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Volumn 156, Issue 1, 2011, Pages 61-77

Functional diversity of isoamylase oligomers: The ISA1 homo-oligomer is essential for amylopectin biosynthesis in rice endosperm

Author keywords

[No Author keywords available]

Indexed keywords

ORYZA SATIVA; SOLANUM TUBEROSUM;

EID: 79955993963     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.111.173435     Document Type: Article
Times cited : (84)

References (40)
  • 1
    • 84954949855 scopus 로고
    • Structural characterization of amylopectin and intermediate material in amylomaize starch granules
    • Baba T, Arai Y (1984) Structural characterization of amylopectin and intermediate material in amylomaize starch granules. Agric Biol Chem 48: 1763-1775
    • (1984) Agric Biol Chem , vol.48 , pp. 1763-1775
    • Baba, T.1    Arai, Y.2
  • 5
    • 15544372016 scopus 로고    scopus 로고
    • Arabidopsis mutants Atisa1 and Atisa2 have identical phenotypes and lack the same multimeric isoamylase, which influences the branch point distribution of amylopectin during starch synthesis
    • Delatte T, Trevisan M, Parker ML, Zeeman SC (2005) Arabidopsis mutants Atisa1 and Atisa2 have identical phenotypes and lack the same multimeric isoamylase, which influences the branch point distribution of amylopectin during starch synthesis. Plant J 41: 815-830
    • (2005) Plant J , vol.41 , pp. 815-830
    • Delatte, T.1    Trevisan, M.2    Parker, M.L.3    Zeeman, S.C.4
  • 6
    • 0033118441 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice
    • Fujita N, Kubo A, Francisco PB Jr, Nakakita M, Harada K, Minaka N, Nakamura Y (1999) Purification, characterization, and cDNA structure of isoamylase from developing endosperm of rice. Planta 208: 283-293
    • (1999) Planta , vol.208 , pp. 283-293
    • Fujita, N.1    Kubo, A.2    Francisco Jr., P.B.3    Nakakita, M.4    Harada, K.5    Minaka, N.6    Nakamura, Y.7
  • 7
    • 0038303343 scopus 로고    scopus 로고
    • Antisense inhibition of isoamylase alters the structure of amylopectin and the physicochemical properties of starch in rice endosperm
    • Fujita N, Kubo A, Suh DS, Wong KS, Jane JL, Ozawa K, Takaiwa F, Inaba Y, Nakamura Y (2003) Antisense inhibition of isoamylase alters the structure of amylopectin and the physicochemical properties of starch in rice endosperm. Plant Cell Physiol 44: 607-618
    • (2003) Plant Cell Physiol , vol.44 , pp. 607-618
    • Fujita, N.1    Kubo, A.2    Suh, D.S.3    Wong, K.S.4    Jane, J.L.5    Ozawa, K.6    Takaiwa, F.7    Inaba, Y.8    Nakamura, Y.9
  • 8
    • 62349142264 scopus 로고    scopus 로고
    • Characterization of pullulanase (PUL)-deficient mutants of rice (Oryza sativa L.) and the function of PUL on starch biosynthesis in the developing rice endosperm
    • Fujita N, Toyosawa Y, Utsumi Y, Higuchi T, Hanashiro I, Ikegami A, Akuzawa S, Yoshida M, Mori A, Inomata K, et al (2009) Characterization of pullulanase (PUL)-deficient mutants of rice (Oryza sativa L.) and the function of PUL on starch biosynthesis in the developing rice endosperm. J Exp Bot 60: 1009-1023
    • (2009) J Exp Bot , vol.60 , pp. 1009-1023
    • Fujita, N.1    Toyosawa, Y.2    Utsumi, Y.3    Higuchi, T.4    Hanashiro, I.5    Ikegami, A.6    Akuzawa, S.7    Yoshida, M.8    Mori, A.9    Inomata, K.10
  • 12
  • 14
    • 0001384883 scopus 로고
    • Debranching enzymes of potato tubers (Solanum tuberosum L.). I. Purification and some properties of potato isoamylase
    • Ishizaki Y, Taniguchi H, Maruyama Y, Nakamura M (1983) Debranching enzymes of potato tubers (Solanum tuberosum L.). I. Purification and some properties of potato isoamylase. Agric Biol Chem 47: 771-779
    • (1983) Agric Biol Chem , vol.47 , pp. 771-779
    • Ishizaki, Y.1    Taniguchi, H.2    Maruyama, Y.3    Nakamura, M.4
  • 15
    • 0037671338 scopus 로고    scopus 로고
    • Introduction of Wx transgene into rice wx mutants leads to both high-and lowamylose rice
    • Itoh K, Ozaki H, Okada K, Hori H, Takeda Y, Mitsui T (2003) Introduction of Wx transgene into rice wx mutants leads to both high-and lowamylose rice. Plant Cell Physiol 44: 473-480
    • (2003) Plant Cell Physiol , vol.44 , pp. 473-480
    • Itoh, K.1    Ozaki, H.2    Okada, K.3    Hori, H.4    Takeda, Y.5    Mitsui, T.6
  • 16
    • 0029278930 scopus 로고
    • Characterization of the maize gene sugary1, a determinant of starch composition in kernels
    • James MG, Robertson DS, Myers AM(1995) Characterization of the maize gene sugary1, 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    Myers, A.M.3
  • 17
    • 84985638083 scopus 로고
    • Naegeli amylodextrin and its relationship to starch granule structure. II. Role of water in crystallization of B-starch
    • Kainuma K, French D (1972) Naegeli amylodextrin and its relationship to starch granule structure. II. Role of water in crystallization of B-starch. Biopolymers 11: 2241-2250
    • (1972) Biopolymers , vol.11 , pp. 2241-2250
    • Kainuma, K.1    French, D.2
  • 19
    • 0032748917 scopus 로고    scopus 로고
    • The starch-debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm
    • Kubo A, Fujita N, Harada K, Matsuda T, Satoh H, Nakamura Y (1999) The starch-debranching enzymes isoamylase and pullulanase are both involved in amylopectin biosynthesis in rice endosperm. Plant Physiol 121: 399-410
    • (1999) Plant Physiol , vol.121 , pp. 399-410
    • Kubo, A.1    Fujita, N.2    Harada, K.3    Matsuda, T.4    Satoh, H.5    Nakamura, Y.6
  • 20
    • 20844446623 scopus 로고    scopus 로고
    • Complementation of sugary-1 phenotype in rice endosperm with the wheat isoamylase1 gene supports a direct role for isoamylase1 in amylopectin biosynthesis
    • Kubo A, Rahman S, Utsumi Y, Li Z, Mukai Y, Yamamoto M, Ugaki M, Harada K, Satoh H, Konik-Rose C, et al (2005) Complementation of sugary-1 phenotype in rice endosperm with the wheat isoamylase1 gene supports a direct role for isoamylase1 in amylopectin biosynthesis. Plant Physiol 137: 43-56
    • (2005) Plant Physiol , vol.137 , pp. 43-56
    • Kubo, A.1    Rahman, S.2    Utsumi, Y.3    Li, Z.4    Mukai, Y.5    Yamamoto, M.6    Ugaki, M.7    Harada, K.8    Satoh, H.9    Konik-Rose, C.10
  • 21
    • 2342577446 scopus 로고    scopus 로고
    • Simple RNAi vectors for stable and transient suppression of gene function in rice
    • Miki D, 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
  • 22
    • 0031741515 scopus 로고    scopus 로고
    • Analysis of starch structure using fluorophore-assisted carbohydrate electrophoresis
    • Morell MK, Samuel MS, O'Shea MG (1998) Analysis of starch structure using fluorophore-assisted carbohydrate electrophoresis. Electrophoresis 19: 2603-2611
    • (1998) Electrophoresis , vol.19 , pp. 2603-2611
    • Morell, M.K.1    Samuel, M.S.2    O'Shea, M.G.3
  • 24
    • 0034003526 scopus 로고    scopus 로고
    • Recent progress toward understanding biosynthesis of the amylopectin crystal
    • Myers AM, Morell MK, James MG, Ball SG (2000) Recent progress toward understanding biosynthesis of the amylopectin crystal. Plant Physiol 122: 989-997
    • (2000) Plant Physiol , vol.122 , pp. 989-997
    • Myers, A.M.1    Morell, M.K.2    James, M.G.3    Ball, S.G.4
  • 25
    • 0036348660 scopus 로고    scopus 로고
    • Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: Rice endosperm as a model tissue
    • Nakamura Y (2002) Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: rice endosperm as a model tissue. Plant Cell Physiol 43: 718-725
    • (2002) Plant Cell Physiol , vol.43 , pp. 718-725
    • Nakamura, Y.1
  • 26
    • 0030814320 scopus 로고    scopus 로고
    • Correlation between activities of starch debranching enzyme and a-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 a-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
  • 28
    • 0000095135 scopus 로고
    • Carbohydrate metabolism in the developing endosperm of rice grains
    • Nakamura Y, Yuki K, Park SY, Ohya T (1989) Carbohydrate metabolism in the developing endosperm of rice grains. Plant Cell Physiol 30: 833-839
    • (1989) Plant Cell Physiol , vol.30 , pp. 833-839
    • Nakamura, Y.1    Yuki, K.2    Park, S.Y.3    Ohya, T.4
  • 29
    • 0034775955 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of the effects of amylose-extender mutation in rice endosperm
    • Nishi A, Nakamura Y, Tanaka N, Satoh H (2001) Biochemical and genetic analysis of the effects 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
  • 31
    • 62549154915 scopus 로고    scopus 로고
    • Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase
    • Streb S, Delatte T, Umhang M, Eicke S, Schorderet M, Reinhardt D, Zeeman SC (2008) Starch granule biosynthesis in Arabidopsis is abolished by removal of all debranching enzymes but restored by the subsequent removal of an endoamylase. Plant Cell 20: 3448-3466
    • (2008) Plant Cell , vol.20 , pp. 3448-3466
    • Streb, S.1    Delatte, T.2    Umhang, M.3    Eicke, S.4    Schorderet, M.5    Reinhardt, D.6    Zeeman, S.C.7
  • 32
    • 36148940638 scopus 로고    scopus 로고
    • Differential chain-length specificities of two isoamylase-type starchdebranching enzymes from developing seeds of kidney bean
    • Takashima Y, Senoura T, Yoshizaki T, Hamada S, Ito H, Matsui H (2007) Differential chain-length specificities of two isoamylase-type starchdebranching enzymes from developing seeds of kidney bean. Biosci Biotechnol Biochem 71: 2308-2312
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 2308-2312
    • Takashima, Y.1    Senoura, T.2    Yoshizaki, T.3    Hamada, S.4    Ito, H.5    Matsui, H.6
  • 33
    • 13444254113 scopus 로고    scopus 로고
    • The structure of starch can be manipulated by changing the expression levels of starch branching enzyme IIb in rice endosperm
    • Tanaka N, Fujita N, Nishi A, Satoh H, Hosaka Y, Ugaki M, Kawasaki S, Nakamura Y (2004) The structure of starch can be manipulated by changing the expression levels of starch branching enzyme IIb in rice endosperm. Plant Biotechnol J 2: 507-516
    • (2004) Plant Biotechnol J , vol.2 , pp. 507-516
    • Tanaka, N.1    Fujita, N.2    Nishi, A.3    Satoh, H.4    Hosaka, Y.5    Ugaki, M.6    Kawasaki, S.7    Nakamura, Y.8
  • 35
    • 0031524467 scopus 로고    scopus 로고
    • Rapid and efficient Agrobacterium-mediated transformation in rice
    • Toki S (1997) Rapid and efficient Agrobacterium-mediated transformation in rice. Plant Mol Biol Rep 15: 16-21
    • (1997) Plant Mol Biol Rep , vol.15 , pp. 16-21
    • Toki, S.1
  • 36
    • 33750967078 scopus 로고    scopus 로고
    • Structural and enzymatic characterization of the isoamylase1 homo-oligomer and the isoamylase1-isoamylase2 hetero-oligomer from rice endosperm
    • Utsumi Y, Nakamura Y (2006) Structural and enzymatic characterization of the isoamylase1 homo-oligomer and the isoamylase1-isoamylase2 hetero-oligomer from rice endosperm. Planta 225: 75-87
    • (2006) Planta , vol.225 , pp. 75-87
    • Utsumi, Y.1    Nakamura, Y.2
  • 37
    • 77952352709 scopus 로고    scopus 로고
    • Quantitative assay method for starch branching enzyme with bicinchoninic acid by measuring the reducing terminals of glucans
    • Utsumi Y, Yoshida M, Francisco PB Jr, Sawada T, Kitamura S, Yasunori N (2009) Quantitative assay method for starch branching enzyme with bicinchoninic acid by measuring the reducing terminals of glucans. J Appl Glycosci 56: 215-222
    • (2009) J Appl Glycosci , vol.56 , pp. 215-222
    • Utsumi, Y.1    Yoshida, M.2    Francisco Jr., P.B.3    Sawada, T.4    Kitamura, S.5    Yasunori, N.6
  • 39
    • 57749084358 scopus 로고    scopus 로고
    • Further evidence for the mandatory nature of polysaccharide debranching for the aggregation of semicrystalline starch and for overlapping functions of debranching enzymes in Arabidopsis leaves
    • Wattebled F, Planchot V, Dong Y, Szydlowski N, Pontoire B, Devin A, Ball S, D'Hulst C (2008) Further evidence for the mandatory nature of polysaccharide debranching for the aggregation of semicrystalline starch and for overlapping functions of debranching enzymes in Arabidopsis leaves. Plant Physiol 148: 1309-1323
    • (2008) Plant Physiol , vol.148 , pp. 1309-1323
    • Wattebled, F.1    Planchot, V.2    Dong, Y.3    Szydlowski, N.4    Pontoire, B.5    Devin, A.6    Ball, S.7    D'Hulst, C.8
  • 40
    • 0037364714 scopus 로고    scopus 로고
    • Structures and properties of amylopectin and phytoglycogen in the endosperm of sugary-1 mutants of rice
    • Wong K, Kubo A, Jane J, Harada K, Satoh H, Nakamura Y (2003) Structures and properties of amylopectin and phytoglycogen in the endosperm of sugary-1 mutants of rice. J Cereal Sci 37: 139-149
    • (2003) J Cereal Sci , vol.37 , pp. 139-149
    • Wong, K.1    Kubo, A.2    Jane, J.3    Harada, K.4    Satoh, H.5    Nakamura, Y.6


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