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Volumn 7, Issue 4, 1997, Pages 359-372

Transcript levels for a mung bean cysteine protease during early seedling growth

Author keywords

CDNA; Cysteine endopeptidase; Expression; Mung bean; Regulation

Indexed keywords


EID: 0031464848     PISSN: 09602585     EISSN: None     Source Type: Journal    
DOI: 10.1017/s0960258500003767     Document Type: Article
Times cited : (10)

References (31)
  • 1
    • 0024978457 scopus 로고
    • Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds
    • Akasofu, H., Yamauchi, D., Mitsuhashi, W. and Minamikawa, T. (1989) Nucleotide sequence of cDNA for sulfhydryl-endopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds. Nucleic Acids Research 17, 6733.
    • (1989) Nucleic Acids Research , vol.17 , pp. 6733
    • Akasofu, H.1    Yamauchi, D.2    Mitsuhashi, W.3    Minamikawa, T.4
  • 2
    • 0017407885 scopus 로고
    • Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung bean seedlings
    • Baumgartner, B. and Chrispeels, M.J. (1977) Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung bean seedlings. European Journal of Biochemistry 77, 223-233.
    • (1977) European Journal of Biochemistry , vol.77 , pp. 223-233
    • Baumgartner, B.1    Chrispeels, M.J.2
  • 3
    • 0018091598 scopus 로고
    • Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedling by immuno-fluorescence microscopy
    • Baumgartner, B., Tokuyasu, K.T. and Chrispeels, M.J. (1978) Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedling by immuno-fluorescence microscopy. Journal of Cell Biology 79, 10-19.
    • (1978) Journal of Cell Biology , vol.79 , pp. 10-19
    • Baumgartner, B.1    Tokuyasu, K.T.2    Chrispeels, M.J.3
  • 6
    • 0002678206 scopus 로고
    • Isolation of total and polysomal RNA from plant tissues
    • Gelvin, S.B., Schilperoort, R.A. and Verma, D.P.S. (Eds) Section B6. Dordrecht, Kluwer Academic Publishers, Section B6
    • DeVries, S., Hoge, H. and Bisseling, T. (1988) Isolation of total and polysomal RNA from plant tissues. pp 1-13 in Gelvin, S.B., Schilperoort, R.A. and Verma, D.P.S. (Eds) Plant molecular biology manual. Section B6. Dordrecht, Kluwer Academic Publishers, Section B6.
    • (1988) Plant Molecular Biology Manual , pp. 1-13
    • Devries, S.1    Hoge, H.2    Bisseling, T.3
  • 7
    • 0002730011 scopus 로고
    • Isolation and characterization of glucosamine-containing storage glycoproteins from the cotyledons of Phaseolus aureus
    • Ericson, M.C. and Chrispeels, M.J. (1973) Isolation and characterization of glucosamine-containing storage glycoproteins from the cotyledons of Phaseolus aureus. Plant Physiology 52, 98-100.
    • (1973) Plant Physiology , vol.52 , pp. 98-100
    • Ericson, M.C.1    Chrispeels, M.J.2
  • 8
    • 0020793569 scopus 로고
    • A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A.P. and Vogelstein, B. (1983) A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Analytical Biochemistry 132, 6-13.
    • (1983) Analytical Biochemistry , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 9
    • 0001992521 scopus 로고
    • Hormonal regulation of the development of protease and carboxypeptidase activities in barley aleurone layers
    • Hammerton, R.W. and Ho, T.-HD. (1986) Hormonal regulation of the development of protease and carboxypeptidase activities in barley aleurone layers. Plant Physiology 80, 692-697.
    • (1986) Plant Physiology , vol.80 , pp. 692-697
    • Hammerton, R.W.1    Ho, T.-H.D.2
  • 10
    • 0001286278 scopus 로고
    • Retention of phytohemagglutinin with carboxyterminal tetrapeptide KDEL in the nuclear envelope and the endoplasmic reticulum
    • Herman, E.M., Tague, B.W., Hoffman, L.M., Kjemtrup, S.E. and Chrispeels, M.J. (1990) Retention of phytohemagglutinin with carboxyterminal tetrapeptide KDEL in the nuclear envelope and the endoplasmic reticulum. Planta 182, 305-312.
    • (1990) Planta , vol.182 , pp. 305-312
    • Herman, E.M.1    Tague, B.W.2    Hoffman, L.M.3    Kjemtrup, S.E.4    Chrispeels, M.J.5
  • 11
    • 0030586707 scopus 로고    scopus 로고
    • Pattern of expression and characteristics of a cysteine proteinase cDNa from germinating seeds of pea (Pisum sativum L.)
    • Jones, C.G., Tucker, G.A. and Lycett, G.W. (1996) Pattern of expression and characteristics of a cysteine proteinase cDNA from germinating seeds of pea (Pisum sativum L.). Biochimica et Biophysica Acta 1296, 13-15.
    • (1996) Biochimica et Biophysica Acta , vol.1296 , pp. 13-15
    • Jones, C.G.1    Tucker, G.A.2    Lycett, G.W.3
  • 13
    • 0027191298 scopus 로고
    • The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assays
    • Kembhavi, A.A., Buttle, D.J., Knight, C.G. and Barrett, A.J. (1993) The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assays. Archives of Biochemistry and Biophysics 303, 208-213.
    • (1993) Archives of Biochemistry and Biophysics , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barrett, A.J.4
  • 14
    • 0000405108 scopus 로고
    • Influence of the axis on the enzymes of protein and amide metabolism in the cotyledons of mung bean seedlings
    • Kern, R. and Chrispeels, M.J. (1978) Influence of the axis on the enzymes of protein and amide metabolism in the cotyledons of mung bean seedlings. Plant Physiology 62, 815-817.
    • (1978) Plant Physiology , vol.62 , pp. 815-817
    • Kern, R.1    Chrispeels, M.J.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0004590845 scopus 로고
    • Influence of axis removal on amino, carboxy and endopeptidase activities in cotyledons of germinating Vigna mungo seeds
    • Mitsuhashi, W., Koshiba, T. and Minamikawa, T. (1984) Influence of axis removal on amino, carboxy and endopeptidase activities in cotyledons of germinating Vigna mungo seeds. Plant and Cell Physiology 25, 547-554.
    • (1984) Plant and Cell Physiology , vol.25 , pp. 547-554
    • Mitsuhashi, W.1    Koshiba, T.2    Minamikawa, T.3
  • 17
    • 84897583639 scopus 로고
    • Synthesis and posttranslational activation of sulfhydryl-endopeptidase in cotyledons of germinating Vigna mungo seeds
    • Mitsuhashi, W. and Minamikawa, T. (1989) Synthesis and posttranslational activation of sulfhydryl-endopeptidase in cotyledons of germinating Vigna mungo seeds. Plant Physiology 89, 274-279.
    • (1989) Plant Physiology , vol.89 , pp. 274-279
    • Mitsuhashi, W.1    Minamikawa, T.2
  • 18
    • 0001064980 scopus 로고    scopus 로고
    • Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • Muntz, K. (1996) Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds. Journal of Experimental Botany 47, 605-622.
    • (1996) Journal of Experimental Botany , vol.47 , pp. 605-622
    • Muntz, K.1
  • 20
    • 0000024298 scopus 로고
    • Degradation of storage proteins in germinating seeds
    • Shutov, A.D. and Vaintraub, I.A. (1987) Degradation of storage proteins in germinating seeds. Photochemistry 26, 1557-1566.
    • (1987) Photochemistry , vol.26 , pp. 1557-1566
    • Shutov, A.D.1    Vaintraub, I.A.2
  • 21
    • 0010242584 scopus 로고
    • Expression of an endopeptidase (EP-C1) in Phaseolus vulgaris plants
    • Tanaka, T., Minamikawa, T., Yamauchi, D. and Ogushi, Y. (1993) Expression of an endopeptidase (EP-C1) in Phaseolus vulgaris plants. Plant Physiology 101, 421-428.
    • (1993) Plant Physiology , vol.101 , pp. 421-428
    • Tanaka, T.1    Minamikawa, T.2    Yamauchi, D.3    Ogushi, Y.4
  • 22
    • 0026176684 scopus 로고
    • Nudeotide sequence of cDNA for an endopeptidase (EP-C1) from pods of maturing Phaseolus vulgaris fruits
    • Tanaka, T., Yamauchi, D. and Minamikawa, T. (1991) Nudeotide sequence of cDNA for an endopeptidase (EP-C1) from pods of maturing Phaseolus vulgaris fruits. Plant Molecular Biology 16, 1083-1084.
    • (1991) Plant Molecular Biology , vol.16 , pp. 1083-1084
    • Tanaka, T.1    Yamauchi, D.2    Minamikawa, T.3
  • 23
    • 0028797515 scopus 로고
    • Influence of axis removal on the expression of a gene for cysteine endopeptidase (EP-C1) in French bean cotyledons during germination
    • Terasaki, Y., Yamauchi D., Morikawa, H. and Minamikawa, T. (1995) Influence of axis removal on the expression of a gene for cysteine endopeptidase (EP-C1) in French bean cotyledons during germination. Plant and Cell Physiology 36, 537-541.
    • (1995) Plant and Cell Physiology , vol.36 , pp. 537-541
    • Terasaki, Y.1    Yamauchi, D.2    Morikawa, H.3    Minamikawa, T.4
  • 24
    • 0023647142 scopus 로고
    • Protein transport: Signals and salvage sequences
    • Warren, G. (1987) Protein transport: signals and salvage sequences. Nature 327, 17-18.
    • (1987) Nature , vol.327 , pp. 17-18
    • Warren, G.1
  • 25
    • 0002150829 scopus 로고
    • Role of proteolytic enzymes in the mobilization of protein reserves in the germinating dicot seed
    • Dalling, M.J. (Ed.) Boca Raton, FL, CRC Press
    • Wilson, K.A. (1986) Role of proteolytic enzymes in the mobilization of protein reserves in the germinating dicot seed. pp 19-47 in Dalling, M.J. (Ed.) Plant proteolytic enzymes, Vol. 2. Boca Raton, FL, CRC Press.
    • (1986) Plant Proteolytic Enzymes , vol.2 , pp. 19-47
    • Wilson, K.A.1
  • 26
    • 0002388572 scopus 로고
    • Amino acid sequence of mung bean trypsin inhibitor and its modified forms appearing during germination
    • Wilson, K.A. and Chen, J.C. (1983) Amino acid sequence of mung bean trypsin inhibitor and its modified forms appearing during germination. Plant Physiology 71, 341-349.
    • (1983) Plant Physiology , vol.71 , pp. 341-349
    • Wilson, K.A.1    Chen, J.C.2
  • 27
    • 0002954416 scopus 로고
    • Characterization of the proteinase that initiates the degradation of the trypsin inhibitor in germinating mung beans (Vigna radiata)
    • Wilson, K.A. and Tan-Wilson, A.L. (1987) Characterization of the proteinase that initiates the degradation of the trypsin inhibitor in germinating mung beans (Vigna radiata). Plant Physiology 84, 93-98.
    • (1987) Plant Physiology , vol.84 , pp. 93-98
    • Wilson, K.A.1    Tan-Wilson, A.L.2
  • 28
    • 0002848366 scopus 로고
    • Involvement of carboxypeptidase in the degradation of the mung bean (Vigna radiata) trypsin inhibitor during germination and early seedling growth
    • Wilson, K.A., Rightmire, B.R. and Tan-Wilson, A.L. (1985) Involvement of carboxypeptidase in the degradation of the mung bean (Vigna radiata) trypsin inhibitor during germination and early seedling growth. Qualitas Plantarum, Plant Foods in Human Nutrition 35, 195-211.
    • (1985) Qualitas Plantarum, Plant Foods in Human Nutrition , vol.35 , pp. 195-211
    • Wilson, K.A.1    Rightmire, B.R.2    Tan-Wilson, A.L.3
  • 30
    • 0000214015 scopus 로고
    • Purification and characterization of a cysteine endopeptidase in cotyledons of germinated mung bean seeds
    • Yamaoka, Y., Takeuchi, M. and Morohashi, Y. (1990) Purification and characterization of a cysteine endopeptidase in cotyledons of germinated mung bean seeds. Plant Physiology 94, 561-566.
    • (1990) Plant Physiology , vol.94 , pp. 561-566
    • Yamaoka, Y.1    Takeuchi, M.2    Morohashi, Y.3
  • 31
    • 0000220251 scopus 로고
    • Cysteine endopeptidase from Vigna mungo: Gene structure and expression
    • Yamauchi, D., Akasofu, H. and Minamikawa, T. (1992) Cysteine endopeptidase from Vigna mungo: Gene structure and expression. Plant and Cell Physiology 33, 789-797.
    • (1992) Plant and Cell Physiology , vol.33 , pp. 789-797
    • Yamauchi, D.1    Akasofu, H.2    Minamikawa, T.3


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