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Volumn 130, Issue 3, 2002, Pages 1464-1475

Characterization of the genes encoding the cytosolic and plastidial forms of ADP-glucose pyrophosphorylase in wheat endosperm

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; ENZYMES; GENES; GLUCOSE; MOLECULAR BIOLOGY; TISSUE;

EID: 0036852074     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.010363     Document Type: Article
Times cited : (97)

References (38)
  • 1
    • 0028871062 scopus 로고
    • Adenosine diphosphate glucose pyrophosphorylase genes in wheat: Differential expression and gene mapping
    • Ainsworth C, Hosein F, Tarvis M, Weir F, Burrell M, Devos KM, Gale MD (1995) Adenosine diphosphate glucose pyrophosphorylase genes in wheat: Differential expression and gene mapping. Planta 197: 1-10
    • (1995) Planta , vol.197 , pp. 1-10
    • Ainsworth, C.1    Hosein, F.2    Tarvis, M.3    Weir, F.4    Burrell, M.5    Devos, K.M.6    Gale, M.D.7
  • 2
    • 0027673057 scopus 로고
    • Isolation and analysis of a cDNA clone encoding the small subunit of ADP-glucose pyrophosphorylase from wheat
    • Ainsworth C, Tarvis M, Clark J (1993) Isolation and analysis of a cDNA clone encoding the small subunit of ADP-glucose pyrophosphorylase from wheat. Plant Mol Biol 23: 23-33
    • (1993) Plant Mol Biol , vol.23 , pp. 23-33
    • Ainsworth, C.1    Tarvis, M.2    Clark, J.3
  • 3
    • 0035109466 scopus 로고    scopus 로고
    • A cytosolic ADP-glucose pyrophosphorylase is a feature of Graminaceous endosperms, bur not of other starch-storing organs
    • Beckles DM, Smith AM, ap Rees T (2001) A cytosolic ADP-glucose pyrophosphorylase is a feature of Graminaceous endosperms, bur not of other starch-storing organs. Plant Physiol 125: 818-827
    • (2001) Plant Physiol , vol.125 , pp. 818-827
    • Beckles, D.M.1    Smith, A.M.2    Ap Rees, T.3
  • 4
    • 0025443897 scopus 로고
    • Identification and molecular characterization of Shrunken-2 cDNA clones of maize
    • Bhave MR, Lawrence S, Barton C, Hannah LC (1990) Identification and molecular characterization of Shrunken-2 cDNA clones of maize. Plant Cell 2: 581-588
    • (1990) Plant Cell , vol.2 , pp. 581-588
    • Bhave, M.R.1    Lawrence, S.2    Barton, C.3    Hannah, L.C.4
  • 5
    • 0033102225 scopus 로고    scopus 로고
    • A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley
    • Burton RA, Zhang X-Q, Hrmova M, Fincher GB (1999) A single limit dextrinase gene is expressed both in the developing endosperm and in germinated grains of barley. Plant Physiol 119: 859-872
    • (1999) Plant Physiol , vol.119 , pp. 859-872
    • Burton, R.A.1    Zhang, X.-Q.2    Hrmova, M.3    Fincher, G.B.4
  • 8
    • 0031422395 scopus 로고    scopus 로고
    • Two isoforms of the GBSSI class of granule-bound starch synthase are differentially expressed in the pea plant (Pisum sativum L)
    • Denyer K, Barber LM, Edwards EA, Smith AM, Wang TL (1997) Two isoforms of the GBSSI class of granule-bound starch synthase are differentially expressed in the pea plant (Pisum sativum L). Plant Cell Environ 20: 1566-1572
    • (1997) Plant Cell Environ , vol.20 , pp. 1566-1572
    • Denyer, K.1    Barber, L.M.2    Edwards, E.A.3    Smith, A.M.4    Wang, T.L.5
  • 9
    • 0030267532 scopus 로고    scopus 로고
    • The major form of ADP-glucose pyrophosphorylase in maize endosperm is extraplastidial
    • Denyer K, Dunlap F, Thorbjørnsen T, Keeling P, Smith AM (1996) The major form of ADP-glucose pyrophosphorylase in maize endosperm is extraplastidial. Plant Physiol 112: 779-785
    • (1996) Plant Physiol , vol.112 , pp. 779-785
    • Denyer, K.1    Dunlap, F.2    Thorbjørnsen, T.3    Keeling, P.4    Smith, A.M.5
  • 10
    • 0001252147 scopus 로고
    • The capacity of plastids from developing pea cotyledons to synthesize acetyl CoA
    • Denyer K, Smith AM (1988) The capacity of plastids from developing pea cotyledons to synthesize acetyl CoA. Planta 173: 172-182
    • (1988) Planta , vol.173 , pp. 172-182
    • Denyer, K.1    Smith, A.M.2
  • 11
    • 0001574803 scopus 로고
    • Presence of ADP-glucose pyrophosphorylase in Shrunken-2 and Brittle-2 mutants of maize endosperm
    • Dickinson DB, Preiss J (1969) Presence of ADP-glucose pyrophosphorylase in Shrunken-2 and Brittle-2 mutants of maize endosperm. Plant Physiol 44: 1058-1062
    • (1969) Plant Physiol , vol.44 , pp. 1058-1062
    • Dickinson, D.B.1    Preiss, J.2
  • 12
    • 0032711802 scopus 로고    scopus 로고
    • The allosterically unregulated isoform of ADP-glucose pyrophosphorylase from barley endosperm is the most likely source of ADP-glucose incorporated into endosperm starch
    • Doan DNP, Rudi H, Olsen O-A (1999) The allosterically unregulated isoform of ADP-glucose pyrophosphorylase from barley endosperm is the most likely source of ADP-glucose incorporated into endosperm starch. Plant Physiol 121: 965-975
    • (1999) Plant Physiol , vol.121 , pp. 965-975
    • Doan, D.N.P.1    Rudi, H.2    Olsen, O.-A.3
  • 13
    • 0030890330 scopus 로고    scopus 로고
    • Molecular cloning and expression of the large subunit of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves
    • Eimert K, Luo C, Déjardin A, Villand P, Thorbjørnsen T, Kleczkowski LA (1997) Molecular cloning and expression of the large subunit of ADP-glucose pyrophosphorylase from barley (Hordeum vulgare) leaves. Gene 189: 79-82
    • (1997) Gene , vol.189 , pp. 79-82
    • Eimert, K.1    Luo, C.2    Déjardin, A.3    Villand, P.4    Thorbjørnsen, T.5    Kleczkowski, L.A.6
  • 14
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O, Nielsen H, von Heijne G (1999) ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci 8: 978-984
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 15
    • 0032566715 scopus 로고    scopus 로고
    • Mechanism of reductive activation of potato tuber ADP-glucose pyrophosphorylase
    • Fu YB, Ballicora MA, Leykam JF, Preiss J (1998) Mechanism of reductive activation of potato tuber ADP-glucose pyrophosphorylase. J Biol Chem 273: 25045-25052
    • (1998) J Biol Chem , vol.273 , pp. 25045-25052
    • Fu, Y.B.1    Ballicora, M.A.2    Leykam, J.F.3    Preiss, J.4
  • 16
    • 0028342598 scopus 로고
    • ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of maize
    • Giroux MJ, Hannah LC (1994) ADP-glucose pyrophosphorylase in shrunken-2 and brittle-2 mutants of maize. Mol Gen Genet 243: 400-408
    • (1994) Mol Gen Genet , vol.243 , pp. 400-408
    • Giroux, M.J.1    Hannah, L.C.2
  • 17
    • 0029336841 scopus 로고
    • The large subunit of the embryo isoform of ADP glucose pyrophosphorylase from maize
    • Giroux MJ, Smith-White B, Gilmore V, Hannah LC, Preiss J (1995) The large subunit of the embryo isoform of ADP glucose pyrophosphorylase from maize. Plant Physiol 108: 1333-1334
    • (1995) Plant Physiol , vol.108 , pp. 1333-1334
    • Giroux, M.J.1    Smith-White, B.2    Gilmore, V.3    Hannah, L.C.4    Preiss, J.5
  • 18
    • 0036941364 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase from wheat endosperm: Purification and characterization of an enzyme with novel regulatory properties
    • Gómez-Casati DF, Iglesias AA (2002) ADP-glucose pyrophosphorylase from wheat endosperm: Purification and characterization of an enzyme with novel regulatory properties. Planta 214: 428-434
    • (2002) Planta , vol.214 , pp. 428-434
    • Gómez-Casati, D.F.1    Iglesias, A.A.2
  • 19
    • 0000600497 scopus 로고
    • Alkaline inorganic pyrophosphatase and starch synthesis in amyloplasts
    • Gross P, ap Rees T (1986) Alkaline inorganic pyrophosphatase and starch synthesis in amyloplasts. Planta 167: 140-145
    • (1986) Planta , vol.167 , pp. 140-145
    • Gross, P.1    Ap Rees, T.2
  • 21
    • 0027951459 scopus 로고
    • Caution on the use of the generally accepted methanol precipitation technique for the assay of soluble starch synthase in crude extracts of plant tissues
    • Jenner CF, Denyer K, Hawker JS (1994) Caution on the use of the generally accepted methanol precipitation technique for the assay of soluble starch synthase in crude extracts of plant tissues. Aust J Plant Physiol 21: 17-22
    • (1994) Aust J Plant Physiol , vol.21 , pp. 17-22
    • Jenner, C.F.1    Denyer, K.2    Hawker, J.S.3
  • 22
    • 84931272246 scopus 로고
    • Multiple forms of ADPglucose pyrophosphorylase of rice endosperm
    • Nakamura Y, Kawaguchi K (1992) Multiple forms of ADPglucose pyrophosphorylase of rice endosperm. Physiol Plant 84: 336-342
    • (1992) Physiol Plant , vol.84 , pp. 336-342
    • Nakamura, Y.1    Kawaguchi, K.2
  • 23
    • 0001608011 scopus 로고
    • Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm
    • Olive MR, Ellis RJ, Schuch WW (1989) Isolation and nucleotide sequences of cDNA clones encoding ADP-glucose pyrophosphorylase polypeptides from wheat leaf and endosperm. Plant Mol Biol 12: 525-538
    • (1989) Plant Mol Biol , vol.12 , pp. 525-538
    • Olive, M.R.1    Ellis, R.J.2    Schuch, W.W.3
  • 25
    • 0000388198 scopus 로고
    • Purification and properties of nonproteolytically degraded ADPglucose pyrophosphorylase from maize endosperm
    • Plaxton WC, Preiss J (1987) Purification and properties of nonproteolytically degraded ADPglucose pyrophosphorylase from maize endosperm. Plant Physiol 83: 105-112
    • (1987) Plant Physiol , vol.83 , pp. 105-112
    • Plaxton, W.C.1    Preiss, J.2
  • 26
    • 0002998420 scopus 로고
    • Biology and molecular biology of starch synthesis and its regulation
    • Preiss J (1991) Biology and molecular biology of starch synthesis and its regulation. Oxford Surveys Plant Mol Cell Biol 7: 59-114
    • (1991) Oxford Surveys Plant Mol Cell Biol , vol.7 , pp. 59-114
    • Preiss, J.1
  • 28
    • 0030028267 scopus 로고    scopus 로고
    • Nucleotides and nucleotide sugars in developing maize endosperms
    • Shannon JC, Pien F-M, Liu K-C (1996) Nucleotides and nucleotide sugars in developing maize endosperms. Plant Physiol 110: 835-843
    • (1996) Plant Physiol , vol.110 , pp. 835-843
    • Shannon, J.C.1    Pien, F.-M.2    Liu, K.-C.3
  • 29
    • 0034879793 scopus 로고    scopus 로고
    • Subcellular compartmentation and allosteric regulation of the rice endosperm ADPglucose pyrophosphorylase
    • Sikka VK, Choi S-B, Kavakli H, Sakulsingharoj C, Gupta S, Ito H, Okita TW (2001) Subcellular compartmentation and allosteric regulation of the rice endosperm ADPglucose pyrophosphorylase. Plant Sci 161: 461-468
    • (2001) Plant Sci , vol.161 , pp. 461-468
    • Sikka, V.K.1    Choi, S.-B.2    Kavakli, H.3    Sakulsingharoj, C.4    Gupta, S.5    Ito, H.6    Okita, T.W.7
  • 30
    • 0001366025 scopus 로고
    • Evidence that the rb locus alters the starch content of developing pea embryos through an effect on ADP glucose pyrophosphorylase
    • Smith AM, Bettey M, Bedford ID (1989) Evidence that the rb locus alters the starch content of developing pea embryos through an effect on ADP glucose pyrophosphorylase. Plant Physiol 89: 1279-1284
    • (1989) Plant Physiol , vol.89 , pp. 1279-1284
    • Smith, A.M.1    Bettey, M.2    Bedford, I.D.3
  • 31
    • 0026767213 scopus 로고
    • Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources
    • Smith-White BJ, Preiss J (1992) Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources. J Mol Evol 34: 449-464
    • (1992) J Mol Evol , vol.34 , pp. 449-464
    • Smith-White, B.J.1    Preiss, J.2
  • 32
    • 0002844767 scopus 로고    scopus 로고
    • Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies
    • Speicher KD (2000) Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies. J Biomol Technol 11: 74-86
    • (2000) J Biomol Technol , vol.11 , pp. 74-86
    • Speicher, K.D.1
  • 33
    • 0000633840 scopus 로고
    • A rapid method for the isolation of purified amyloplasts from wheat endosperm
    • Tetlow IJ, Blissett KJ, Emes MJ (1993) A rapid method for the isolation of purified amyloplasts from wheat endosperm. Planta 189: 597-600
    • (1993) Planta , vol.189 , pp. 597-600
    • Tetlow, I.J.1    Blissett, K.J.2    Emes, M.J.3
  • 34
    • 0030483916 scopus 로고    scopus 로고
    • Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm
    • Thorbjørnsen T, Villand P, Denyer K, Olsen O-A, Smith AM (1996a) Distinct isoforms of ADPglucose pyrophosphorylase occur inside and outside the amyloplasts in barley endosperm. Plant J 10: 243-250
    • (1996) Plant J , vol.10 , pp. 243-250
    • Thorbjørnsen, T.1    Villand, P.2    Denyer, K.3    Olsen, O.-A.4    Smith, A.M.5
  • 35
    • 0030062188 scopus 로고    scopus 로고
    • A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare)
    • Thorbjørnsen T, Villand P, Kleczkowski LA, Olsen OA (1996b) A single gene encodes two different transcripts for the ADP-glucose pyrophosphorylase small subunit from barley (Hordeum vulgare). Biochem J 313: 149-154
    • (1996) Biochem J , vol.313 , pp. 149-154
    • Thorbjørnsen, T.1    Villand, P.2    Kleczkowski, L.A.3    Olsen, O.A.4
  • 36
    • 0014023725 scopus 로고
    • Starch-deficient maize mutants lacking adenosine diphosphate glucose pyrophosphorylase activity
    • Tsai CY, Nelson OE (1966) Starch-deficient maize mutants lacking adenosine diphosphate glucose pyrophosphorylase activity. Science 151: 341-343
    • (1966) Science , vol.151 , pp. 341-343
    • Tsai, C.Y.1    Nelson, O.E.2
  • 37
    • 0026875704 scopus 로고
    • PCR amplification and sequences of cDNA clones for the small and large subunits of ADP-glucose pyrophosphorylase from barley tissues
    • Villand P, Aalen R, Olsen OA, Lüthi E, Lonneborg A, Kleczkowski LA (1992) PCR amplification and sequences of cDNA clones for the small and large subunits of ADP-glucose pyrophosphorylase from barley tissues. Plant Mol Biol 19: 381-389
    • (1992) Plant Mol Biol , vol.19 , pp. 381-389
    • Villand, P.1    Aalen, R.2    Olsen, O.A.3    Lüthi, E.4    Lonneborg, A.5    Kleczkowski, L.A.6
  • 38
    • 0033782945 scopus 로고    scopus 로고
    • Protein import: The hitchhikers guide into chloroplasts
    • Vothknecht UC, Soll J (2000) Protein import: The hitchhikers guide into chloroplasts. Biol Chem 381: 887-897
    • (2000) Biol Chem , vol.381 , pp. 887-897
    • Vothknecht, U.C.1    Soll, J.2


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