메뉴 건너뛰기




Volumn 55, Issue 2, 2014, Pages 320-332

Nucleotide pyrophosphatase/phosphodiesterase 1 exerts a negative effect on starch accumulation and growth in rice seedlings under high temperature and CO2 concentration conditions

Author keywords

ADP glucose; CO2; NPP; Oryza sativa; Plastid; Starch

Indexed keywords

ADENOSINE DIPHOSPHATE GLUCOSE; CARBON DIOXIDE; COMPLEMENTARY DNA; INORGANIC PYROPHOSPHATASE; NUCLEOTIDE PYROPHOSPHATASE; PHOSPHODIESTERASE; STARCH; VEGETABLE PROTEIN;

EID: 84893874363     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pct139     Document Type: Article
Times cited : (18)

References (75)
  • 3
    • 84862907757 scopus 로고    scopus 로고
    • Sucrose synthase activity in the sus1/ sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production
    • Baroja-Fernández, E., Muñoz, F.J., Li, J., Bahaji, A., Almagro, G., Montero, M. et al. (2012) Sucrose synthase activity in the sus1/ sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production. Proc. Natl Acad. Sci. USA 109: 321-326
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 321-326
    • Baroja-Fernández, E.1    Muñoz, F.J.2    Li, J.3    Bahaji, A.4    Almagro, G.5    Montero, M.6
  • 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, M.M. (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
    • 79959909340 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation in plants
    • Briggs, A.G. and Bent, A.F. (2011) Poly(ADP-ribosyl)ation in plants. Trends Plant Sci. 16: 372-380
    • (2011) Trends Plant Sci , vol.16 , pp. 372-380
    • Briggs, A.G.1    Bent, A.F.2
  • 9
    • 79958744741 scopus 로고    scopus 로고
    • Importance of post-translational modifications for functionality of a chloroplastlocalized carbonic anhydrase (CAH1) in Arabidopsis thaliana
    • Burén, S., Ortega-Villasante, C., Blanco-Rivero, A., Martínez- Bernardini, A., Shutova, T., Shevela, D. et al. (2011) Importance of post-translational modifications for functionality of a chloroplastlocalized carbonic anhydrase (CAH1) in Arabidopsis thaliana. PLoS One 6: 1-15
    • (2011) PLoS One , vol.6 , pp. 1-15
    • Burén, S.1    Ortega-Villasante, C.2    Blanco-Rivero, A.3    Martínez-Bernardini, A.4    Shutova, T.5    Shevela, D.6
  • 10
    • 78650978686 scopus 로고    scopus 로고
    • Update on mechanisms of plant cell wall biosyn thesis: How plants make cellulose and other (1!4)-b-D-glycans
    • Carpita, N.C. (2011) Update on mechanisms of plant cell wall biosynthesis: How plants make cellulose and other (1!4)-b-D-glycans. Plant Physiol. 155: 171-184
    • (2011) Plant Physiol , vol.155 , pp. 171-184
    • Carpita, N.C.1
  • 11
    • 0002135275 scopus 로고
    • Alterations in growth, photosyn thesis, and respiration in a starchless mutant of Arabidopsis thaliana L) deficient in chloroplast phosphoglucomutase activity
    • Caspar, T., Huber, S.C. and Somerville, C. (1985) Alterations in growth, photosynthesis, and respiration in a starchless mutant of Arabidopsis thaliana (L.) deficient in chloroplast phosphoglucomutase activity. Plant Physiol. 79: 11-17
    • (1985) Plant Physiol , vol.79 , pp. 11-17
    • Caspar, T.1    Huber, S.C.2    Somerville, C.3
  • 12
    • 3543041300 scopus 로고    scopus 로고
    • Signal peptide-dependent targeting of a rice a-amylase and cargo proteins to plastids and extracellular compartments of plant cells
    • Chen, M.H., Huang, L.F., Li, H.M., Chen, Y.R. and Yu, S.M. (2004) Signal peptide-dependent targeting of a rice a-amylase and cargo proteins to plastids and extracellular compartments of plant cells. Plant Physiol. 135: 1367-1377
    • (2004) Plant Physiol , vol.135 , pp. 1367-1377
    • Chen, M.H.1    Huang, L.F.2    Li, H.M.3    Chen, Y.R.4    Yu, S.M.5
  • 13
    • 0028180895 scopus 로고
    • Expression of a-amylase, carbohydrate metabolism, and autophagy in cultured rice cells is coordinately regulated by sugar nutrient
    • Chen, M.H., Liu, L.F., Chen, Y.R., Wu, H.K. and Yu, S.M. (1994) Expression of a-amylase, carbohydrate metabolism, and autophagy in cultured rice cells is coordinately regulated by sugar nutrient. Plant J. 6: 625-636
    • (1994) Plant J. , vol.6 , pp. 625-636
    • Chen, M.H.1    Liu, L.F.2    Chen, Y.R.3    Wu, H.K.4    Yu, S.M.5
  • 14
    • 0026816010 scopus 로고
    • Maize polyubiquitin genes: Structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer to protoplasts by electroporation
    • Christensen, A.H., Sharrock, R.A. and Quail, P.H. (1992) Maize polyubiquitin genes: Structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer to protoplasts by electroporation. Plant Mol. Biol. 18: 675-689
    • (1992) Plant Mol. Biol , vol.18 , pp. 675-689
    • Christensen, A.H.1    Sharrock, R.A.2    Quail, P.H.3
  • 15
    • 33645302617 scopus 로고    scopus 로고
    • Upregulation of sucrose synthase and UDP-glucose pyrophosphorylase impacts plant growth and metabolism
    • Coleman, H.D., Ellis, D.D., Gilbert, M. and Mansfield, S.D. (2006) Upregulation of sucrose synthase and UDP-glucose pyrophosphorylase impacts plant growth and metabolism. Plant Biotechnol. J. 4: 87-101
    • (2006) Plant Biotechnol. J. , vol.4 , pp. 87-101
    • Coleman, H.D.1    Ellis, D.D.2    Gilbert, M.3    Mansfield, S.D.4
  • 16
    • 69149094770 scopus 로고    scopus 로고
    • Sucrose synthase affects carbon partitioning to increase cellulose production and altered cell wall ultrastructure
    • Coleman, H.D., Yan, J. and Mansfield, S.D. (2009) Sucrose synthase affects carbon partitioning to increase cellulose production and altered cell wall ultrastructure. Proc. Natl Acad. Sci. USA 106: 13118-13123
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13118-13123
    • Coleman, H.D.1    Yan, J.2    Mansfield, S.D.3
  • 17
    • 0038063019 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of cytosolic phosphoglucomutase in wheat endosperm (triticum aestivum L cv axona
    • Davies, E.J., Tetlow, I.J., Bowsher, C.G. and Emes, M.J. (2003) Molecular and biochemical characterization of cytosolic phosphoglucomutase in wheat endosperm (Triticum aestivum L. cv. Axona). J. Exp. Bot. 386: 1351-1360
    • (2003) J. Exp. Bot , vol.386 , pp. 1351-1360
    • Davies, E.J.1    Tetlow, I.J.2    Bowsher, C.G.3    Emes, M.J.4
  • 18
    • 0028874114 scopus 로고
    • The contributions of ADP-glucose pyrophosphorylase and starch-branching enzyme to the control of starch synthesis in developing pea embryos
    • Denyer, K., Foster, J. and Smith, A.M. (1995) The contributions of ADP-glucose pyrophosphorylase and starch-branching enzyme to the control of starch synthesis in developing pea embryos. Planta 197: 57-62
    • (1995) Planta , vol.197 , pp. 57-62
    • Denyer, K.1    Foster, J.2    Smith, A.M.3
  • 19
    • 0033559677 scopus 로고    scopus 로고
    • The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization
    • Durmus, A., Eicken, C., Sift, B.H., Kratel, A., Kappl, R., Huttermann, J. and Krebs, B. (1999) The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization. Eur. J. Biochem. 260: 709-716
    • (1999) Eur. J. Biochem , vol.260 , pp. 709-716
    • Durmus, A.1    Eicken, C.2    Sift, B.H.3    Kratel, A.4    Kappl, R.5    Huttermann, J.6    Krebs, B.7
  • 20
    • 0033304931 scopus 로고    scopus 로고
    • A soluble PC-1 circulates in human plasma: Relationship with insulin resistance and associated abnormalities
    • Frittitta, L., Camastra, S., Baratta, R., Costanzo, B.V., D'adamo, M., Graci, S. et al. (1999) A soluble PC-1 circulates in human plasma: Relationship with insulin resistance and associated abnormalities. J. Clin. Endocrinol. Metab. 84: 3620-3625
    • (1999) J. Clin. Endocrinol. Metab , vol.84 , pp. 3620-3625
    • Frittitta, L.1    Camastra, S.2    Baratta, R.3    Costanzo, B.V.4    D'adamo, M.5    Graci, S.6
  • 21
    • 4944227719 scopus 로고    scopus 로고
    • Adjustment of diurnal starch turnover to short days: Depletion of sugar during the night leads to a temporary inhibition of carbohydrate utilization, accumulation of sugars and post-translational activation of ADP-glucose pyrophosphorylase in the following light period
    • Gibon, Y., Bläsing, O.E., Palacios-Rojas, N., Pankovic, D., Hendriks, J.H.M., Fishan, J. et al. (2004) Adjustment of diurnal starch turnover to short days: Depletion of sugar during the night leads to a temporary inhibition of carbohydrate utilization, accumulation of sugars and post-translational activation of ADP-glucose pyrophosphorylase in the following light period. Plant J. 39: 847-62
    • (2004) Plant J. , vol.39 , pp. 847-62
    • Gibon, Y.1    Bläsing, O.E.2    Palacios-Rojas, N.3    Pankovic, D.4    Hendriks, J.H.M.5    Fishan, J.6
  • 22
    • 0035847049 scopus 로고    scopus 로고
    • Structural and catalytic similarities between nucleotide pyrophosphatases/ phosphodiesterases and alkaline phosphatases
    • Gijsbers, R., Ceulemans, H., Stalmans, W. and Bollen, W. (2001) Structural and catalytic similarities between nucleotide pyrophosphatases/ phosphodiesterases and alkaline phosphatases. J. Biol. Chem. 276: 1361-1368
    • (2001) J. Biol. Chem , vol.276 , pp. 1361-1368
    • Gijsbers, R.1    Ceulemans, H.2    Stalmans, W.3    Bollen, W.4
  • 23
    • 0031885056 scopus 로고    scopus 로고
    • Ecto-phosphodiesterase/pyrophosphatase of lymphocytes and non-lymphoid cells: Structure and function of the PC-1 family
    • Goding, J.W., Terkeltaub, R., Maurice, M., Deterre, P., Sali, A. and Belli, S.I. (1998) Ecto-phosphodiesterase/pyrophosphatase of lymphocytes and non-lymphoid cells: Structure and function of the PC-1 family. Immunol. Res. 161: 11-26
    • (1998) Immunol. Res , vol.161 , pp. 11-26
    • Goding, J.W.1    Terkeltaub, R.2    Maurice, M.3    Deterre, P.4    Sali, A.5    Belli, S.I.6
  • 25
    • 0021845192 scopus 로고
    • Formation of lipid-linked oligosaccharides by MOPC 315 plasmacytoma cells
    • Hickman, S., Wong-Yip, Y.P., Rebbe, N.F. and Greco, J.M. (1985) Formation of lipid-linked oligosaccharides by MOPC 315 plasmacytoma cells. J. Biol. Chem. 260: 6098-6106
    • (1985) J. Biol. Chem , vol.260 , pp. 6098-6106
    • Hickman, S.1    Wong-Yip, Y.P.2    Rebbe, N.F.3    Greco, J.M.4
  • 26
    • 0028483231 scopus 로고
    • Efficient transformation of rice (oryza sativa L) mediated by agrobacterium and sequence analysis of the boundaries of the T-DNA
    • Hiei, Y., Ohta, S., Komari, T. and Kumashiro, T. (1994) Efficient transformation of rice (Oryza sativa L.) mediated by Agrobacterium and sequence analysis of the boundaries of the T-DNA. Plant J. 6: 271-282
    • (1994) Plant J. , vol.6 , pp. 271-282
    • Hiei, Y.1    Ohta, S.2    Komari, T.3    Kumashiro, T.4
  • 27
    • 0022917028 scopus 로고
    • The hypervirulence of Agrobacterium tumefaciens A281 is encoded in a region of pTiBo542 outsiDe of T-DNA
    • Hood, E.E., Helmer, G.L., Fraley, R.T. and Chilton, M.D. (1986) The hypervirulence of Agrobacterium tumefaciens A281 is encoded in a region of pTiBo542 outsiDe of T-DNA. J. Bacteriol. 168: 1291-1301
    • (1986) J. Bacteriol , vol.168 , pp. 1291-1301
    • Hood, E.E.1    Helmer, G.L.2    Fraley, R.T.3    Chilton, M.D.4
  • 28
    • 70349650810 scopus 로고    scopus 로고
    • Modulation of the poly(ADP-ribosyl)ation reaction via the arabidopsis adp-ribose/nadh pyrophosphohydrolase, atnudx7, is involved in the response to oxidative stress
    • Ishikawa, K., Ogawa, T., Hirosue, E., Nakayama, Y., Harada, K., Fukusaki, E. et al. (2009) Modulation of the poly(ADP-ribosyl)ation reaction via the Arabidopsis ADP-ribose/NADH pyrophosphohydrolase, AtNUDX7, is involved in the response to oxidative stress. Plant Physiol. 151: 741-754
    • (2009) Plant Physiol , vol.151 , pp. 741-754
    • Ishikawa, K.1    Ogawa, T.2    Hirosue, E.3    Nakayama, Y.4    Harada, K.5    Fukusaki, E.6
  • 30
    • 0037403609 scopus 로고    scopus 로고
    • Effect of high temperature on fine structure of amylopectin in rice endosperm by reducing the activity of the starch branching enzyme
    • Jiang, H., Dian, W. and Wu, P. (2003) Effect of high temperature on fine structure of amylopectin in rice endosperm by reducing the activity of the starch branching enzyme. Phytochemistry 63: 53-59
    • (2003) Phytochemistry , vol.63 , pp. 53-59
    • Jiang, H.1    Dian, W.2    Wu, P.3
  • 31
    • 56949108503 scopus 로고    scopus 로고
    • Purple acid phosphatase in the wall of tobacco cells
    • Kaida, R., Hayashi, T. and Kaneko, T.S. (2008) Purple acid phosphatase in the wall of tobacco cells. Phytochemistry 69: 2546-2551
    • (2008) Phytochemistry , vol.69 , pp. 2546-2551
    • Kaida, R.1    Hayashi, T.2    Kaneko, T.S.3
  • 32
    • 79955130077 scopus 로고    scopus 로고
    • Differential localizations and functions of rice nucleotide pyrophosphatase/phosphodiesterase isozymes 1 and 3
    • Kaneko, K., Yamada, C., Yanagida, A., Koshu, T., Umezawa, Y., Itoh, K. et al. (2011) Differential localizations and functions of rice nucleotide pyrophosphatase/phosphodiesterase isozymes 1 and 3. Plant Biotechnol. 28: 69-76
    • (2011) Plant Biotechnol , vol.28 , pp. 69-76
    • Kaneko, K.1    Yamada, C.2    Yanagida, A.3    Koshu, T.4    Umezawa, Y.5    Itoh, K.6
  • 33
    • 0030456403 scopus 로고    scopus 로고
    • Reducing sugars trigger oxidative modification and apoptosis in pancreatic beta-cells by provoking oxidative stress through the glycation reaction
    • Kaneto, H., Fujii, J., Myint, T., Miyazawa, N., Islam, K.N., Kawasaki, Y. et al. (1996) Reducing sugars trigger oxidative modification and apoptosis in pancreatic beta-cells by provoking oxidative stress through the glycation reaction. Biochem. J. 320: 855-863
    • (1996) Biochem. J. , vol.320 , pp. 855-863
    • Kaneto, H.1    Fujii, J.2    Myint, T.3    Miyazawa, N.4    Islam, K.N.5    Kawasaki, Y.6
  • 34
    • 0034115517 scopus 로고    scopus 로고
    • Possible involvement of phosphoinositide-Ca2+ signaling in the regulation of a-amylase expression and germination of rice seed (oryza sativa L
    • Kashem, M.A., Itoh, K., Iwabuchi, S., Hori, H. and Mitsui, T. (2000) Possible involvement of phosphoinositide-Ca2+ signaling in the regulation of a-amylase expression and germination of rice seed (Oryza sativa L.). Plant Cell Physiol. 41: 399-407
    • (2000) Plant Cell Physiol , vol.41 , pp. 399-407
    • Kashem, M.A.1    Itoh, K.2    Iwabuchi, S.3    Hori, H.4    Mitsui, T.5
  • 35
    • 34250076038 scopus 로고
    • Elevated temperature reduces starch deposition in wheat endosperm by reducing the activity of soluble starch synthase
    • Keeling, P.L., Bacon, P.J. and Holt, D.C. (1993) Elevated temperature reduces starch deposition in wheat endosperm by reducing the activity of soluble starch synthase. Planta 191: 342-348
    • (1993) Planta , vol.191 , pp. 342-348
    • Keeling, P.L.1    Bacon, P.J.2    Holt, D.C.3
  • 36
    • 0021759103 scopus 로고
    • Anaerobic expression of maize glucose phosphate isomerase I
    • Kelley, P.M. and Freeling, M. (1984) Anaerobic expression of maize glucose phosphate isomerase I. J. Biol. Chem. 259: 673-677
    • (1984) J. Biol. Chem , vol.259 , pp. 673-677
    • Kelley, P.M.1    Freeling, M.2
  • 37
    • 0001451455 scopus 로고
    • Purification, characterization and localization of rice UDP-glucose pyrophosphorylase
    • Kimura, S., Mitsui, T., Matsuoka, T. and Igaue, I. (1992) Purification, characterization and localization of rice UDP-glucose pyrophosphorylase. Plant Physiol. Biochem. 30: 683-693
    • (1992) Plant Physiol. Biochem , vol.30 , pp. 683-693
    • Kimura, S.1    Mitsui, T.2    Matsuoka, T.3    Igaue, I.4
  • 38
    • 70949096336 scopus 로고    scopus 로고
    • The rice a-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids
    • Kitajima, A., Asatsuma, S., Okada, H., Hamada, Y., Kaneko, K., Nanjo, Y. et al. (2009) The rice a-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids. Plant Cell 21: 2844-2858
    • (2009) Plant Cell , vol.21 , pp. 2844-2858
    • Kitajima, A.1    Asatsuma, S.2    Okada, H.3    Hamada, Y.4    Kaneko, K.5    Nanjo, Y.6
  • 39
    • 0034613299 scopus 로고    scopus 로고
    • Constitutive release of ATP and evidence for major contribution of ectonucleotide pyrophosphatase and nucleosiDe diphosphokinase to extracellular nucleotiDe concentration
    • Lazarowski, E.R., Boucher, R.C. and Harden, T.K. (2000) Constitutive release of ATP and evidence for major contribution of ectonucleotide pyrophosphatase and nucleosiDe diphosphokinase to extracellular nucleotiDe concentration. J. Biol. Chem. 275: 31061-31068
    • (2000) J. Biol. Chem , vol.275 , pp. 31061-31068
    • Lazarowski, E.R.1    Boucher, R.C.2    Harden, T.K.3
  • 40
    • 0030453191 scopus 로고    scopus 로고
    • Molecular genetics of sulfate assimilation in plants
    • Leustek, T. (1996) Molecular genetics of sulfate assimilation in plants. Physiol. Plant. 97: 411-419
    • (1996) Physiol. Plant , vol.97 , pp. 411-419
    • Leustek, T.1
  • 41
    • 84863143777 scopus 로고    scopus 로고
    • Post-translational redox modification of ADP-glucose pyrophosphorylase in response to light is not a major determinant of fine regulation of transitory starch accumulation in arabidopsis leaves
    • Li, J., Almagro, G., Muñoz, F.J., Baroja-Fernández, E., Bahaji, A., Montero, M. et al. (2012) Post-translational redox modification of ADP-glucose pyrophosphorylase in response to light is not a major determinant of fine regulation of transitory starch accumulation in Arabidopsis leaves. Plant Cell Physiol. 53: 433-444
    • (2012) Plant Cell Physiol , vol.53 , pp. 433-444
    • Li, J.1    Almagro, G.2    Muñoz, F.J.3    Baroja-Fernández, E.4    Bahaji, A.5    Montero, M.6
  • 42
    • 84874274976 scopus 로고    scopus 로고
    • Enhancing sucrose synthase activity results in increased levels of starch and ADP-glucose in maize (Zea mays L) seed endosperms
    • Li, J., Baroja-Fernández, E., Bahaji, A., Muñoz, F.J., Ovecka, M., Montero, M. et al. (2013) Enhancing sucrose synthase activity results in increased levels of starch and ADP-glucose in maize (Zea mays L) seed endosperms. Plant Cell Physiol. 54: 282-294
    • (2013) Plant Cell Physiol , vol.54 , pp. 282-294
    • Li, J.1    Baroja-Fernández, E.2    Bahaji, A.3    Muñoz, F.J.4    Ovecka, M.5    Montero, M.6
  • 43
    • 0001117527 scopus 로고
    • Isolation and characterization of a starchless mutant of Arabidopsis thaliana L) heynh lacking adpglucose pyrophosphorylase activity
    • Lin, T-P., Caspar, T., Somerville, C.R. and Preiss, J. (1988) Isolation and characterization of a starchless mutant of Arabidopsis thaliana (L.) Heynh lacking ADPglucose pyrophosphorylase activity. Plant Physiol. 86: 1131-1135
    • (1988) Plant Physiol , vol.86 , pp. 1131-1135
    • Lin, T.-P.1    Caspar, T.2    Somerville, C.R.3    Preiss, J.4
  • 44
    • 77951072181 scopus 로고    scopus 로고
    • Metabolomic analysis via reversedphase ion-pairing liquid chromatography coupled to a stand alone orbitrap mass spectrometer
    • Lu, W., Clasquin, M.F., Melamud, E., Amador-Noguez, D., Caudy, A.A. and Rabinowitz, J.D. (2010) Metabolomic analysis via reversedphase ion-pairing liquid chromatography coupled to a stand alone orbitrap mass spectrometer. Anal. Chem. 82: 3212-3221
    • (2010) Anal. Chem , vol.82 , pp. 3212-3221
    • Lu, W.1    Clasquin, M.F.2    Melamud, E.3    Amador-Noguez, D.4    Caudy, A.A.5    Rabinowitz, J.D.6
  • 45
    • 70149098891 scopus 로고    scopus 로고
    • Gene nomenclature system for rice
    • McCouch, S.R. (2008) Gene nomenclature system for rice. Rice 1: 72-84
    • (2008) Rice , vol.1 , pp. 72-84
    • McCouch, S.R.1
  • 46
    • 30744470374 scopus 로고    scopus 로고
    • The nudix hydrolase superfamily
    • McLennan, A.G. (2006) The Nudix hydrolase superfamily. Cell. Mol. Life Sci. 63: 123-143
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 123-143
    • McLennan, A.G.1
  • 48
    • 2342577446 scopus 로고    scopus 로고
    • Simple RNAi vectors for stable and transient suppression of gene function in rice
    • Miki, D. and Shimamoto, K. (2004) Simple RNAi vectors for stable and transient suppression of gene function in rice. Plant Cell Physiol. 45: 490-495
    • (2004) Plant Cell Physiol , vol.45 , pp. 490-495
    • Miki, D.1    Shimamoto, K.2
  • 49
    • 0030113407 scopus 로고    scopus 로고
    • Physicochemical and serological characterization of rice a-amylase isoforms and identification of their corresponding genes
    • Mitsui, T., Yamaguchi, J. and Akazawa, T. (1996) Physicochemical and serological characterization of rice a-amylase isoforms and identification of their corresponding genes. Plant Physiol. 110: 1395-1404
    • (1996) Plant Physiol , vol.110 , pp. 1395-1404
    • Mitsui, T.1    Yamaguchi, J.2    Akazawa, T.3
  • 50
    • 0041419305 scopus 로고    scopus 로고
    • Target site specificity of the Tos17 retrotransposon shows a preference for insertion within genes and against insertion in retrotransposon- rich regions of the genome
    • Miyao, A., Tanaka, K., Murata, K., Sawaki, H., Takeda, S., Abe, K. et al. (2003) Target site specificity of the Tos17 retrotransposon shows a preference for insertion within genes and against insertion in retrotransposon- rich regions of the genome. Plant Cell 15: 1771-1780
    • (2003) Plant Cell , vol.15 , pp. 1771-1780
    • Miyao, A.1    Tanaka, K.2    Murata, K.3    Sawaki, H.4    Takeda, S.5    Abe, K.6
  • 51
    • 0035298435 scopus 로고    scopus 로고
    • Purification and characterization of the maize amyloplast stromal 112-kDa starch phosphorylase
    • Mu, H.H., Yu, Y., Wasserman, B.P. and Carman, G.M. (2001) Purification and characterization of the maize amyloplast stromal 112-kDa starch phosphorylase. Arch. Biochem. Biophys. 388: 155-164
    • (2001) Arch. Biochem. Biophys , vol.388 , pp. 155-164
    • Mu, H.H.1    Yu, Y.2    Wasserman, B.P.3    Carman, G.M.4
  • 53
    • 56449085510 scopus 로고    scopus 로고
    • Plastidial localization of a potato 'nudix' hydrolase of ADP-glucose linked to starch biosynthesis
    • Muñoz, F.J., Baroja-Fernández, E., Ovecka, M., Li, J., Mitsui, T., Sesma, M.T. et al. (2008) Plastidial localization of a potato 'Nudix' hydrolase of ADP-glucose linked to starch biosynthesis. Plant Cell Physiol. 49: 1734-1746
    • (2008) Plant Cell Physiol , vol.49 , pp. 1734-1746
    • Muñoz, F.J.1    Baroja-Fernández, E.2    Ovecka, M.3    Li, J.4    Mitsui, T.5    Sesma, M.T.6
  • 54
    • 0030476543 scopus 로고    scopus 로고
    • Evidence for a UDP-glucose transporter in golgi apparatus-derived vesicles from pea and its possible role in polysaccharide biosynthesis
    • Muñoz, P., Norambuena, L. and Orellana, A. (1996) Evidence for a UDP-glucose transporter in Golgi apparatus-derived vesicles from pea and its possible role in polysacchariDe biosynthesis. Plant Physiol. 112: 1585-1594
    • (1996) Plant Physiol , vol.112 , pp. 1585-1594
    • Muñoz, P.1    Norambuena, L.2    Orellana, A.3
  • 55
    • 3142640923 scopus 로고    scopus 로고
    • Posttranscriptional regulation of alpha-amylase II-4 expression by gibberellin in germinating rice seeds
    • Nanjo, Y., Asatuma, S., Itoh, K., Hori, H., Mitsui, T. and Fujisawa, Y. (2004) Posttranscriptional regulation of alpha-amylase II-4 expression by gibberellin in germinating rice seeds. Plant Physiol. Biochem. 42: 477-484
    • (2004) Plant Physiol. Biochem , vol.42 , pp. 477-484
    • Nanjo, Y.1    Asatuma, S.2    Itoh, K.3    Hori, H.4    Mitsui, T.5    Fujisawa, Y.6
  • 56
    • 33750974169 scopus 로고    scopus 로고
    • Rice plastidial N-glycosylated nucleotide pyrophosphatase/ phosphodiesterase is transported from the ER-Golgi to the chloroplast through the secretory pathway
    • Nanjo, Y., Oka, H., Ikarashi, N., Kaneko, K., Kitajima, A., Mitsui, T. et al. (2006) Rice plastidial N-glycosylated nucleotide pyrophosphatase/ phosphodiesterase is transported from the ER-Golgi to the chloroplast through the secretory pathway. Plant Cell 18: 2582-2592
    • (2006) Plant Cell , vol.18 , pp. 2582-2592
    • Nanjo, Y.1    Oka, H.2    Ikarashi, N.3    Kaneko, K.4    Kitajima, A.5    Mitsui, T.6
  • 57
    • 0034775955 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of the effect of amylose-extender mutation in rice endosperm
    • Nishi, A., Nakamura, Y., Tanaka, N. and Satoh, H. (2001) Biochemical and genetic analysis of the effect of Amylose-Extender mutation in rice endosperm. Plant Physiol. 127: 459-472
    • (2001) Plant Physiol , vol.127 , pp. 459-472
    • Nishi, A.1    Nakamura, Y.2    Tanaka, N.3    Satoh, H.4
  • 58
    • 58349114282 scopus 로고    scopus 로고
    • Overexpression of an ADP-ribose pyrophosphatase, AtNUDX2, confers enhanced tolerance to oxidative stress in arabidopsis plants
    • Ogawa, T., Ishikawa, K., Harada, K., Fukusaki, E., Yoshimura, K. and Shigeoka, S. (2009) Overexpression of an ADP-ribose pyrophosphatase, AtNUDX2, confers enhanced tolerance to oxidative stress in Arabidopsis plants. Plant J. 57: 289-301
    • (2009) Plant J. , vol.57 , pp. 289-301
    • Ogawa, T.1    Ishikawa, K.2    Harada, K.3    Fukusaki, E.4    Yoshimura, K.5    Shigeoka, S.6
  • 59
    • 70349466506 scopus 로고    scopus 로고
    • Diphosphonucleotide phosphatase/phosphodiesterase (PPD1) from yellow lupin (lupinus luteus L) contains an iron-manganese center
    • Olczak, M., Ciuraszkiewicz, J., Wójtowicz, H., Maszczak, D. and Olczak, T. (2009) Diphosphonucleotide phosphatase/phosphodiesterase (PPD1) from yellow lupin (Lupinus luteus L) contains an iron-manganese center. FEBS Lett. 583: 3280-3284
    • (2009) FEBS Lett , vol.583 , pp. 3280-3284
    • Olczak, M.1    Ciuraszkiewicz, J.2    Wójtowicz, H.3    Maszczak, D.4    Olczak, T.5
  • 60
    • 0037157181 scopus 로고    scopus 로고
    • Diphosphonucleotide phosphatase/ phosphodiesterase from yellow lupin (lupinus luteus L) belongs to a novel group of specific metallophosphatases
    • Olczak, M. and Olczak, T. (2002) Diphosphonucleotide phosphatase/ phosphodiesterase from yellow lupin (Lupinus luteus L) belongs to a novel group of specific metallophosphatases. FEBS Lett. 519: 159-163
    • (2002) FEBS Lett , vol.519 , pp. 159-163
    • Olczak, M.1    Olczak, T.2
  • 61
    • 77953607619 scopus 로고    scopus 로고
    • UDP-glucose pyrophosphorylase is rate limiting in vegetative and reproductive phases in arabidopsis thaliana
    • Park, J.I., Ishimizu, T., Suwabe, K., Sudo, K., Masuko, H., Hakozaki, H. et al. (2010) UDP-glucose pyrophosphorylase is rate limiting in vegetative and reproductive phases in Arabidopsis thaliana. Plant Cell Physiol. 51: 981-996
    • (2010) Plant Cell Physiol , vol.51 , pp. 981-996
    • Park, J.I.1    Ishimizu, T.2    Suwabe, K.3    Sudo, K.4    Masuko, H.5    Hakozaki, H.6
  • 62
    • 0027138759 scopus 로고
    • ATP sulfurylase from higher plants: Kinetic and structural characteristics of the chloroplast and cytosol enzymes from spinach leaf
    • Renosto, F., Patel, H., Martin, R.L., Thomassian, C., Zimmerman, G. and Segel, I.H. (1993) ATP sulfurylase from higher plants: Kinetic and structural characteristics of the chloroplast and cytosol enzymes from spinach leaf. Arch. Biochem. Biophys. 307: 272-285
    • (1993) Arch. Biochem. Biophys , vol.307 , pp. 272-285
    • Renosto, F.1    Patel, H.2    Martin, R.L.3    Thomassian, C.4    Zimmerman, G.5    Segel, I.H.6
  • 64
    • 0036923872 scopus 로고    scopus 로고
    • Antisense-inhibition of ADP-glucose pyrophosphorylase in Vicia narbonensis seeds increases soluble sugars and leads to higher water and nitrogen uptake
    • Rolletschek, H., Hijirezaei, M.-R., Wobus, U. and Weber, H. (2002) Antisense-inhibition of ADP-glucose pyrophosphorylase in Vicia narbonensis seeds increases soluble sugars and leads to higher water and nitrogen uptake. Planta 214: 954-964
    • (2002) Planta , vol.214 , pp. 954-964
    • Rolletschek, H.1    Hijirezaei, M.-R.2    Wobus, U.3    Weber, H.4
  • 65
    • 0035376979 scopus 로고    scopus 로고
    • A purple acid phosphatase from sweet potato contains an antiferromagnetically coupled binuclear Fe-Mn center
    • Schenk, G., Boutchard, C.L., Carrington, L.E., Noble, C.J., Moubaraki, B., Murray, K.S. et al. (2001) A purple acid phosphatase from sweet potato contains an antiferromagnetically coupled binuclear Fe-Mn center. J. Biol. Chem. 276: 19084-19088
    • (2001) J. Biol. Chem , vol.276 , pp. 19084-19088
    • Schenk, G.1    Boutchard, C.L.2    Carrington, L.E.3    Noble, C.J.4    Moubaraki, B.5    Murray, K.S.6
  • 67
    • 0028855261 scopus 로고
    • The plant golgi apparatus: Structure, functional organization and trafficking mechanisms
    • Staehelin, L.A. and Moore, I. (1995) The plant Golgi apparatus: Structure, functional organization and trafficking mechanisms. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46: 261-288
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol , vol.46 , pp. 261-288
    • Staehelin, L.A.1    Moore, I.2
  • 68
    • 71049134362 scopus 로고    scopus 로고
    • The debate on the pathway of starch syn thesis a closer look at low-starch mutants lacking plastidial phosphoglucomutase supports the chloroplastlocalised pathway
    • Streb, S., Egli, B., Eicke, S. and Zeeman, S.C. (2009) The debate on the pathway of starch synthesis: A closer look at low-starch mutants lacking plastidial phosphoglucomutase supports the chloroplastlocalised pathway. Plant Physiol. 151: 1769-1772
    • (2009) Plant Physiol , vol.151 , pp. 1769-1772
    • Streb, S.1    Egli, B.2    Eicke, S.3    Zeeman, S.C.4
  • 69
    • 84880570732 scopus 로고    scopus 로고
    • Starch metabolism in arabidopsis
    • doi: 10.1199/tab.0160
    • Streb, S. and Zeeman, S.C. (2012) Starch metabolism in Arabidopsis. The Arabidopsis Book doi: 10.1199/tab.0160
    • (2012) Arabidopsis Book
    • Streb, S.1    Zeeman, S.C.2
  • 71
    • 28544447361 scopus 로고    scopus 로고
    • Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast
    • Villarejo, A., Burén, S., Larsson, S., Déjardin, A., Monné, M., Rudhe, C. et al. (2005) Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast. Nat. Cell Biol. 7: 1224-1231
    • (2005) Nat. Cell Biol , vol.7 , pp. 1224-1231
    • Villarejo, A.1    Burén, S.2    Larsson, S.3    Déjardin, A.4    Monné, M.5    Rudhe, C.6
  • 72
    • 33646859762 scopus 로고    scopus 로고
    • Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center
    • Waratrujiwong, T., Krebs, B., Spener, F. and Visoottiviseth, P. (2006) Recombinant purple acid phosphatase isoform 3 from sweet potato is an enzyme with a diiron metal center. FEBS J. 273: 1649-1659
    • (2006) FEBS J. , vol.273 , pp. 1649-1659
    • Waratrujiwong, T.1    Krebs, B.2    Spener, F.3    Visoottiviseth, P.4
  • 73
    • 0033771295 scopus 로고    scopus 로고
    • Antisense-inhibition of ADP-glucose pyrophosphorylase in developing seeds of Vicia narbonensis moderately decreases starch but increases protein content and affects seed maturation
    • Weber, H., Rolletschek, H., Heim, U., Golombek, S., Gubatz, S. and Wobus, U. (2000) Antisense-inhibition of ADP-glucose pyrophosphorylase in developing seeds of Vicia narbonensis moderately decreases starch but increases protein content and affects seed maturation. Plant J. 24: 33-43
    • (2000) Plant J. , vol.24 , pp. 33-43
    • Weber, H.1    Rolletschek, H.2    Heim, U.3    Golombek, S.4    Gubatz, S.5    Wobus, U.6
  • 74
    • 79953185052 scopus 로고    scopus 로고
    • Golgi nucleotiDe sugar transporter modulates cell wall biosynthesis and plant growth in rice
    • Zhang, B., Liu, X., Qian, Q., Liu, L., Dong, G., Xiong, G. et al. (2011) Golgi nucleotiDe sugar transporter modulates cell wall biosynthesis and plant growth in rice. Proc. Natl Acad. Sci. USA 108: 5110-5115
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 5110-5115
    • Zhang, B.1    Liu, X.2    Qian, Q.3    Liu, L.4    Dong, G.5    Xiong, G.6
  • 75
    • 26944432679 scopus 로고    scopus 로고
    • Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower
    • Zhu, H., Qian, W., Lu, X., Li, D., Liu, X., Liu, K. et al. (2005) Expression patterns of purple acid phosphatase genes in Arabidopsis organs and functional analysis of AtPAP23 predominantly transcribed in flower. Plant Mol. Biol. 59: 581-594 Technology
    • (2005) Plant Mol. Biol , vol.59 , pp. 581-594
    • Zhu, H.1    Qian, W.2    Lu, X.3    Li, D.4    Liu, X.5    Liu, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.