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Volumn 277, Issue 2, 2010, Pages 428-440

The starch-binding capacity of the noncatalytic SBD2 region and the interaction between the N- and C-terminal domains are involved in the modulation of the activity of starch synthase III from Arabidopsis thaliana: Enzymes and catalysis

Author keywords

Arabidopsis; Enzyme regulation; Protein interaction; Starch synthase; Starch binding domain

Indexed keywords

ADENOSINE DIPHOSPHATE GLUCOSE; AMINO ACID; POLYSACCHARIDE; STARCH; SYNTHETASE;

EID: 74549189480     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07495.x     Document Type: Article
Times cited : (40)

References (47)
  • 1
    • 0034890627 scopus 로고    scopus 로고
    • The biosynthesis of starch granules
    • Smith AM (2001) The biosynthesis of starch granules. Biomacromolecules 2, 335 341.
    • (2001) Biomacromolecules , vol.2 , pp. 335-341
    • Smith, A.M.1
  • 2
    • 0031613064 scopus 로고    scopus 로고
    • Biochemistry, molecular biology and regulation of starch synthesis
    • Preiss J Sivak MN (1998) Biochemistry, molecular biology and regulation of starch synthesis. Genet Eng (NY) 20, 177 223.
    • (1998) Genet Eng (NY) , vol.20 , pp. 177-223
    • Preiss, J.1    Sivak, M.N.2
  • 3
    • 0142040430 scopus 로고    scopus 로고
    • From bacterial glycogen to starch: Understanding the biogenesis of the plant starch granule
    • Ball SG Morell MK (2003) From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule. Annu Rev Plant Biol 54, 207 233.
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 207-233
    • Ball, S.G.1    Morell, M.K.2
  • 4
    • 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
  • 5
    • 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
  • 8
    • 26944490008 scopus 로고    scopus 로고
    • Mutations affecting starch synthase III in Arabidopsis alter leaf starch structure and increase the rate of starch synthesis
    • Zhang X, Myers AM James MG (2005) Mutations affecting starch synthase III in Arabidopsis alter leaf starch structure and increase the rate of starch synthesis. Plant Physiol 138, 663 674.
    • (2005) Plant Physiol , vol.138 , pp. 663-674
    • Zhang, X.1    Myers, A.M.2    James, M.G.3
  • 9
    • 0026652567 scopus 로고
    • Waxy Chlamydomonas reinhardtii: Monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin
    • Delrue B, Fontaine T, Routier F, Decq A, Wieruszeski JM, Van Den Koornhuyse N, Maddelein ML, Fournet B Ball S (1992) Waxy Chlamydomonas reinhardtii: monocellular algal mutants defective in amylose biosynthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin. J Bacteriol 174, 3612 3620.
    • (1992) J Bacteriol , vol.174 , pp. 3612-3620
    • Delrue, B.1    Fontaine, T.2    Routier, F.3    Decq, A.4    Wieruszeski, J.M.5    Van Den Koornhuyse, N.6    Maddelein, M.L.7    Fournet, B.8    Ball, S.9
  • 10
    • 33846403747 scopus 로고    scopus 로고
    • The phenotype of soluble starch synthase IV defective mutants of Arabidopsis thaliana suggests a novel function of elongation enzymes in the control of starch granule formation
    • Roldan I, Wattebled F, Mercedes Lucas M, Delvalle D, Planchot V, Jimenez S, Perez R, Ball S, D'Hulst C Merida A (2007) The phenotype of soluble starch synthase IV defective mutants of Arabidopsis thaliana suggests a novel function of elongation enzymes in the control of starch granule formation. Plant J 49, 492 504.
    • (2007) Plant J , vol.49 , pp. 492-504
    • Roldan, I.1    Wattebled, F.2    Mercedes Lucas, M.3    Delvalle, D.4    Planchot, V.5    Jimenez, S.6    Perez, R.7    Ball, S.8    D'Hulst, C.9    Merida, A.10
  • 15
    • 0034089676 scopus 로고    scopus 로고
    • The structure and expression of the wheat starch synthase III gene. Motifs in the expressed gene define the lineage of the starch synthase III gene family
    • Li Z, Mouille G, Kosar-Hashemi B, Rahman S, Clarke B, Gale KR, Appels R Morell MK (2000) The structure and expression of the wheat starch synthase III gene. Motifs in the expressed gene define the lineage of the starch synthase III gene family. Plant Physiol 123, 613 624.
    • (2000) Plant Physiol , vol.123 , pp. 613-624
    • Li, Z.1    Mouille, G.2    Kosar-Hashemi, B.3    Rahman, S.4    Clarke, B.5    Gale, K.R.6    Appels, R.7    Morell, M.K.8
  • 16
    • 14544289247 scopus 로고    scopus 로고
    • Evolution and expression analysis of starch synthase III and IV in rice
    • Dian W, Jiang H Wu P (2005) Evolution and expression analysis of starch synthase III and IV in rice. J Exp Bot 56, 623 632.
    • (2005) J Exp Bot , vol.56 , pp. 623-632
    • Dian, W.1    Jiang, H.2    Wu, P.3
  • 18
    • 34548128331 scopus 로고    scopus 로고
    • Enzymatic characterization of starch synthase III from kidney bean (Phaseolus vulgaris L.)
    • Senoura T, Asao A, Takashima Y, Isono N, Hamada S, Ito H Matsui H (2007) Enzymatic characterization of starch synthase III from kidney bean (Phaseolus vulgaris L.). FEBS J 274, 4550 4560.
    • (2007) FEBS J , vol.274 , pp. 4550-4560
    • Senoura, T.1    Asao, A.2    Takashima, Y.3    Isono, N.4    Hamada, S.5    Ito, H.6    Matsui, H.7
  • 19
    • 40149108056 scopus 로고    scopus 로고
    • Role of the N-terminal starch-binding domains in the kinetic properties of starch synthase III from Arabidopsis thaliana
    • Valdez HA, Busi MV, Wayllace NZ, Parisi G, Ugalde RA Gomez-Casati DF (2008) Role of the N-terminal starch-binding domains in the kinetic properties of starch synthase III from Arabidopsis thaliana. Biochemistry 47, 3026 3032.
    • (2008) Biochemistry , vol.47 , pp. 3026-3032
    • Valdez, H.A.1    Busi, M.V.2    Wayllace, N.Z.3    Parisi, G.4    Ugalde, R.A.5    Gomez-Casati, D.F.6
  • 23
    • 33845498615 scopus 로고    scopus 로고
    • Starch-binding domains in the post-genome era
    • Machovic M Janecek S (2006) Starch-binding domains in the post-genome era. Cell Mol Life Sci 63, 2710 2724.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2710-2724
    • MacHovic, M.1    Janecek, S.2
  • 24
    • 33750979827 scopus 로고    scopus 로고
    • The evolution of putative starch-binding domains
    • Machovic M Janecek S (2006) The evolution of putative starch-binding domains. FEBS Lett 580, 6349 6356.
    • (2006) FEBS Lett , vol.580 , pp. 6349-6356
    • MacHovic, M.1    Janecek, S.2
  • 25
    • 0035834494 scopus 로고    scopus 로고
    • Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose
    • Giardina T, Gunning AP, Juge N, Faulds CB, Furniss CS, Svensson B, Morris VJ Williamson G (2001) Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose. J Mol Biol 313, 1149 1159.
    • (2001) J Mol Biol , vol.313 , pp. 1149-1159
    • Giardina, T.1    Gunning, A.P.2    Juge, N.3    Faulds, C.B.4    Furniss, C.S.5    Svensson, B.6    Morris, V.J.7    Williamson, G.8
  • 28
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to β-cyclodextrin
    • Sorimachi K, Le Gal-Coeffet MF, Williamson G, Archer DB Williamson MP (1997) Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. Structure 5, 647 661. (Pubitemid 27236264)
    • (1997) Structure , vol.5 , Issue.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coeffet, M.-F.2    Williamson, G.3    Archer, D.B.4    Williamson, M.P.5
  • 29
    • 43549108852 scopus 로고    scopus 로고
    • Prospects for increasing starch and sucrose yields for bioethanol production
    • Smith AM (2008) Prospects for increasing starch and sucrose yields for bioethanol production. Plant J 54, 546 558.
    • (2008) Plant J , vol.54 , pp. 546-558
    • Smith, A.M.1
  • 30
    • 1542380999 scopus 로고    scopus 로고
    • Improving starch for food and industrial applications
    • Jobling S (2004) Improving starch for food and industrial applications. Curr Opin Plant Biol 7, 210 218.
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 210-218
    • Jobling, S.1
  • 31
    • 0033028207 scopus 로고    scopus 로고
    • A combined reduction in activity of starch synthases II and III of potato has novel effects on the starch of tubers
    • Edwards A, Fulton DC, Hylton C, Jobling SA, Gidley M, Rössner U, Martin C Smith A (1999) A combined reduction in activity of starch synthases II and III of potato has novel effects on the starch of tubers. Plant J 17, 251 261.
    • (1999) Plant J , vol.17 , pp. 251-261
    • Edwards, A.1    Fulton, D.C.2    Hylton, C.3    Jobling, S.A.4    Gidley, M.5    Rössner, U.6    Martin, C.7    Smith, A.8
  • 32
    • 0032029093 scopus 로고    scopus 로고
    • Characterization of dull1, a maize gene coding for a novel starch synthase
    • Gao M, Wanat J, Stinard PS, James MG Myers AM (1998) Characterization of dull1, a maize gene coding for a novel starch synthase. Plant Cell 10, 399 412.
    • (1998) Plant Cell , vol.10 , pp. 399-412
    • Gao, M.1    Wanat, J.2    Stinard, P.S.3    James, M.G.4    Myers, A.M.5
  • 33
    • 0442314288 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis
    • Ballicora MA, Iglesias AA Preiss J (2004) ADP-glucose pyrophosphorylase: a regulatory enzyme for plant starch synthesis. Photosynth Res 79, 1 24.
    • (2004) Photosynth Res , vol.79 , pp. 1-24
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 34
    • 4344680114 scopus 로고    scopus 로고
    • The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
    • Bejar CM, Ballicora MA, Gomez-Casati DF, Iglesias AA Preiss J (2004) The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains. FEBS Lett 573, 99 104.
    • (2004) FEBS Lett , vol.573 , pp. 99-104
    • Bejar, C.M.1    Ballicora, M.A.2    Gomez-Casati, D.F.3    Iglesias, A.A.4    Preiss, J.5
  • 35
    • 63549116698 scopus 로고    scopus 로고
    • Proteins from multiple metabolic pathways associate with starch biosynthetic enzymes in high molecular weight complexes: A model for regulation of carbon allocation in maize amyloplasts
    • Hennen-Bierwagen TA, Lin Q, Grimaud F, Planchot V, Keeling PL, James MG Myers AM (2009) Proteins from multiple metabolic pathways associate with starch biosynthetic enzymes in high molecular weight complexes: a model for regulation of carbon allocation in maize amyloplasts. Plant Physiol 149, 1541 1559.
    • (2009) Plant Physiol , vol.149 , pp. 1541-1559
    • Hennen-Bierwagen, T.A.1    Lin, Q.2    Grimaud, F.3    Planchot, V.4    Keeling, P.L.5    James, M.G.6    Myers, A.M.7
  • 37
    • 61349124174 scopus 로고    scopus 로고
    • A single residue mutation abolishes attachment of the CBM26 starch-binding domain from Lactobacillus amylovorus alpha-amylase
    • Rodríguez-Sanoja R, Oviedo N, Escalante L, Ruiz B Sánchez S (2009) A single residue mutation abolishes attachment of the CBM26 starch-binding domain from Lactobacillus amylovorus alpha-amylase. J Ind Microbiol Biotechnol 36, 341 346.
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 341-346
    • Rodríguez-Sanoja, R.1    Oviedo, N.2    Escalante, L.3    Ruiz, B.4    Sánchez, S.5
  • 39
  • 41
    • 0026170523 scopus 로고
    • Alpha-Amylase adsorption on starch crystallites
    • Leloup VM, Colonna P Ring SG (1991) alpha-Amylase adsorption on starch crystallites. Biotechnol Bioeng 38, 127 134.
    • (1991) Biotechnol Bioeng , vol.38 , pp. 127-134
    • Leloup, V.M.1    Colonna, P.2    Ring, S.G.3
  • 42
    • 39149110297 scopus 로고    scopus 로고
    • Detecting protein-protein interactions by far western blotting
    • Wu Y, Li Q Chen XZ (2007) Detecting protein-protein interactions by far western blotting. Nat Protoc 2, 3278 3284.
    • (2007) Nat Protoc , vol.2 , pp. 3278-3284
    • Wu, Y.1    Li, Q.2    Chen, X.Z.3
  • 44
    • 0141703314 scopus 로고    scopus 로고
    • De novo synthesis of bacterial glycogen: Agrobacterium tumefaciens glycogen synthase is involved in glucan initiation and elongation
    • Ugalde JE, Parodi AJ Ugalde RA (2003) De novo synthesis of bacterial glycogen: Agrobacterium tumefaciens glycogen synthase is involved in glucan initiation and elongation. Proc Natl Acad Sci USA 100, 10659 10663.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10659-10663
    • Ugalde, J.E.1    Parodi, A.J.2    Ugalde, R.A.3
  • 45
    • 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
  • 46
    • 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


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