higgins, T.J.V.: Engineering plant protein composition for improved nutrition. - Trends Plant Sci. 3: 282-286, 1998.
    • (1998) Trends Plant Sci. , vol.3 , pp. 282-286
    • Tabe, L.1    Higgins, T.J.V.2
  • 39
    • 0032125858 scopus 로고    scopus 로고
    • Expression of the Brazil nut methionine-rich protein and mutants with increased methionine in transgenic potato
    • 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.
    • (1998) Plant Mol. Biol. , vol.37 , pp. 829-838
    • Tu, H.M.1    Godfrey, L.W.2    Sun, S.S.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.