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Volumn 227, Issue 4, 2008, Pages 795-807

New insights on sucrose metabolism: Evidence for an active A/N-Inv in chloroplasts uncovers a novel component of the intracellular carbon trafficking

Author keywords

Alkaline neutral invertase; Arabidopsis; Chloroplasts; Spinach subcellular localization; Sucrose hydrolysis

Indexed keywords

BETA FRUCTOFURANOSIDASE; CARBON; ISOENZYME; SUCROSE; VEGETABLE PROTEIN;

EID: 38649133860     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-007-0657-1     Document Type: Article
Times cited : (79)

References (78)
  • 3
    • 0029073522 scopus 로고
    • A membrane-associated form of sucrose synthase and its potential role in synthesis of cellulose and callose in plants
    • Amor Y, Haigler CH, Johnson S, Wainscott M, Delmer DP (1995) A membrane-associated form of sucrose synthase and its potential role in synthesis of cellulose and callose in plants. Poc Natl Acad Sci USA 92:9353-9357
    • (1995) Poc Natl Acad Sci USA , vol.92 , pp. 9353-9357
    • Amor, Y.1    Haigler, C.H.2    Johnson, S.3    Wainscott, M.4    Delmer, D.P.5
  • 5
    • 77956997090 scopus 로고
    • Colorimetric analysis of sugars
    • Academic New York
    • Ashwell G (1957) Colorimetric analysis of sugars. In: Colowik SP, Kaplan NO (eds) Methods enzymol, vol 3. Academic, New York, pp 73-105
    • (1957) Methods Enzymol , vol.3 , pp. 73-105
    • Ashwell, G.1    Colowik, S.P.2    Kaplan, N.O.3
  • 6
    • 0026777839 scopus 로고
    • Subcellular localization of ubiquitin and ubiquitinated proteins in Arabidopsis thaliana
    • Beers EP, Moreno TN, Callis J (1992) Subcellular localization of ubiquitin and ubiquitinated proteins in Arabidopsis thaliana. J Biol Chem 267:15432-15439
    • (1992) J Biol Chem , vol.267 , pp. 15432-15439
    • Beers, E.P.1    Moreno, T.N.2    Callis, J.3
  • 7
    • 0000002475 scopus 로고
    • D-Glucose: Determination with hexokinase and glucose-6-phosphate dehydrogenase
    • Academic New York
    • Bergmeyer HU, Bernt E, Schmidt F, Stork H (1974) d-Glucose: determination with hexokinase and glucose-6-phosphate dehydrogenase. In: Bergmeyer HU (ed) Methods of enzymatic analysis, vol 3. Academic, New York, pp 1196-1201
    • (1974) Methods of Enzymatic Analysis , vol.3 , pp. 1196-1201
    • Bergmeyer, H.U.1    Bernt, E.2    Schmidt, F.3    Stork, H.4    Bergmeyer, H.U.5
  • 9
    • 0034928217 scopus 로고    scopus 로고
    • Growth stage-based phenotypic analysis of Arabidopsis: A model for high throughput functional genomics in plants
    • Boyes DC, Zayed AM, Ascenzi R, McCaskill AJ, Hoffman NE, Davis KR, Görlach J (2001) Growth stage-based phenotypic analysis of Arabidopsis: a model for high throughput functional genomics in plants. Plant Cell 13:1499-1510
    • (2001) Plant Cell , vol.13 , pp. 1499-1510
    • Boyes, D.C.1    Zayed, A.M.2    Ascenzi, R.3    McCaskill, A.J.4    Hoffman, N.E.5    Davis, K.R.6    Görlach, J.7
  • 10
    • 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 7:248-254
    • (1976) Anal Biochem , vol.7 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0026650426 scopus 로고
    • Biochemical and immunological properties of alkaline invertase isolated from sprouting soybean hypocotyls
    • Chen JQ, Black CC (1992) Biochemical and immunological properties of alkaline invertase isolated from sprouting soybean hypocotyls. Arch Biochem Biophys 295:61-69
    • (1992) Arch Biochem Biophys , vol.295 , pp. 61-69
    • Chen, J.Q.1    Black, C.C.2
  • 12
    • 3543041300 scopus 로고    scopus 로고
    • Signal peptide-dependent targeting of a rice α-amylase and cargo proteins to plastids and extracellular compartments of plant cells
    • Chen M-H, Huang L-F, Li H-M, Chen Y-R, Yu S-M (2004) Signal peptide-dependent targeting of a rice α-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
    • 33750435187 scopus 로고    scopus 로고
    • Regulatory functions of nuclear hexokinase1 complex in glucose signaling
    • Cho Y-H, Yoo S-D, Sheen J (2006) Regulatory functions of nuclear hexokinase1 complex in glucose signaling. Cell 127:579-589
    • (2006) Cell , vol.127 , pp. 579-589
    • Cho, Y.-H.1    Yoo, S.-D.2    Sheen, J.3
  • 14
    • 0014670328 scopus 로고
    • Mitochondria and glyoxysomes from castor bean endosperm. Enzyme constituents and catalytic capacity
    • Cooper TG, Beevers H (1969) Mitochondria and glyoxysomes from castor bean endosperm. Enzyme constituents and catalytic capacity. J Biol Chem 244:3507-3513
    • (1969) J Biol Chem , vol.244 , pp. 3507-3513
    • Cooper, T.G.1    Beevers, H.2
  • 15
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorscent protein (gfp)
    • Cormack BP, Valdivia RH, Falkow S (1996) FACS-optimized mutants of the green fluorscent protein (gfp). Gene 173:33-38
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 17
    • 38649088487 scopus 로고
    • Permeability of sugar-cane chloroplasts to sucrose
    • Edelman J, Schoolar AI, Bonnor HW (1971) Permeability of sugar-cane chloroplasts to sucrose. J Exp Bot 22:534-545
    • (1971) J Exp Bot , vol.22 , pp. 534-545
    • Edelman, J.1    Schoolar, A.I.2    Bonnor, H.W.3
  • 19
    • 0035081595 scopus 로고    scopus 로고
    • Improved salt tolerance of transgenic tobacco expressing apoplastic yeast-derived invertase
    • Fukushima E, Arata Y, Endo T, Sonnewald U, Sato F (2001) Improved salt tolerance of transgenic tobacco expressing apoplastic yeast-derived invertase. Plant Cell Physiol 42:245-249
    • (2001) Plant Cell Physiol , vol.42 , pp. 245-249
    • Fukushima, E.1    Arata, Y.2    Endo, T.3    Sonnewald, U.4    Sato, F.5
  • 20
    • 0031978414 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA clone from Lolium temulentum encoding for a Suc hydrolytic enzyme which shows alkaline/neutral invertase activity
    • Gallagher JA, Pollock CJ (1998) Isolation and characterization of a cDNA clone from Lolium temulentum encoding for a Suc hydrolytic enzyme which shows alkaline/neutral invertase activity. J Exp Bot 49:789-795
    • (1998) J Exp Bot , vol.49 , pp. 789-795
    • Gallagher, J.A.1    Pollock, C.J.2
  • 22
    • 12744263638 scopus 로고    scopus 로고
    • Isolation and functional characterization of a novel plastidic hexokinase from Nicotiana tabacum
    • Giese JO, Herbers K, Hoffmann M, Klösgen RB, Sonnewald U (2005) Isolation and functional characterization of a novel plastidic hexokinase from Nicotiana tabacum. FEBS Lett 579:827-831
    • (2005) FEBS Lett , vol.579 , pp. 827-831
    • Giese, J.O.1    Herbers, K.2    Hoffmann, M.3    Klösgen, R.B.4    Sonnewald, U.5
  • 24
    • 0028039637 scopus 로고
    • Accumulation of hexoses in leaf vacuoles: Studies with transgenic tobacco plants expressing yeast-derived invertase in the cytosol, vacuole or apoplasm
    • Heineke D, Wildenberger K, Sonnewald U, Willmitzer L, Heldt HW (1994) Accumulation of hexoses in leaf vacuoles: studies with transgenic tobacco plants expressing yeast-derived invertase in the cytosol, vacuole or apoplasm. Planta 194:29-33
    • (1994) Planta , vol.194 , pp. 29-33
    • Heineke, D.1    Wildenberger, K.2    Sonnewald, U.3    Willmitzer, L.4    Heldt, H.W.5
  • 25
    • 0015212654 scopus 로고
    • The inner membrane of the chloroplast envelope as site of specific metabolite transport
    • Heldt HW, Sauer F (1971) The inner membrane of the chloroplast envelope as site of specific metabolite transport. Biochim Biophys Acta 234:83-91
    • (1971) Biochim Biophys Acta , vol.234 , pp. 83-91
    • Heldt, H.W.1    Sauer, F.2
  • 26
    • 0142214642 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase is activated by posttranslational redox-modification in response to light and to sugars in leaves of Arabidopsis and other plant species
    • Hendriks JH, Kolbe A, Gibon Y, Stitt M, Geigenberger P (2003) ADP-glucose pyrophosphorylase is activated by posttranslational redox-modification in response to light and to sugars in leaves of Arabidopsis and other plant species. Plant Physiol 133:838-849
    • (2003) Plant Physiol , vol.133 , pp. 838-849
    • Hendriks, J.H.1    Kolbe, A.2    Gibon, Y.3    Stitt, M.4    Geigenberger, P.5
  • 28
    • 0040419081 scopus 로고    scopus 로고
    • Role and regulation of sucrose-phosphate synthase in higher plants
    • Huber SC, Huber JL (1996) Role and regulation of sucrose-phosphate synthase in higher plants. Annu Rev Plant Physiol Plant Mol Biol 47:431-444
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 431-444
    • Huber, S.C.1    Huber, J.L.2
  • 29
    • 21244447375 scopus 로고    scopus 로고
    • Structure, evolution, and expression of the two invertase gene families of rice
    • Ji X, Van den Ende W, Van Laere A, Cheng S, Bennett J (2005) Structure, evolution, and expression of the two invertase gene families of rice. J Mol Evol 60:615-634
    • (2005) J Mol Evol , vol.60 , pp. 615-634
    • Ji, X.1    Van Den Ende, W.2    Van Laere, A.3    Cheng, S.4    Bennett, J.5
  • 31
    • 33644637941 scopus 로고    scopus 로고
    • The function and diversity of plastid protein import pathways: A multilane GTPase highway into plastids
    • Kessler F, Schnell DJ (2006) The function and diversity of plastid protein import pathways: a multilane GTPase highway into plastids. Traffic 7:248-257
    • (2006) Traffic , vol.7 , pp. 248-257
    • Kessler, F.1    Schnell, D.J.2
  • 32
    • 2442459991 scopus 로고    scopus 로고
    • Sucrose metabolism: Regulatory mechanisms and pivotal roles in sugar sensing and plant development
    • Koch K (2004) Sucrose metabolism: regulatory mechanisms and pivotal roles in sugar sensing and plant development. Curr Opin Plant Biol 7:235-246
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 235-246
    • Koch, K.1
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 33646835436 scopus 로고    scopus 로고
    • Functional characterization of sequence motifs in the transit peptide of Arabidopsis small subunit of rubisco
    • Lee DW, Lee S, Lee G-j, Lee KH, Kim S, Cheong GW, Hwang I (2006) Functional characterization of sequence motifs in the transit peptide of Arabidopsis small subunit of rubisco. Plant Physiol 140:466-483
    • (2006) Plant Physiol , vol.140 , pp. 466-483
    • Lee, D.W.1    Lee, S.2    G-J, L.3    Lee, K.H.4    Kim, S.5    Cheong, G.W.6    Hwang, I.7
  • 35
    • 0030468569 scopus 로고    scopus 로고
    • Purification and characterization of neutral and alkaline invertase from carrot
    • Lee HS, Sturm A (1996) Purification and characterization of neutral and alkaline invertase from carrot. Plant Physiol 112:1513-1522
    • (1996) Plant Physiol , vol.112 , pp. 1513-1522
    • Lee, H.S.1    Sturm, A.2
  • 36
    • 33845957146 scopus 로고    scopus 로고
    • Plastid biogenesis, between light and shadows
    • López-Juez E (2007) Plastid biogenesis, between light and shadows. J Exp Bot 58:11-26
    • (2007) J Exp Bot , vol.58 , pp. 11-26
    • López-Juez, E.1
  • 37
    • 27744432391 scopus 로고    scopus 로고
    • Plastids unleashed: Their development and their integration in plant development
    • López-Juez E, Pyke KA (2005) Plastids unleashed: their development and their integration in plant development. Int J Dev Biol 49:557-577
    • (2005) Int J Dev Biol , vol.49 , pp. 557-577
    • López-Juez, E.1    Pyke, K.A.2
  • 38
    • 34249792376 scopus 로고    scopus 로고
    • PIP5K9, an Arabidopsis phosphatidylinositol monophosphate kinase, interacts with a cytosolic invertase to negatively regulate sugar-mediated root growth
    • Lou Y, Gou J-Y, Xue H-W (2007) PIP5K9, an Arabidopsis phosphatidylinositol monophosphate kinase, interacts with a cytosolic invertase to negatively regulate sugar-mediated root growth. Plant Cell 19:163-181
    • (2007) Plant Cell , vol.19 , pp. 163-181
    • Lou, Y.1    Gou, J.-Y.2    Xue, H.-W.3
  • 39
    • 0033740573 scopus 로고    scopus 로고
    • Purification, molecular cloning, and sequence analysis of Suc-6-phosphate phosphohydrolase from plants
    • Lunn J, Ashton A, Hatch M, Heldt H (2000) Purification, molecular cloning, and sequence analysis of Suc-6-phosphate phosphohydrolase from plants. Proc Natl Acad Sci USA 97:12914-12919
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12914-12919
    • Lunn, J.1    Ashton, A.2    Hatch, M.3    Heldt, H.4
  • 40
    • 0000411157 scopus 로고
    • Absortion of light by chlorophyll solutions
    • Mackinney G (1941) Absortion of light by chlorophyll solutions. J Biol Chem 140:315-322
    • (1941) J Biol Chem , vol.140 , pp. 315-322
    • MacKinney, G.1
  • 41
    • 0029328417 scopus 로고
    • Starch biosynthesis
    • Martin C, Smith AM (1995) Starch biosynthesis. Plant Cell 7:971-985
    • (1995) Plant Cell , vol.7 , pp. 971-985
    • Martin, C.1    Smith, A.M.2
  • 42
    • 0031627086 scopus 로고    scopus 로고
    • Protoplasts isolation, culture and regeneration
    • Martínez-Zapater JM, Salinas J (eds) Humana Press, Totowa, NJ
    • Mathur J, Koncz C (1998) Protoplasts isolation, culture and regeneration. In: Martínez-Zapater JM, Salinas J (eds) Arabidopsis protocols. Methods in molecular biology, vol 8. Humana Press, Totowa, NJ, pp 35-42
    • (1998) Arabidopsis Protocols. Methods in Molecular Biology , vol.8 , pp. 35-42
    • Mathur, J.1    Koncz, C.2
  • 43
    • 0000167609 scopus 로고
    • Slow passive diffusion of orthophosphate between intact isolated chloroplasts and suspending medium
    • Mourioux G, Douce R (1981) Slow passive diffusion of orthophosphate between intact isolated chloroplasts and suspending medium. Plant Physiol 67:470-473
    • (1981) Plant Physiol , vol.67 , pp. 470-473
    • Mourioux, G.1    Douce, R.2
  • 44
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassay with tobacco tissue culture
    • Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassay with tobacco tissue culture. Physiol Plant 15:473-497
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 45
    • 33947267616 scopus 로고    scopus 로고
    • Genes for alkaline/neutral invertase in rice: Alkaline/neutral invertases are located in plant mitochondria and also in plastids
    • Murayama H, Handa S (2007) Genes for alkaline/neutral invertase in rice: alkaline/neutral invertases are located in plant mitochondria and also in plastids. Planta 225:1193-1203
    • (2007) Planta , vol.225 , pp. 1193-1203
    • Murayama, H.1    Handa, S.2
  • 46
    • 0034935172 scopus 로고    scopus 로고
    • Sink regulation of photosynthesis
    • Paul MJ, Foyer CH (2001) Sink regulation of photosynthesis. J Exp Bot 52:1383-1400
    • (2001) J Exp Bot , vol.52 , pp. 1383-1400
    • Paul, M.J.1    Foyer, C.H.2
  • 47
    • 0033550217 scopus 로고    scopus 로고
    • Differential synthesis of sucrose and trehalose in Euglena gracilis cells during growth and salt stress
    • Porchia AC, Fiol DF, Salerno GL (1999) Differential synthesis of sucrose and trehalose in Euglena gracilis cells during growth and salt stress. Plant Sci 149:43-49
    • (1999) Plant Sci , vol.149 , pp. 43-49
    • Porchia, A.C.1    Fiol, D.F.2    Salerno, G.L.3
  • 49
    • 0036276818 scopus 로고    scopus 로고
    • Sugar sensing and signaling in plants
    • Suppl
    • Rolland F, Moore B, Sheen J (2002) Sugar sensing and signaling in plants. Plant Cell 14(Suppl):S185-S205
    • (2002) Plant Cell , vol.14
    • Rolland, F.1    Moore, B.2    Sheen, J.3
  • 50
    • 0000578976 scopus 로고    scopus 로고
    • Sucrolytic enzyme activities in cotyledons of the faba bean (developmental changes and purification of alkaline invertase)
    • Ross HA, McRae D, Davies HV (1996) Sucrolytic enzyme activities in cotyledons of the faba bean (developmental changes and purification of alkaline invertase). Plant Physiol 111:329-338
    • (1996) Plant Physiol , vol.111 , pp. 329-338
    • Ross, H.A.1    McRae, D.2    Davies, H.V.3
  • 51
    • 0035282660 scopus 로고    scopus 로고
    • How many genes in Arabidopsis come from cyanobacteria? An estimate from 386 protein phylogenies
    • Rujan T, Martin W (2001) How many genes in Arabidopsis come from cyanobacteria? An estimate from 386 protein phylogenies. Trends Genet 17:113-120
    • (2001) Trends Genet , vol.17 , pp. 113-120
    • Rujan, T.1    Martin, W.2
  • 52
    • 38649119063 scopus 로고    scopus 로고
    • Studies on Suc-phosphate synthase from rice leaves
    • Salerno GL, Pagnussat GC, Pontis HG (1998) Studies on Suc-phosphate synthase from rice leaves. Cell Mol Biol 44:404-416
    • (1998) Cell Mol Biol , vol.44 , pp. 404-416
    • Salerno, G.L.1    Pagnussat, G.C.2    Pontis, H.G.3
  • 53
    • 0037937490 scopus 로고    scopus 로고
    • Origin of sucrose metabolism in higher plants: When, how and why?
    • Salerno G, Curatti L (2003) Origin of sucrose metabolism in higher plants: when, how and why? Trends Plant Sci 8:63-69
    • (2003) Trends Plant Sci , vol.8 , pp. 63-69
    • Salerno, G.1    Curatti, L.2
  • 55
    • 0000417960 scopus 로고
    • Sugar compartmentation in frost-hardy and partially deharded cabbage leaf cells
    • Santarius KA, Milde H (1977) Sugar compartmentation in frost-hardy and partially deharded cabbage leaf cells. Planta 136:163-166
    • (1977) Planta , vol.136 , pp. 163-166
    • Santarius, K.A.1    Milde, H.2
  • 56
    • 0001691843 scopus 로고
    • Comparison of NADP-malate dehydrogenase activation, QA reduction and O2 evolution in spinach leaves
    • Scheibe R, Stitt M (1988) Comparison of NADP-malate dehydrogenase activation, QA reduction and O2 evolution in spinach leaves. Plant Physiol Biochem 26:473-481
    • (1988) Plant Physiol Biochem , vol.26 , pp. 473-481
    • Scheibe, R.1    Stitt, M.2
  • 60
    • 0001188945 scopus 로고
    • Pyrophosphorylases in Solanum tuberosum
    • Sowokinos J (1981) Pyrophosphorylases in Solanum tuberosum. Plant Physiol 68:924-929
    • (1981) Plant Physiol , vol.68 , pp. 924-929
    • Sowokinos, J.1
  • 61
    • 0001250491 scopus 로고
    • Physiological rates of starch breakdown in isolated intact spinach chloroplasts
    • Stitt M, Heldt HW (1981) Physiological rates of starch breakdown in isolated intact spinach chloroplasts. Plant Physiol 68:755-761
    • (1981) Plant Physiol , vol.68 , pp. 755-761
    • Stitt, M.1    Heldt, H.W.2
  • 62
    • 0033199981 scopus 로고    scopus 로고
    • Invertases. Primary structures, functions, and roles in plant development and sucrose partitioning
    • Sturm A (1999) Invertases. Primary structures, functions, and roles in plant development and sucrose partitioning. Plant Physiol 121:1-7
    • (1999) Plant Physiol , vol.121 , pp. 1-7
    • Sturm, A.1
  • 63
    • 0033431057 scopus 로고    scopus 로고
    • Neutral invertase is a novel type of Suc-cleaving enzyme
    • Sturm A, Hess D, Lee HS, Lienhard S (1999) Neutral invertase is a novel type of Suc-cleaving enzyme. Physiol Plant 107:159-165
    • (1999) Physiol Plant , vol.107 , pp. 159-165
    • Sturm, A.1    Hess, D.2    Lee, H.S.3    Lienhard, S.4
  • 65
    • 5144229754 scopus 로고    scopus 로고
    • Recent developments in understanding the regulation of starch metabolism in higher plants
    • Tetlow IJ, Morell MK, Emes MJ (2004) Recent developments in understanding the regulation of starch metabolism in higher plants. J Exp Bot 55:2131-2145
    • (2004) J Exp Bot , vol.55 , pp. 2131-2145
    • Tetlow, I.J.1    Morell, M.K.2    Emes, M.J.3
  • 66
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak FM, Jeanmougin F, Higgins DG (1997) The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 15:4876-4882
    • (1997) Nucleic Acids Res , vol.15 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.M.3    Jeanmougin, F.4    Higgins, D.G.5
  • 67
    • 0036743460 scopus 로고    scopus 로고
    • Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: A novel regulatory mechanism linking starch synthesis to the sucrose supply
    • Tiessen A, Hendriks JHM, Stitt M, Branscheid A, Gibon Y, Farré EM, Geigenberger P (2002) Starch synthesis in potato tubers is regulated by post-translational redox modification of ADP-glucose pyrophosphorylase: a novel regulatory mechanism linking starch synthesis to the sucrose supply. Plant Cell 14:2191:2213
    • (2002) Plant Cell , vol.14 , pp. 2191-2213
    • Tiessen, A.1    Hendriks, J.H.M.2    Stitt, M.3    Branscheid, A.4    Gibon, Y.5    Farré, E.M.6    Geigenberger, P.7
  • 68
    • 0029106371 scopus 로고
    • Purification and properties of a neutral invertase from the roots of Cichorium intybus
    • Van den Ende W, Van Laere A (1995) Purification and properties of a neutral invertase from the roots of Cichorium intybus. Physiol Plant 93:241-248
    • (1995) Physiol Plant , vol.93 , pp. 241-248
    • Van Den Ende, W.1    Van Laere, A.2
  • 69
    • 0038610799 scopus 로고    scopus 로고
    • Cyanobacterial alkaline/neutral invertases. Origin of Suc hydrolysis in the plant cytosol?
    • Vargas W, Cumino AC, Salerno GL (2003) Cyanobacterial alkaline/neutral invertases. Origin of Suc hydrolysis in the plant cytosol? Planta 216:951-960
    • (2003) Planta , vol.216 , pp. 951-960
    • Vargas, W.1    Cumino, A.C.2    Salerno, G.L.3
  • 70
    • 35348922311 scopus 로고    scopus 로고
    • Differential expression of alkaline and neutral invertases in response to environmental stresses: Characterization of an alkaline isoform as a stress-response enzyme in wheat leaves
    • Vargas WA, Pontis HG, Salerno GL (2007) Differential expression of alkaline and neutral invertases in response to environmental stresses: characterization of an alkaline isoform as a stress-response enzyme in wheat leaves. Planta 226:1535-1545
    • (2007) Planta , vol.226 , pp. 1535-1545
    • Vargas, W.A.1    Pontis, H.G.2    Salerno, G.L.3
  • 71
    • 0032188999 scopus 로고    scopus 로고
    • Partial purification and characterization of sugarcane neutral invertase
    • Vorster DJ, Botha FC (1998) Partial purification and characterization of sugarcane neutral invertase. Phytochemistry 49:651-655
    • (1998) Phytochemistry , vol.49 , pp. 651-655
    • Vorster, D.J.1    Botha, F.C.2
  • 72
    • 0029868470 scopus 로고    scopus 로고
    • Phosphorylation of the transit sequence of chloroplast precursor proteins
    • Waegemann K, Soll J (1996) Phosphorylation of the transit sequence of chloroplast precursor proteins. J Biol Chem 271:6545-6554
    • (1996) J Biol Chem , vol.271 , pp. 6545-6554
    • Waegemann, K.1    Soll, J.2
  • 73
    • 0041844096 scopus 로고
    • Chloroplast and cell. the movement of certain key substances, etc. across the chloroplast envelope
    • Butterworth London
    • Walker DA (1974) Chloroplast and cell. The movement of certain key substances, etc. across the chloroplast envelope. In: Northcote DH (ed) MTP International review of science, biochemistry series one, vol 11. Butterworth, London, pp 1-49
    • (1974) MTP International Review of Science, Biochemistry Series One , vol.11 , pp. 1-49
    • Walker, D.A.1    Northcote, D.H.2
  • 74
    • 0031452962 scopus 로고    scopus 로고
    • Purification and characterization of invertases from leaves of Lolium temulentum
    • Walker RP, Winters AL, Pollock CJ (1997) Purification and characterization of invertases from leaves of Lolium temulentum. New Phytol 135:259-266
    • (1997) New Phytol , vol.135 , pp. 259-266
    • Walker, R.P.1    Winters, A.L.2    Pollock, C.J.3
  • 75
    • 0015212862 scopus 로고
    • Permeability of pea chloroplastst alcohols and aldoses as measured by reflection coefficients
    • Wang CT, Nobel PS (1971) Permeability of pea chloroplastst alcohols and aldoses as measured by reflection coefficients. Biochim Biophys Acta 241:200-212
    • (1971) Biochim Biophys Acta , vol.241 , pp. 200-212
    • Wang, C.T.1    Nobel, P.S.2
  • 76
    • 0033984161 scopus 로고    scopus 로고
    • Regulation of sucrose metabolism in higher plants: Localization and regulation of activity of key enzymes
    • Winter H, Huber SC (2000) Regulation of sucrose metabolism in higher plants: localization and regulation of activity of key enzymes. Crit Rev Plant Sci 19:31-67
    • (2000) Crit Rev Plant Sci , vol.19 , pp. 31-67
    • Winter, H.1    Huber, S.C.2
  • 77
    • 0027976083 scopus 로고
    • Subcellular volumes and metabolite concentrations in spinach leaves
    • Winter H, Robinson DG, Heldt HW (1994) Subcellular volumes and metabolite concentrations in spinach leaves. Planta 193:530-535
    • (1994) Planta , vol.193 , pp. 530-535
    • Winter, H.1    Robinson, D.G.2    Heldt, H.W.3
  • 78
    • 20744443090 scopus 로고    scopus 로고
    • Optimization of Agrobacterium-mediated transient assays of gene expression in lettuce, tomato and Arabidopsis
    • Wroblewski T, Tomczak A, Michelmore R (2005) Optimization of Agrobacterium-mediated transient assays of gene expression in lettuce, tomato and Arabidopsis. Plant Biotech J 3:259-273
    • (2005) Plant Biotech J , vol.3 , pp. 259-273
    • Wroblewski, T.1    Tomczak, A.2    Michelmore, R.3


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