메뉴 건너뛰기




Volumn 119, Issue 3, 1999, Pages 859-871

A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of Barley

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID ANALYSIS; DEXTRINASE; ENZYME ACTIVITY; GENE EXPRESSION; GIBBERELLIC ACID; INTRON; MESSENGER RNA; MOLECULAR WEIGHT; PLANT DEVELOPMENT; PROMOTER REGION; PULLULANASE; STARCH;

EID: 0033102225     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.119.3.859     Document Type: Article
Times cited : (65)

References (55)
  • 1
    • 84988160866 scopus 로고
    • The variation in chemical composition of Swedish barleys
    • Aman P, Hesselman K, Tilly A-C (1985) The variation in chemical composition of Swedish barleys. J Cereal Sci 3: 73-77
    • (1985) J Cereal Sci , vol.3 , pp. 73-77
    • Aman, P.1    Hesselman, K.2    Tilly, A.-C.3
  • 2
    • 0023897655 scopus 로고
    • Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15
    • Amemura A, Chakraborty R, Fujita M, Noumi T, Futai M (1988) Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15. J Biol Chem 263: 9271-9275
    • (1988) J Biol Chem , vol.263 , pp. 9271-9275
    • Amemura, A.1    Chakraborty, R.2    Fujita, M.3    Noumi, T.4    Futai, M.5
  • 5
    • 0030238170 scopus 로고    scopus 로고
    • Molecular cloning of cDNAs encoding (1-→4)-β-xylan endohydrolases from the aleurone layer of germinated barley (Hordeum vulgare)
    • Banik M, Garrett TPJ, Fincher GB (1996) Molecular cloning of cDNAs encoding (1-→4)-β-xylan endohydrolases from the aleurone layer of germinated barley (Hordeum vulgare). Plant Mol Biol 31: 1163-1172
    • (1996) Plant Mol Biol , vol.31 , pp. 1163-1172
    • Banik, M.1    Garrett, T.P.J.2    Fincher, G.B.3
  • 6
    • 0031025401 scopus 로고    scopus 로고
    • Structure, hormonal regulation, and chromosomal location of genes encoding barley (1-→4)-β-xylan endohydrolases
    • Banik M, Li C-D, Langridge P, Fincher GB (1997) Structure, hormonal regulation, and chromosomal location of genes encoding barley (1-→4)-β-xylan endohydrolases. Mol Gen Genet 253: 599-608
    • (1997) Mol Gen Genet , vol.253 , pp. 599-608
    • Banik, M.1    Li, C.-D.2    Langridge, P.3    Fincher, G.B.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0025879069 scopus 로고
    • Eukaryotic start and stop translation sites
    • Cavener DR, Ray SC (1991) Eukaryotic start and stop translation sites. Nucleic Acids Res 19: 3185-3192
    • (1991) Nucleic Acids Res , vol.19 , pp. 3185-3192
    • Cavener, D.R.1    Ray, S.C.2
  • 9
    • 0026149592 scopus 로고
    • Primer extension studies on α-amylase mRNAs in barley aleurone. II. Hormonal regulation of expression
    • Chandler PM, Jacobsen JV (1991) Primer extension studies on α-amylase mRNAs in barley aleurone. II. Hormonal regulation of expression. Plant Mol Biol 16: 637-645
    • (1991) Plant Mol Biol , vol.16 , pp. 637-645
    • Chandler, P.M.1    Jacobsen, J.V.2
  • 10
    • 0002746824 scopus 로고
    • The effects of gibberellic acid and abscisic acid on α-amylase mRNA levels in barley aleurone layers studied using an α-amylase cDNA clone
    • Chandler PM, Zwar JA, Jacobsen JV, Higgins TJV, Inglis AS (1984) The effects of gibberellic acid and abscisic acid on α-amylase mRNA levels in barley aleurone layers studied using an α-amylase cDNA clone. Plant Mol Biol 3: 407-418
    • (1984) Plant Mol Biol , vol.3 , pp. 407-418
    • Chandler, P.M.1    Zwar, J.A.2    Jacobsen, J.V.3    Higgins, T.J.V.4    Inglis, A.S.5
  • 11
    • 0027424984 scopus 로고
    • Evolution of polysaccharide hydrolase substrate specificity: Catalytic amino acids are conserved in barley (1-→3,1-→4)-glucanase and (1-→3)-β-glucanase
    • Chen L, Fincher GB, Hoj PB (1993) Evolution of polysaccharide hydrolase substrate specificity: catalytic amino acids are conserved in barley (1-→3,1-→4)-glucanase and (1-→3)-β-glucanase. J Biol Chem 268: 13318-13326
    • (1993) J Biol Chem , vol.268 , pp. 13318-13326
    • Chen, L.1    Fincher, G.B.2    Hoj, P.B.3
  • 12
    • 0000941910 scopus 로고
    • Gibberellic acid enhanced synthesis and release of α-amylase and ribonuclease by isolated barley aleurone layers
    • Chrispeels MJ, Varner JE (1967) Gibberellic acid enhanced synthesis and release of α-amylase and ribonuclease by isolated barley aleurone layers. Plant Physiol 42: 398-406
    • (1967) Plant Physiol , vol.42 , pp. 398-406
    • Chrispeels, M.J.1    Varner, J.E.2
  • 13
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smithies O (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12: 387-395
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 14
    • 0141986391 scopus 로고
    • Development, structure and composition of the barley kernel
    • AW MacGregor, RS Bhatty, eds, American Association of Cereal Chemists, St. Paul, MN
    • Duffus CM, Cochrane MP (1993) Development, structure and composition of the barley kernel. In AW MacGregor, RS Bhatty, eds, Barley: Chemistry and Technology. American Association of Cereal Chemists, St. Paul, MN, pp 31-72
    • (1993) Barley: Chemistry and Technology
    • Duffus, C.M.1    Cochrane, M.P.2
  • 15
    • 0029347013 scopus 로고
    • Biochemical and molecular characterisation of a novel starch synthase from potato tubers
    • Edwards A, Marshall J, Sidebottom C, Visser RGF, Smith AM, Martin C (1995) Biochemical and molecular characterisation of a novel starch synthase from potato tubers. Plant J 8: 283-294
    • (1995) Plant J , vol.8 , pp. 283-294
    • Edwards, A.1    Marshall, J.2    Sidebottom, C.3    Visser, R.G.F.4    Smith, A.M.5    Martin, C.6
  • 16
    • 0000860075 scopus 로고
    • Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains
    • Fincher GB (1989) Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains. Annu Rev Plant Physiol Plant Mol Biol 40: 305-346
    • (1989) Annu Rev Plant Physiol Plant Mol Biol , vol.40 , pp. 305-346
    • Fincher, G.B.1
  • 17
    • 0024212067 scopus 로고
    • Rapid amplification of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • Frohman M, Dush M, Martin G (1988) Rapid amplification of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc Natl Acad Sci USA 85: 8998-9002
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8998-9002
    • Frohman, M.1    Dush, M.2    Martin, G.3
  • 18
    • 0026949721 scopus 로고
    • Gibberellin-responsive elements in the promoter of a barley high-pI α-amylase gene
    • Gubler F, Jacobsen JV (1992) Gibberellin-responsive elements in the promoter of a barley high-pI α-amylase gene. Plant Cell 4: 1435-1441
    • (1992) Plant Cell , vol.4 , pp. 1435-1441
    • Gubler, F.1    Jacobsen, J.V.2
  • 19
    • 0029410792 scopus 로고
    • Gibberellin-regulated expression of a Myb gene in barley aleurone cells: Evidence for Myb transactivation of a high-pI α-amylase gene promoter
    • Gubler F, Kalla R, Roberts JK, Jacobsen JV (1995) Gibberellin-regulated expression of a Myb gene in barley aleurone cells: evidence for Myb transactivation of a high-pI α-amylase gene promoter. Plant Cell 7: 1879-1891
    • (1995) Plant Cell , vol.7 , pp. 1879-1891
    • Gubler, F.1    Kalla, R.2    Roberts, J.K.3    Jacobsen, J.V.4
  • 21
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293: 781-788
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 22
    • 0027439791 scopus 로고
    • Purification and properties of three (1-→3)-β-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)
    • Hrmova M, Fincher GB (1993) Purification and properties of three (1-→3)-β-glucanase isoenzymes from young leaves of barley (Hordeum vulgare). Biochem J 289: 453-461
    • (1993) Biochem J , vol.289 , pp. 453-461
    • Hrmova, M.1    Fincher, G.B.2
  • 23
    • 0029278930 scopus 로고
    • Characterization of the maize gene sugaryl, a determinant of starch composition in kernels
    • James MG, Robertson DS, Meyers AM (1995) Characterization of the maize gene sugaryl, a determinant of starch composition in kernels. Plant Cell 7: 417-429
    • (1995) Plant Cell , vol.7 , pp. 417-429
    • James, M.G.1    Robertson, D.S.2    Meyers, A.M.3
  • 24
    • 0026040317 scopus 로고
    • Comparison of the domain-level organization of starch hydrolases and related enzymes
    • Jesperson HM, MacGregor EA, Sierks MR, Svensson B (1991) Comparison of the domain-level organization of starch hydrolases and related enzymes. Biochem J 280: 51-55
    • (1991) Biochem J , vol.280 , pp. 51-55
    • Jesperson, H.M.1    MacGregor, E.A.2    Sierks, M.R.3    Svensson, B.4
  • 25
    • 0041810350 scopus 로고
    • Gibberellic acid and the fine structure of barley aleurone cells. II. Changes during the synthesis and secretion of α-amylase
    • Jones RL (1969) Gibberellic acid and the fine structure of barley aleurone cells. II. Changes during the synthesis and secretion of α-amylase. Planta 88: 73-86
    • (1969) Planta , vol.88 , pp. 73-86
    • Jones, R.L.1
  • 26
    • 0023664776 scopus 로고
    • An inspection of the domain between putative TATA box and translation start site in 79 plant genes
    • Joshi CP (1987) An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucleic Acids Res 15: 6643-6653
    • (1987) Nucleic Acids Res , vol.15 , pp. 6643-6653
    • Joshi, C.P.1
  • 27
    • 0023176586 scopus 로고
    • Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70
    • Katsuragi N, Takizawa N, Murooka Y (1987) Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70. J Bacteriol 169: 2301-2306
    • (1987) J Bacteriol , vol.169 , pp. 2301-2306
    • Katsuragi, N.1    Takizawa, N.2    Murooka, Y.3
  • 28
    • 0031873219 scopus 로고    scopus 로고
    • Large scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family
    • Kristensen M, Planchot V, Abe J-i, Svensson B (1998) Large scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family. Cereal Chem 75: 473-479
    • (1998) Cereal Chem , vol.75 , pp. 473-479
    • Kristensen, M.1    Planchot, V.2    Abe, J.-I.3    Svensson, B.4
  • 29
    • 0030087964 scopus 로고    scopus 로고
    • Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells
    • Kuo A, Cappelluti S, Cervantes-Cervantes M, Rodriguez M, Bush DS (1996) Okadaic acid, a protein phosphatase inhibitor, blocks calcium changes, gene expression, and cell death induced by gibberellin in wheat aleurone cells. Plant Cell 8: 259-269
    • (1996) Plant Cell , vol.8 , pp. 259-269
    • Kuo, A.1    Cappelluti, S.2    Cervantes-Cervantes, M.3    Rodriguez, M.4    Bush, D.S.5
  • 30
    • 0015051534 scopus 로고
    • The substrate specificity of amylopectin-debranching enzymes from sweet corn
    • Lee EY, Marshall JJ, Whelan WJ (1971) The substrate specificity of amylopectin-debranching enzymes from sweet corn. Arch Biochem Biophys 143: 365-374
    • (1971) Arch Biochem Biophys , vol.143 , pp. 365-374
    • Lee, E.Y.1    Marshall, J.J.2    Whelan, W.J.3
  • 31
    • 0000687121 scopus 로고
    • Development of limit dextrinase in germinated barley (Hordeum vulgare L.). Evidence of proteolytic activation
    • Longstaff MA, Bryce JH (1993) Development of limit dextrinase in germinated barley (Hordeum vulgare L.). Evidence of proteolytic activation. Plant Physiol 101: 881-889
    • (1993) Plant Physiol , vol.101 , pp. 881-889
    • Longstaff, M.A.1    Bryce, J.H.2
  • 33
    • 0002895097 scopus 로고
    • Carbohydrates of the barley grain
    • AW MacGregor, RS Bhatty, eds, American Association of Cereal Chemists, St. Paul, MN
    • MacGregor AW, Fincher GB (1993) Carbohydrates of the barley grain. In AW MacGregor, RS Bhatty, eds, Barley: Chemistry and Technology. American Association of Cereal Chemists, St. Paul, MN, pp 73-130
    • (1993) Barley: Chemistry and Technology , pp. 73-130
    • MacGregor, A.W.1    Fincher, G.B.2
  • 34
    • 0000955950 scopus 로고
    • Limit dextrinase from malted barley: Extraction, purification, and characterization
    • MacGregor AW, Macri LJ, Schroeder SW, Bazin SL (1994a) Limit dextrinase from malted barley: extraction, purification, and characterization. Cereal Chem 71: 610-617
    • (1994) Cereal Chem , vol.71 , pp. 610-617
    • MacGregor, A.W.1    Macri, L.J.2    Schroeder, S.W.3    Bazin, S.L.4
  • 35
    • 0028095685 scopus 로고
    • Purification and characterisation of limit dextrinase inhibitors from barley
    • MacGregor AW, Macri LJ, Schroeder SW, Bazin SL (1994b) Purification and characterisation of limit dextrinase inhibitors from barley. J Cereal Sci 20: 33-41
    • (1994) J Cereal Sci , vol.20 , pp. 33-41
    • Macgregor, A.W.1    Macri, L.J.2    Schroeder, S.W.3    Bazin, S.L.4
  • 36
    • 0002399030 scopus 로고
    • Temperature effects on starch granules in developing barley grains
    • MacLeod LC, Duffus CM (1988) Temperature effects on starch granules in developing barley grains. J Cereal Sci 8: 29-37
    • (1988) J Cereal Sci , vol.8 , pp. 29-37
    • Macleod, L.C.1    Duffus, C.M.2
  • 38
    • 0027113459 scopus 로고
    • Measurement of the content of limit dextrinase in cereal flours
    • McCleary BV (1992) Measurement of the content of limit dextrinase in cereal flours. Carbohydr Res 227: 257-268
    • (1992) Carbohydr Res , vol.227 , pp. 257-268
    • McCleary, B.V.1
  • 40
    • 38249042701 scopus 로고
    • Effects of gibberellic acid and abscisic acid on levels of translatable mRNA for (1-→3,1-→4)-β-glucanase in barley aleurone
    • Mundy J, Fincher GB (1986) Effects of gibberellic acid and abscisic acid on levels of translatable mRNA for (1-→3,1-→4)-β-glucanase in barley aleurone. FEBS Lett 198: 349-352
    • (1986) FEBS Lett , vol.198 , pp. 349-352
    • Mundy, J.1    Fincher, G.B.2
  • 41
    • 0030814320 scopus 로고    scopus 로고
    • Correlation between activities of starch debranching enzyme and alpha-polyglucan structure in endosperms of sugary-1 mutants of rice
    • Nakamura Y, Kubo A, Shimamune T, Matsuda T, Harada K, Satoh H (1997) Correlation between activities of starch debranching enzyme and alpha-polyglucan structure in endosperms of sugary-1 mutants of rice. Plant J 12: 143-153
    • (1997) Plant J , vol.12 , pp. 143-153
    • Nakamura, Y.1    Kubo, A.2    Shimamune, T.3    Matsuda, T.4    Harada, K.5    Satoh, H.6
  • 42
    • 0029681154 scopus 로고    scopus 로고
    • Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm: Purification, cDNA and chromosomal localization of the gene
    • Nakamura Y, Umemoto T, Ogata N, Kuboki Y, Yano M, Sasaki T (1996) Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm: purification, cDNA and chromosomal localization of the gene. Planta 199: 209-218
    • (1996) Planta , vol.199 , pp. 209-218
    • Nakamura, Y.1    Umemoto, T.2    Ogata, N.3    Kuboki, Y.4    Yano, M.5    Sasaki, T.6
  • 43
    • 0000420233 scopus 로고
    • A debranching enzyme deficiency in endosperm of the sugary-1 mutants of maize (Zea mays)
    • Pan D, Nelson OE (1984) A debranching enzyme deficiency in endosperm of the sugary-1 mutants of maize (Zea mays). Plant Physiol 74: 324-328
    • (1984) Plant Physiol , vol.74 , pp. 324-328
    • Pan, D.1    Nelson, O.E.2
  • 44
    • 0031419356 scopus 로고    scopus 로고
    • Programmed cell death in plants
    • Pennell RI, Lamb C (1997) Programmed cell death in plants. Plant Cell 9: 1157-1168
    • (1997) Plant Cell , vol.9 , pp. 1157-1168
    • Pennell, R.I.1    Lamb, C.2
  • 45
    • 0032081295 scopus 로고    scopus 로고
    • Characterization of SU1 isoamylase, a determinant of storage starch structure in maize
    • Rahman A, Wong K, Jane J, Myers AM, James MG (1998) Characterization of SU1 isoamylase, a determinant of storage starch structure in maize. Plant Physiol 117: 425-435
    • (1998) Plant Physiol , vol.117 , pp. 425-435
    • Rahman, A.1    Wong, K.2    Jane, J.3    Myers, A.M.4    James, M.G.5
  • 48
    • 0002440434 scopus 로고    scopus 로고
    • Synthesis of limit dextrinase in germinated barley kernels and aleurone tissues
    • Schroeder SW, MacGregor AW (1998) Synthesis of limit dextrinase in germinated barley kernels and aleurone tissues. J Am Soc Brew Chem 56: 32-37
    • (1998) J Am Soc Brew Chem , vol.56 , pp. 32-37
    • Schroeder, S.W.1    MacGregor, A.W.2
  • 49
    • 0030255869 scopus 로고    scopus 로고
    • Splicing of precursors to mRNA in higher plants: Mechanism, regulation and sub-nuclear organization of the spliceosomal machinery
    • Simpson GG, Filipowicz W (1996) Splicing of precursors to mRNA in higher plants: mechanism, regulation and sub-nuclear organization of the spliceosomal machinery [Review]. Plant Mol Biol 32: 1-41
    • (1996) Plant Mol Biol , vol.32 , pp. 1-41
    • Simpson, G.G.1    Filipowicz, W.2
  • 50
    • 85013160792 scopus 로고
    • Studies on limit dextrinase in barley. I. Purification of malt limit dextrinase and production of monospecific antibodies
    • Sissons MJ, Lance RCM, Sparrow DHB (1992) Studies on limit dextrinase in barley. I. Purification of malt limit dextrinase and production of monospecific antibodies. J Cereal Sci 16: 107-116
    • (1992) J Cereal Sci , vol.16 , pp. 107-116
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 51
    • 0010980673 scopus 로고
    • Studies on limit dextrinase in barley. 3. Limit dextrinase in developing kernels
    • Sissons MJ, Lance RCM, Sparrow DHB (1993) Studies on limit dextrinase in barley. 3. Limit dextrinase in developing kernels. J Cereal Sci 17: 19-24
    • (1993) J Cereal Sci , vol.17 , pp. 19-24
    • Sissons, M.J.1    Lance, R.C.M.2    Sparrow, D.H.B.3
  • 52
    • 0025649961 scopus 로고
    • Structure and tissue-specific regulation of genes encoding barley (1-→3,1→4)-β-glucan endohydrolases
    • Slakeski N, Baulcombe DC, Devos KM, Doan DNF, Fincher GB (1990) Structure and tissue-specific regulation of genes encoding barley (1-→3,1→4)-β-glucan endohydrolases. Mol Gen Genet 224: 437-449
    • (1990) Mol Gen Genet , vol.224 , pp. 437-449
    • Slakeski, N.1    Baulcombe, D.C.2    Devos, K.M.3    Doan, D.N.F.4    Fincher, G.B.5
  • 53
    • 84971030199 scopus 로고
    • Observations on the scutellum. II. Histochemistry and autofluorescence of the cell wall in mature grain and during germination of wheat, barley, oats and ryegrass
    • Smart MG, O'Brien TP (1973) Observations on the scutellum. II. Histochemistry and autofluorescence of the cell wall in mature grain and during germination of wheat, barley, oats and ryegrass. Aust J Bot 27: 403-411
    • (1973) Aust J Bot , vol.27 , pp. 403-411
    • Smart, M.G.1    O'Brien, T.P.2
  • 54
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heijne G, Steppuhn J, Herrmann RG (1989) Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535-545
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 55
    • 0030448481 scopus 로고    scopus 로고
    • Apoptosis in barley aleurone during germination and its inhibition by abscisic acid
    • Wang M, Oppedijk BJ, Lu X, Duijn BV, Schilperoort RA (1996) Apoptosis in barley aleurone during germination and its inhibition by abscisic acid. Plant Mol Biol 32: 1125-1134
    • (1996) Plant Mol Biol , vol.32 , pp. 1125-1134
    • Wang, M.1    Oppedijk, B.J.2    Lu, X.3    Duijn, B.V.4    Schilperoort, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.