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Volumn 162, Issue 10, 2005, Pages 1077-1086

Isolation of cDNA and enzymatic properties of betaine aldehyde dehydrogenase from Zoysia tenuifolia

Author keywords

Amino aldehyde dehydrogenase; Enzyme activity; Zoysia tenuifolia

Indexed keywords

ALDEHYDES; AMINO ACIDS; CLONING; ENZYMES; ESCHERICHIA COLI; PH EFFECTS;

EID: 24944548596     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jplph.2005.01.020     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 0037285326 scopus 로고    scopus 로고
    • Pea seedling aminoaldehyde dehydrogenase: Primary structure and active site residues
    • F. Brauner, M. Sebela, J. Snegaroff, P. Pec, and J. Meunier Pea seedling aminoaldehyde dehydrogenase: primary structure and active site residues Plant Physiol Biochem 41 2003 1 10
    • (2003) Plant Physiol Biochem , vol.41 , pp. 1-10
    • Brauner, F.1    Sebela, M.2    Snegaroff, J.3    Pec, P.4    Meunier, J.5
  • 2
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • P. Chomczynski, and N. Sacchi Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction Anal Biochem 162 1987 156 159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 3
    • 0021016329 scopus 로고
    • A simple and very efficient method for generating cDNA libraries
    • U. Gubler, and B.J. Hoffman A simple and very efficient method for generating cDNA libraries Gene 25 1983 263 269
    • (1983) Gene , vol.25 , pp. 263-269
    • Gubler, U.1    Hoffman, B.J.2
  • 4
    • 0034958914 scopus 로고    scopus 로고
    • Mitochondrial adaptations to NaCl: Complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine
    • E.W. Hamilton Jr, and S.A. Heckathorn Mitochondrial adaptations to NaCl: complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine Plant Physiol 126 2001 1266 1274
    • (2001) Plant Physiol , vol.126 , pp. 1266-1274
    • Hamilton Jr., E.W.1    Heckathorn, S.A.2
  • 5
    • 0031154927 scopus 로고    scopus 로고
    • Changes in targeting efficiencies of proteins to plant microbodies caused by amino acid substitutions in the carboxy-terminal tripeptide
    • M. Hayashi, M. Aoki, M. Kondo, and M. Nishimura Changes in targeting efficiencies of proteins to plant microbodies caused by amino acid substitutions in the carboxy-terminal tripeptide Plant Cell Physiol 38 1997 759 768
    • (1997) Plant Cell Physiol , vol.38 , pp. 759-768
    • Hayashi, M.1    Aoki, M.2    Kondo, M.3    Nishimura, M.4
  • 6
    • 0035078248 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of two kinds of betaine-aldehyde dehydrogenase in betaine-accumulating mangrove Avicennia marina (Forsk.) Vierh
    • T. Hibino, Y.L. Meng, Y. Kawamitsu, N. Uehara, N. Matsuda, Y. Tanaka, H. Ishikawa, S. Baba, and T. Takabe Molecular cloning and functional characterization of two kinds of betaine-aldehyde dehydrogenase in betaine-accumulating mangrove Avicennia marina (Forsk.) Vierh Plant Mol Biol 45 2001 353 363
    • (2001) Plant Mol Biol , vol.45 , pp. 353-363
    • Hibino, T.1    Meng, Y.L.2    Kawamitsu, Y.3    Uehara, N.4    Matsuda, N.5    Tanaka, Y.6    Ishikawa, H.7    Baba, S.8    Takabe, T.9
  • 7
    • 0034531927 scopus 로고    scopus 로고
    • Overproduction of spinach betaine aldehyde dehydrogenase in Escherichia coli: Structural and functional properties of wild-type, mutants and e coli. enzymes
    • A. Incharoensakdi, N. Matsuda, T. Hibino, Y.L. Meng, H. Ishikawa, A. Hara, T. Funaguma, T. Takabe, and T. Takabe Overproduction of spinach betaine aldehyde dehydrogenase in Escherichia coli: structural and functional properties of wild-type, mutants and E coli. enzymes Eur J Biochem 267 2000 7015 7023
    • (2000) Eur J Biochem , vol.267 , pp. 7015-7023
    • Incharoensakdi, A.1    Matsuda, N.2    Hibino, T.3    Meng, Y.L.4    Ishikawa, H.5    Hara, A.6    Funaguma, T.7    Takabe, T.8    Takabe, T.9
  • 8
    • 0029110729 scopus 로고
    • Expression of the betaine aldehyde dehydrogenase gene in barley in response to osmotic stress and abscisic acid
    • M. Ishitani, T. Nakamura, S.Y. Han, and T. Takabe Expression of the betaine aldehyde dehydrogenase gene in barley in response to osmotic stress and abscisic acid Plant Mol Biol 27 1995 307 315
    • (1995) Plant Mol Biol , vol.27 , pp. 307-315
    • Ishitani, M.1    Nakamura, T.2    Han, S.Y.3    Takabe, T.4
  • 10
    • 0042329725 scopus 로고    scopus 로고
    • Cloning of cDNA encoding choline monooxygenase from Suaeda liaotungensis and salt tolerance of transgenic tobacco
    • Q.L. Li, D.W. Liu, X.R. Gao, Q. Su, and L.J. An Cloning of cDNA encoding choline monooxygenase from Suaeda liaotungensis and salt tolerance of transgenic tobacco Acta Bot Sin 45 2003 242 247
    • (2003) Acta Bot Sin , vol.45 , pp. 242-247
    • Li, Q.L.1    Liu, D.W.2    Gao, X.R.3    Su, Q.4    An, L.J.5
  • 13
    • 0032794863 scopus 로고    scopus 로고
    • Salinity tolerance mechanisms of grasses in the subfamily Chloridoideae
    • K.B. Marcum Salinity tolerance mechanisms of grasses in the subfamily Chloridoideae Crop Sci 39 1999 1153 1160
    • (1999) Crop Sci , vol.39 , pp. 1153-1160
    • Marcum, K.B.1
  • 14
    • 0027947198 scopus 로고
    • Salinity tolerance mechanisms of six C4 turfgrasses
    • K.B. Marcum, and C.L. Murdoch Salinity tolerance mechanisms of six C 4 turfgrasses J Am Soc Hortic Sci 119 1994 779 784
    • (1994) J Am Soc Hortic Sci , vol.119 , pp. 779-784
    • Marcum, K.B.1    Murdoch, C.L.2
  • 15
    • 0026477598 scopus 로고
    • Salt-inducible betaine aldehyde dehydrogenase from sugar beet: CDNA cloning and expression
    • K.F. McCue, and A.D. Hanson Salt-inducible betaine aldehyde dehydrogenase from sugar beet: cDNA cloning and expression Plant Mol Biol 18 1992 1 11
    • (1992) Plant Mol Biol , vol.18 , pp. 1-11
    • McCue, K.F.1    Hanson, A.D.2
  • 16
    • 0036204455 scopus 로고    scopus 로고
    • Purification and properties of betaine aldehyde dehydrogenase with high affinity for NADP from Arthrobacter globiformis
    • N. Mori, S. Fuchigami, and Y. Kitamoto Purification and properties of betaine aldehyde dehydrogenase with high affinity for NADP from Arthrobacter globiformis J Biosci Bioeng 93 2002 130 135
    • (2002) J Biosci Bioeng , vol.93 , pp. 130-135
    • Mori, N.1    Fuchigami, S.2    Kitamoto, Y.3
  • 17
    • 0026649768 scopus 로고
    • Purification and properties of betaine aldehyde dehydrogenase from Xanthomonas translucens
    • N. Mori, N. Yoshida, and Y. Kitamoto Purification and properties of betaine aldehyde dehydrogenase from Xanthomonas translucens J Ferment Bioeng 73 1992 352 356
    • (1992) J Ferment Bioeng , vol.73 , pp. 352-356
    • Mori, N.1    Yoshida, N.2    Kitamoto, Y.3
  • 18
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • M.G. Murray, and W.F. Thompson Rapid isolation of high molecular weight plant DNA Nucleic Acids Res 8 1980 4321 4325
    • (1980) Nucleic Acids Res , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 20
    • 0031149153 scopus 로고    scopus 로고
    • Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes
    • T. Nakamura, S. Yokota, Y. Muramoto, K. Tsutsui, Y. Oguri, K. Fukui, and T. Takabe Expression of a betaine aldehyde dehydrogenase gene in rice, a glycinebetaine nonaccumulator, and possible localization of its protein in peroxisomes Plant J 11 1997 1115 1120
    • (1997) Plant J , vol.11 , pp. 1115-1120
    • Nakamura, T.1    Yokota, S.2    Muramoto, Y.3    Tsutsui, K.4    Oguri, Y.5    Fukui, K.6    Takabe, T.7
  • 21
    • 0031924117 scopus 로고    scopus 로고
    • Transgenically produced glycinebetaine protects ribulose 1,5-bisphosphate carboxylase/oxygenase from inactivation in Synechococcus sp. PCC7942 under salt stress
    • M. Nomura, T. Hibino, T. Takabe, T. Sugiyama, A. Yokota, H. Miyake, and T. Takabe Transgenically produced glycinebetaine protects ribulose 1,5-bisphosphate carboxylase/oxygenase from inactivation in Synechococcus sp. PCC7942 under salt stress Plant Cell Physiol 39 1998 425 432
    • (1998) Plant Cell Physiol , vol.39 , pp. 425-432
    • Nomura, M.1    Hibino, T.2    Takabe, T.3    Sugiyama, T.4    Yokota, A.5    Miyake, H.6    Takabe, T.7
  • 23
    • 0001190173 scopus 로고
    • Betaine accumulation and betaine-aldehyde dehydrogenase in spinach leaves
    • S.M. Pan, R.A. Moreau, C. Yu, and A.H.C. Huang Betaine accumulation and betaine-aldehyde dehydrogenase in spinach leaves Plant Physiol 67 1981 1105 1108
    • (1981) Plant Physiol , vol.67 , pp. 1105-1108
    • Pan, S.M.1    Moreau, R.A.2    Yu, C.3    Huang, A.H.C.4
  • 24
    • 0028794805 scopus 로고
    • The unusually strong stabilizing effects of glycine betaine on the structure and function of the oxygen-evolving photosystem II complex
    • G.C. Papageorgiou, and N. Murata The unusually strong stabilizing effects of glycine betaine on the structure and function of the oxygen-evolving photosystem II complex Photosynth Res 44 1995 243 252
    • (1995) Photosynth Res , vol.44 , pp. 243-252
    • Papageorgiou, G.C.1    Murata, N.2
  • 25
    • 0030970522 scopus 로고    scopus 로고
    • Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning
    • B. Rathinasabapathi, M. Burnet, B.L. Russell, D.A. Gage, P.C. Liao, G.J. Nye, P. Scott, J.H. Golbeck, and A.D. Hanson Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: prosthetic group characterization and cDNA cloning Proc Natl Acad Sci USA 94 1997 3454 3458
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3454-3458
    • Rathinasabapathi, B.1    Burnet, M.2    Russell, B.L.3    Gage, D.A.4    Liao, P.C.5    Nye, G.J.6    Scott, P.7    Golbeck, J.H.8    Hanson, A.D.9
  • 26
    • 0027962805 scopus 로고
    • Metabolic engineering of glycine betaine synthesis: Plant betaine aldehyde dehydrogenases lacking typical transit peptides are targeted to tobacco chloroplasts where they confer betaine aldehyde resistance
    • B. Rathinasabapathi, K.F. McCue, D.A. Gage, and A.D. Hanson Metabolic engineering of glycine betaine synthesis: plant betaine aldehyde dehydrogenases lacking typical transit peptides are targeted to tobacco chloroplasts where they confer betaine aldehyde resistance Planta 193 1994 155 162
    • (1994) Planta , vol.193 , pp. 155-162
    • Rathinasabapathi, B.1    McCue, K.F.2    Gage, D.A.3    Hanson, A.D.4
  • 27
    • 6244268962 scopus 로고
    • Quaternary ammonium and tertiary sulfonium compounds in higher plants
    • D. Rhodes, and A.D. Hanson Quaternary ammonium and tertiary sulfonium compounds in higher plants Annu Rev Plant Physiol Plant Mol Biol 44 1993 357 384
    • (1993) Annu Rev Plant Physiol Plant Mol Biol , vol.44 , pp. 357-384
    • Rhodes, D.1    Hanson, A.D.2
  • 28
    • 0031989203 scopus 로고    scopus 로고
    • Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth
    • B.L. Russell, B. Rathinasabapathi, and A.D. Hanson Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth Plant Physiol 116 1998 859 865
    • (1998) Plant Physiol , vol.116 , pp. 859-865
    • Russell, B.L.1    Rathinasabapathi, B.2    Hanson, A.D.3
  • 30
    • 0036944976 scopus 로고    scopus 로고
    • AhCMO, regulated by stresses in Atriplex hortensis, can improve drought tolerance in transgenic tobacco
    • Y.G. Shen, B.X. Du, W.K. Zhang, J.S. Zhang, and S.Y. Chen AhCMO, regulated by stresses in Atriplex hortensis, can improve drought tolerance in transgenic tobacco Theor Appl Genet 105 2002 815 821
    • (2002) Theor Appl Genet , vol.105 , pp. 815-821
    • Shen, Y.G.1    Du, B.X.2    Zhang, W.K.3    Zhang, J.S.4    Chen, S.Y.5
  • 31
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res 24 1997 4876 4882
    • (1997) Nucleic Acids Res , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 32
    • 0030908412 scopus 로고    scopus 로고
    • Transgenically expressed betaine aldehyde dehydrogenase efficiently catalyzes oxidation of dimethylsulfoniopropinaldehyde and ω-aminoaldehydes
    • C. Trossat, B. Rathinasabapathi, and A.D. Hanson Transgenically expressed betaine aldehyde dehydrogenase efficiently catalyzes oxidation of dimethylsulfoniopropinaldehyde and ω-aminoaldehydes Plant Physiol 113 1997 1457 1461
    • (1997) Plant Physiol , vol.113 , pp. 1457-1461
    • Trossat, C.1    Rathinasabapathi, B.2    Hanson, A.D.3
  • 33
    • 0028050884 scopus 로고
    • Purification and properties of betaine aldehyde dehydrogenase extracted from detached leaves of Amaranthus hypochondriacus L. subjected to water deficit
    • E.M. Valenzuela-Soto, and R.A. Muñoz-Clares Purification and properties of betaine aldehyde dehydrogenase extracted from detached leaves of Amaranthus hypochondriacus L. subjected to water deficit J Plant Physiol 143 1994 145 152
    • (1994) J Plant Physiol , vol.143 , pp. 145-152
    • Valenzuela-Soto, E.M.1    Muñoz-Clares, R.A.2
  • 34
    • 0031005273 scopus 로고    scopus 로고
    • Betaine-aldehyde dehydrogenase from Amaranth leaves efficiently catalyzes the NAD-dependent oxidation of dimethylsulfoniopropionaldehyde to dimethylsulfoniopropionate
    • M. Vojtechová, A.D. Hanson, and R.A. Muñoz-Clares Betaine-aldehyde dehydrogenase from Amaranth leaves efficiently catalyzes the NAD-dependent oxidation of dimethylsulfoniopropionaldehyde to dimethylsulfoniopropionate Arch Biochem Biophys 337 1997 81 88
    • (1997) Arch Biochem Biophys , vol.337 , pp. 81-88
    • Vojtechová, M.1    Hanson, A.D.2    Muñoz-Clares, R.A.3
  • 35
    • 0031128078 scopus 로고    scopus 로고
    • Polyamines: Small molecules triggering pathways in plant growth and development
    • R. Walden, A. Cordeiro, and A.F. Tiburcio Polyamines: small molecules triggering pathways in plant growth and development Plant Physiol 113 1997 1009 1013
    • (1997) Plant Physiol , vol.113 , pp. 1009-1013
    • Walden, R.1    Cordeiro, A.2    Tiburcio, A.F.3
  • 36
    • 0001586272 scopus 로고
    • Betaine aldehyde oxidation by spinach chloroplasts
    • P. Weigel, E.A. Weretilnyk, and A.D. Hanson Betaine aldehyde oxidation by spinach chloroplasts Plant Physiol 82 1986 753 759
    • (1986) Plant Physiol , vol.82 , pp. 753-759
    • Weigel, P.1    Weretilnyk, E.A.2    Hanson, A.D.3
  • 37
    • 0025270591 scopus 로고
    • Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought
    • E.A. Weretilnyk, and A.D. Hanson Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought Proc Natl Acad Sci USA 87 1990 2745 2749
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2745-2749
    • Weretilnyk, E.A.1    Hanson, A.D.2
  • 38
    • 0030113389 scopus 로고    scopus 로고
    • Betaine aldehyde dehydrogenase in sorghum: Molecular cloning and expression of two related genes
    • A.J. Wood, H. Saneoka, D. Rhodes, R.J. Joly, and P.B. Goldsbrough Betaine aldehyde dehydrogenase in sorghum: molecular cloning and expression of two related genes Plant Physiol 110 1996 1301 1308
    • (1996) Plant Physiol , vol.110 , pp. 1301-1308
    • Wood, A.J.1    Saneoka, H.2    Rhodes, D.3    Joly, R.J.4    Goldsbrough, P.B.5
  • 39
    • 0032959586 scopus 로고    scopus 로고
    • Allotetraploidy of Zoysia species with 2n = 40 based on a RFLP genetic map
    • M. Yaneshita, S. Kaneko, and T. Sasakuma Allotetraploidy of Zoysia species with 2n = 40 based on a RFLP genetic map Theor Appl Genet 98 1999 751 756
    • (1999) Theor Appl Genet , vol.98 , pp. 751-756
    • Yaneshita, M.1    Kaneko, S.2    Sasakuma, T.3


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