메뉴 건너뛰기




Volumn 43, Issue 9, 2005, Pages 821-827

Isolation and characterization of an α-amylase gene in cassava (Manihot esculenta)

Author keywords

Amylase; Cassava; Phytohormones; Starch degradation

Indexed keywords

AMYLASE; PRIMER DNA;

EID: 28444434741     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2005.07.014     Document Type: Article
Times cited : (32)

References (40)
  • 2
    • 0033621108 scopus 로고    scopus 로고
    • Rice gibberellin-insensitive dwarf mutant gene Dwarf 1 encodes the α-subunit of GTP-binding protein
    • M. Ashikari, J. Wu, M. Yano, T. Sasaki, and A. Yoshimura Rice gibberellin-insensitive dwarf mutant gene Dwarf 1 encodes the α-subunit of GTP-binding protein Proc. Natl. Acad. Sci. USA 96 1999 10284 10289
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10284-10289
    • Ashikari, M.1    Wu, J.2    Yano, M.3    Sasaki, T.4    Yoshimura, A.5
  • 4
    • 0006203382 scopus 로고    scopus 로고
    • Effects of gibberellic acid and environmental factors on cytosolic calcium in wheat aleurone cells
    • D.S. Bush Effects of gibberellic acid and environmental factors on cytosolic calcium in wheat aleurone cells Planta 199 1996 89 99
    • (1996) Planta , vol.199 , pp. 89-99
    • Bush, D.S.1
  • 5
    • 0000543592 scopus 로고
    • Carbohydrate metabolism during sprouting
    • H. Davies Carbohydrate metabolism during sprouting Am. Potato J. 67 1990 815 827
    • (1990) Am. Potato J. , vol.67 , pp. 815-827
    • Davies, H.1
  • 6
    • 20444430710 scopus 로고
    • Hydrolytic and phosphorolytic enzyme activity and reserve mobilisation in sprouting tubers of potato (Solanum tuberosum L)
    • H. Davies, and H. Ross Hydrolytic and phosphorolytic enzyme activity and reserve mobilisation in sprouting tubers of potato (Solanum tuberosum L) J. Plant Physiol. 126 1986 379 386
    • (1986) J. Plant Physiol. , vol.126 , pp. 379-386
    • Davies, H.1    Ross, H.2
  • 7
    • 0000479431 scopus 로고
    • Isolation of plant DNA from fresh tissue
    • J.J. Doyle, and J.L. Doyle Isolation of plant DNA from fresh tissue Focus 12 1990 13 15
    • (1990) Focus , vol.12 , pp. 13-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 8
    • 0000860075 scopus 로고
    • Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains
    • G. Fincher Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains Annu. Rev. Plant Physiol. Plant Mol. Biol. 40 1989 350 356
    • (1989) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.40 , pp. 350-356
    • Fincher, G.1
  • 9
    • 0028812455 scopus 로고
    • Reorientation of cortical microtubules in the sub-apical region during tuberization in single note stem segments of potato in culture
    • K. Fujino, Y. Koda, and Y. Kikuta Reorientation of cortical microtubules in the sub-apical region during tuberization in single note stem segments of potato in culture Plant Cell Physiol. 36 1995 891 895
    • (1995) Plant Cell Physiol. , vol.36 , pp. 891-895
    • Fujino, K.1    Koda, Y.2    Kikuta, Y.3
  • 10
    • 0028100243 scopus 로고
    • Perception of gibberellin and abscisic acid at the external face of the plasma membrane of barley (Hordeum vulgare L.)
    • S. Gilroy, and R.L. Jones Perception of gibberellin and abscisic acid at the external face of the plasma membrane of barley (Hordeum vulgare L.) aleurone protoplasts. Plant Physiol. 104 1994 1185 1192
    • (1994) Aleurone Protoplasts. Plant Physiol. , vol.104 , pp. 1185-1192
    • Gilroy, S.1    Jones, R.L.2
  • 11
    • 0033573898 scopus 로고    scopus 로고
    • An abscisic acid-induced protein kinase, PKABA1, mediates abscisic acid-suppressed gene expression in barley aleurone layers
    • A. Gomez-Cadenas, S.D. Verhey, L.D. Holappa, Q. Shen, T.H. Ho, and M.K. Walker-Simmons An abscisic acid-induced protein kinase, PKABA1, mediates abscisic acid-suppressed gene expression in barley aleurone layers Proc. Natl. Acad. Sci. USA 96 1999 1767 1772
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1767-1772
    • Gomez-Cadenas, A.1    Verhey, S.D.2    Holappa, L.D.3    Shen, Q.4    Ho, T.H.5    Walker-Simmons, M.K.6
  • 12
    • 0029410792 scopus 로고
    • Gibberellin-regulated expression of a myb gene in barley aleurone cells: Evidence for Myb transactivation of a high-pI α-amylase gene promoter
    • F. Gubler, R. Kalla, J.K. Roberts, and J.V. Jacobsen Gibberellin- regulated expression of a myb gene in barley aleurone cells: evidence for Myb transactivation of a high-pI α-amylase gene promoter Plant Cell 7 1995 1879 1891
    • (1995) Plant Cell , vol.7 , pp. 1879-1891
    • Gubler, F.1    Kalla, R.2    Roberts, J.K.3    Jacobsen, J.V.4
  • 13
    • 0028878441 scopus 로고
    • Effect of Anoxia on Carbohydrate Metabolism in Rice Seedlings
    • L. Guglielminetti, P. Perata, and A. Alpi Effect of Anoxia on Carbohydrate Metabolism in Rice Seedlings Plant Physiol. 108 1995 735 741
    • (1995) Plant Physiol. , vol.108 , pp. 735-741
    • Guglielminetti, L.1    Perata, P.2    Alpi, A.3
  • 14
    • 0025429268 scopus 로고
    • Classification and characterization of the rice α-amylase multigene family
    • N. Huang, T.D. Sutliff, J.C. Litts, and R.L. Rodriguez Classification and characterization of the rice α-amylase multigene family Plant Mol. Biol. 14 1990 655 668
    • (1990) Plant Mol. Biol. , vol.14 , pp. 655-668
    • Huang, N.1    Sutliff, T.D.2    Litts, J.C.3    Rodriguez, R.L.4
  • 15
    • 0030500409 scopus 로고    scopus 로고
    • Control of tuberization in potato by gibberellins and phytochrome B
    • S. Jackson, and S. Prat Control of tuberization in potato by gibberellins and phytochrome B Physiol. Plant. 98 1996 407 412
    • (1996) Physiol. Plant. , vol.98 , pp. 407-412
    • Jackson, S.1    Prat, S.2
  • 16
    • 0030920242 scopus 로고    scopus 로고
    • Photoreceptors and signals in the photoperiodic control of development
    • S. Jackson, and B. Thomas Photoreceptors and signals in the photoperiodic control of development Plant Cell Environ. 20 1997 790 795
    • (1997) Plant Cell Environ. , vol.20 , pp. 790-795
    • Jackson, S.1    Thomas, B.2
  • 17
    • 0033025132 scopus 로고    scopus 로고
    • Close evolutionary relatedness of alpha-amylases from Archaea and plants
    • S. Janecek, E. Leveque, A. Belarbi, and B. Haye Close evolutionary relatedness of alpha-amylases from Archaea and plants J. Mol. Evol. 48 1999 421 426
    • (1999) J. Mol. Evol. , vol.48 , pp. 421-426
    • Janecek, S.1    Leveque, E.2    Belarbi, A.3    Haye, B.4
  • 18
    • 0027740009 scopus 로고
    • Starch- and glycogen-debranching and branching enzymes: Prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes
    • H.M. Jespersen, E.A. MacGregor, B. Henrissat, M.R. Sierks, and B. Svensson Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes J. Protein Chem. 12 1993 791 805
    • (1993) J. Protein Chem. , vol.12 , pp. 791-805
    • Jespersen, H.M.1    MacGregor, E.A.2    Henrissat, B.3    Sierks, M.R.4    Svensson, B.5
  • 19
    • 0025784036 scopus 로고
    • Regulation of synthesis and transport of secreted proteins in cereal aleurone
    • R.L. Jones, and J.V. Jacobsen Regulation of synthesis and transport of secreted proteins in cereal aleurone Int. Rev. Cytol. 126 1991 49 88
    • (1991) Int. Rev. Cytol. , vol.126 , pp. 49-88
    • Jones, R.L.1    Jacobsen, J.V.2
  • 20
    • 0028229326 scopus 로고
    • Crystal and molecular structure of barley α-amylase
    • A. Kadziola, J. Abe, B. Svensson, and R. Haser Crystal and molecular structure of barley α-amylase J. Mol. Biol. 239 1994 104 121
    • (1994) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Abe, J.2    Svensson, B.3    Haser, R.4
  • 21
    • 0032562777 scopus 로고    scopus 로고
    • Molecular structure of a barley alpha-amylase-inhibitor complex: Implications for starch binding and catalysis
    • A. Kadziola, M. Sogaard, B. Svensson, and R. Haser Molecular structure of a barley alpha-amylase-inhibitor complex: implications for starch binding and catalysis J. Mol. Biol. 278 1998 205 217
    • (1998) J. Mol. Biol. , vol.278 , pp. 205-217
    • Kadziola, A.1    Sogaard, M.2    Svensson, B.3    Haser, R.4
  • 23
    • 0036010650 scopus 로고    scopus 로고
    • The alpha-amylase induction in endosperm during rice seed germination is caused by gibberellin synthesized in epithelium
    • M. Kaneko, H. Itoh, M. Ueguchi-Tanaka, M. Ashikari, and M. Matsuoka The alpha-amylase induction in endosperm during rice seed germination is caused by gibberellin synthesized in epithelium Plant Physiol. 128 2002 1264 1270
    • (2002) Plant Physiol. , vol.128 , pp. 1264-1270
    • Kaneko, M.1    Itoh, H.2    Ueguchi-Tanaka, M.3    Ashikari, M.4    Matsuoka, M.5
  • 24
    • 0026166257 scopus 로고
    • Differential expression of α-amylase genes in germinating rice and barley seeds
    • E.E. Karrer, J.C. Litts, and R.L. Rodriguez Differential expression of α-amylase genes in germinating rice and barley seeds Plant Mol. Biol. 16 1991 797 805
    • (1991) Plant Mol. Biol. , vol.16 , pp. 797-805
    • Karrer, E.E.1    Litts, J.C.2    Rodriguez, R.L.3
  • 26
    • 0034162708 scopus 로고    scopus 로고
    • Gibberellin and abscisic acid signalling in aleurone
    • A. Lovegrove, and R. Hooley Gibberellin and abscisic acid signalling in aleurone Trends Plant Sci. 5 2000 102 110
    • (2000) Trends Plant Sci. , vol.5 , pp. 102-110
    • Lovegrove, A.1    Hooley, R.2
  • 28
    • 0026739736 scopus 로고
    • Artifactual detection of ADP-dependent sucrose synthase in crude plant extracts
    • P. Perata, J. Pozueta-Romero, J. Yamaguchi, and T. Akazawa Artifactual detection of ADP-dependent sucrose synthase in crude plant extracts FEBS Lett. 309 1992 283 287
    • (1992) FEBS Lett. , vol.309 , pp. 283-287
    • Perata, P.1    Pozueta-Romero, J.2    Yamaguchi, J.3    Akazawa, T.4
  • 29
    • 0001487359 scopus 로고
    • Chromosomal localization and genomic organization of α-amylase genes in rice
    • S. Ranjhan, J. Litts, M. Foolad, and R.L. Rodriguez Chromosomal localization and genomic organization of α-amylase genes in rice Theor. Appl. Genet. 82 1991 481 488
    • (1991) Theor. Appl. Genet. , vol.82 , pp. 481-488
    • Ranjhan, S.1    Litts, J.2    Foolad, M.3    Rodriguez, R.L.4
  • 30
    • 0001176645 scopus 로고    scopus 로고
    • Calcium-dependent protein phosphorylation may mediate the gibberellic acid response in barley aleurone
    • S. Ritchie, and S. Gilroy Calcium-dependent protein phosphorylation may mediate the gibberellic acid response in barley aleurone Plant Physiol. 116 1998 765 776
    • (1998) Plant Physiol. , vol.116 , pp. 765-776
    • Ritchie, S.1    Gilroy, S.2
  • 31
    • 0032100903 scopus 로고    scopus 로고
    • Identification of a negative regulator of gibberellin action, HvSPY, in barley
    • M. Robertson, S.M. Swain, P.M. Chandler, and N.E. Olszewski Identification of a negative regulator of gibberellin action, HvSPY, in barley Plant Cell 10 1998 995 1007
    • (1998) Plant Cell , vol.10 , pp. 995-1007
    • Robertson, M.1    Swain, S.M.2    Chandler, P.M.3    Olszewski, N.E.4
  • 32
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 33
    • 0027134235 scopus 로고
    • Regulation by gibberellins of the orientation of cortical microtubules in plant cells
    • H. Shibaoka Regulation by gibberellins of the orientation of cortical microtubules in plant cells Aust. J. Plant Physiol. 20 1993 461 470
    • (1993) Aust. J. Plant Physiol. , vol.20 , pp. 461-470
    • Shibaoka, H.1
  • 35
    • 0027425535 scopus 로고
    • Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1
    • M. Sogaard, A. Kadziola, R. Haser, and B. Svensson Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1 J. Biol. Chem. 268 1993 22480 22484
    • (1993) J. Biol. Chem. , vol.268 , pp. 22480-22484
    • Sogaard, M.1    Kadziola, A.2    Haser, R.3    Svensson, B.4
  • 37
    • 0032724933 scopus 로고    scopus 로고
    • Gibberellin signal transduction presents ellipsisthe SPY who O-GlcNAc'd me
    • T.M. Thornton, S.M. Swain, and N.E. Olszewski Gibberellin signal transduction presents ellipsisthe SPY who O-GlcNAc'd me Trends Plant Sci. 4 1999 424 428
    • (1999) Trends Plant Sci. , vol.4 , pp. 424-428
    • Thornton, T.M.1    Swain, S.M.2    Olszewski, N.E.3
  • 38
    • 0026199290 scopus 로고
    • Isolation and analysis of cDNA encoding the 33:kDa precursor protein of the oxygen-evolving complex of potato
    • M. van Spanje, W.G. Dirkse, J.P. Nap, and W.J. Stiekema Isolation and analysis of cDNA encoding the 33:kDa precursor protein of the oxygen-evolving complex of potato Plant Mol. Biol. 17 1991 157 160
    • (1991) Plant Mol. Biol. , vol.17 , pp. 157-160
    • Van Spanje, M.1    Dirkse, W.G.2    Nap, J.P.3    Stiekema, W.J.4
  • 39
    • 0034014178 scopus 로고    scopus 로고
    • A novel α-amylase gene is transiently upregulated during low temperature exposure in apple fruit
    • T. Wegrzyn, K. Reilly, G. Cipriani, P. Murphy, R. Newcomb, R. Gardner, and E. MacRae A novel α-amylase gene is transiently upregulated during low temperature exposure in apple fruit Eur. J. Biochem. 267 2000 1313 1322
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1313-1322
    • Wegrzyn, T.1    Reilly, K.2    Cipriani, G.3    Murphy, P.4    Newcomb, R.5    Gardner, R.6    MacRae, E.7
  • 40
    • 0028447769 scopus 로고
    • Structure and expression of α-amylase gene from Vigna mungo
    • D. Yamauchi, H. Takeuchi, and T. Minamikawa Structure and expression of α-amylase gene from Vigna mungo Plant Cell Physiol. 35 1994 705 711
    • (1994) Plant Cell Physiol. , vol.35 , pp. 705-711
    • Yamauchi, D.1    Takeuchi, H.2    Minamikawa, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.