메뉴 건너뛰기




Volumn 164, Issue 9, 2007, Pages 1208-1219

Cloning, functional identification and structural modelling of Vitis vinifera S-adenosylmethionine decarboxylase

Author keywords

Grapevine; Homology modelling; Polyamines; S adenosylmethionine decarboxylase; Vitis vinifera

Indexed keywords

AMINES; CLONING; MOLECULAR STRUCTURE; PLANTS (BOTANY);

EID: 34547743197     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jplph.2006.07.009     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0035089142 scopus 로고    scopus 로고
    • Biosynthesis, oxidation and conjugation of aliphatic polyamines in higher plants
    • Bagni N., and Tassoni A. Biosynthesis, oxidation and conjugation of aliphatic polyamines in higher plants. Amino Acids 20 (2001) 301-317
    • (2001) Amino Acids , vol.20 , pp. 301-317
    • Bagni, N.1    Tassoni, A.2
  • 2
    • 0037058821 scopus 로고    scopus 로고
    • Monomeric S-adenosylmethionine decarboxylase from plants provides an alternative to putrescine stimulation
    • Bennett E.M., Ekstrom J.L., Pegg A.E., and Ealick S.E. Monomeric S-adenosylmethionine decarboxylase from plants provides an alternative to putrescine stimulation. Biochemistry 41 (2002) 14509-14517
    • (2002) Biochemistry , vol.41 , pp. 14509-14517
    • Bennett, E.M.1    Ekstrom, J.L.2    Pegg, A.E.3    Ealick, S.E.4
  • 3
    • 1842434456 scopus 로고    scopus 로고
    • Polyamines and somatic embryogenesis in two Vitis vinifera cultivars
    • Bertoldi D., Tassoni A., Martinelli L., and Bagni N. Polyamines and somatic embryogenesis in two Vitis vinifera cultivars. Physiol Plant 120 (2004) 657-666
    • (2004) Physiol Plant , vol.120 , pp. 657-666
    • Bertoldi, D.1    Tassoni, A.2    Martinelli, L.3    Bagni, N.4
  • 4
    • 51249169259 scopus 로고
    • A simple and efficient method for isolating RNA from pine trees
    • Chang S., Puryear J., and Cairney J. A simple and efficient method for isolating RNA from pine trees. Plant Mol Rep 11 (1993) 113-116
    • (1993) Plant Mol Rep , vol.11 , pp. 113-116
    • Chang, S.1    Puryear, J.2    Cairney, J.3
  • 6
    • 0035859781 scopus 로고    scopus 로고
    • Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant
    • Ekstrom J.L., Tolbert W.D., Xiong H., Pegg A.E., and Ealick S.E. Structure of a human S-adenosylmethionine decarboxylase self-processing ester intermediate and mechanism of putrescine stimulation of processing as revealed by the H243A mutant. Biochemistry 40 (2001) 9495-9504
    • (2001) Biochemistry , vol.40 , pp. 9495-9504
    • Ekstrom, J.L.1    Tolbert, W.D.2    Xiong, H.3    Pegg, A.E.4    Ealick, S.E.5
  • 7
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elbe R. A simple and efficient procedure for transformation of yeasts. Biotechniques 13 (1992) 18-22
    • (1992) Biotechniques , vol.13 , pp. 18-22
    • Elbe, R.1
  • 8
    • 0035862984 scopus 로고    scopus 로고
    • Characterization of monocot and dicot plant S-adenosyl-l-methionine decarboxylase gene families including identification in the mRNA of a highly conserved pair of upstream overlapping open reading frames
    • Franceschetti M., Hanfrey C., Scaramagli S., Torrigiani P., Bagni N., Burtin D., et al. Characterization of monocot and dicot plant S-adenosyl-l-methionine decarboxylase gene families including identification in the mRNA of a highly conserved pair of upstream overlapping open reading frames. Biochem J 353 (2001) 403-409
    • (2001) Biochem J , vol.353 , pp. 403-409
    • Franceschetti, M.1    Hanfrey, C.2    Scaramagli, S.3    Torrigiani, P.4    Bagni, N.5    Burtin, D.6
  • 9
    • 4944244431 scopus 로고    scopus 로고
    • Effects of spermidine synthase overexpression on polyamine biosynthetic pathway in tobacco plants
    • Franceschetti M., Fornalè S., Tassoni A., Zuccherelli K., Mayer M.J., and Bagni N. Effects of spermidine synthase overexpression on polyamine biosynthetic pathway in tobacco plants. J Plant Physiol 161 (2004) 989-1001
    • (2004) J Plant Physiol , vol.161 , pp. 989-1001
    • Franceschetti, M.1    Fornalè, S.2    Tassoni, A.3    Zuccherelli, K.4    Mayer, M.J.5    Bagni, N.6
  • 10
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: multiple sequence alignments in PostScript
    • Gouet P., Courcelle E., Stuart D., and Metoz F. ESPript: multiple sequence alignments in PostScript. Bioinformatics 15 (1999) 305-308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.3    Metoz, F.4
  • 11
    • 0037113965 scopus 로고    scopus 로고
    • Abrogation of upstream open reading frame-mediated translational control of a plant S-adenosylmethionine decarboxylase results in polyamine disruption and growth perturbations
    • Hanfrey C., Franceschetti M., Mayer M.J., Illingworth C., and Michael A.J. Abrogation of upstream open reading frame-mediated translational control of a plant S-adenosylmethionine decarboxylase results in polyamine disruption and growth perturbations. J Biol Chem 277 (2002) 44131-44139
    • (2002) J Biol Chem , vol.277 , pp. 44131-44139
    • Hanfrey, C.1    Franceschetti, M.2    Mayer, M.J.3    Illingworth, C.4    Michael, A.J.5
  • 12
    • 28244500966 scopus 로고    scopus 로고
    • A dual upstream open reading frame-based autoregulatory circuit controlling polyamine-responsive translation
    • Hanfrey C., Elliott K.A., Franceschetti M., Mayer M.J., Illingworth C., and Michael A.J. A dual upstream open reading frame-based autoregulatory circuit controlling polyamine-responsive translation. J Biol Chem 280 (2005) 39229-39237
    • (2005) J Biol Chem , vol.280 , pp. 39229-39237
    • Hanfrey, C.1    Elliott, K.A.2    Franceschetti, M.3    Mayer, M.J.4    Illingworth, C.5    Michael, A.J.6
  • 13
    • 17044415721 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of two apple S-adenosylmethionine decarboxylase genes and their different expression in fruit development, cell growth and stress response
    • Hao Y.J., Zhang Z., Kitashiba H., Honda C., Ubi B., Kita M., and Moriguchi T. Molecular cloning and functional characterization of two apple S-adenosylmethionine decarboxylase genes and their different expression in fruit development, cell growth and stress response. Gene 350 (2005) 41-50
    • (2005) Gene , vol.350 , pp. 41-50
    • Hao, Y.J.1    Zhang, Z.2    Kitashiba, H.3    Honda, C.4    Ubi, B.5    Kita, M.6    Moriguchi, T.7
  • 14
    • 19044374467 scopus 로고    scopus 로고
    • The pivotal roles of the plant S-adenosylmethionine decarboxylase 5′ untranslated leader sequence in regulation of gene expression at the transcriptional and posttranscriptional levels
    • Hu W.W., Gong H., and Pua E.C. The pivotal roles of the plant S-adenosylmethionine decarboxylase 5′ untranslated leader sequence in regulation of gene expression at the transcriptional and posttranscriptional levels. Plant Physiol 138 (2005) 276-286
    • (2005) Plant Physiol , vol.138 , pp. 276-286
    • Hu, W.W.1    Gong, H.2    Pua, E.C.3
  • 15
    • 0025687384 scopus 로고
    • Spermidine biosynthesis in Saccharomyces cerevisiae. Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase
    • Kashiwagi K., Taneja S.K., Liu T.Y., Tabor C.W., and Tabor H. Spermidine biosynthesis in Saccharomyces cerevisiae. Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase. J Biol Chem 265 (1990) 22321-22328
    • (1990) J Biol Chem , vol.265 , pp. 22321-22328
    • Kashiwagi, K.1    Taneja, S.K.2    Liu, T.Y.3    Tabor, C.W.4    Tabor, H.5
  • 17
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski R., MacArthur M., Moss D., and Thornton J. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26 (1993) 283-291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 20
    • 0030019664 scopus 로고    scopus 로고
    • Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA
    • Michael A.J., Furze J.M., Rhodes M.J., and Burtin D. Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA. Biochem J 314 (1996) 241-248
    • (1996) Biochem J , vol.314 , pp. 241-248
    • Michael, A.J.1    Furze, J.M.2    Rhodes, M.J.3    Burtin, D.4
  • 21
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A., Brenner S., Hubbard T., and Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247 (1995) 536-540
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.1    Brenner, S.2    Hubbard, T.3    Chothia, C.4
  • 23
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl M. Recognition of errors in three-dimensional structures of proteins. Proteins 17 (1993) 355-362
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.1
  • 24
    • 0026015245 scopus 로고
    • Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity
    • Stanley B.A., and Pegg A.E. Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity. J Biol Chem 266 (1991) 18502-18506
    • (1991) J Biol Chem , vol.266 , pp. 18502-18506
    • Stanley, B.A.1    Pegg, A.E.2
  • 25
    • 0028309730 scopus 로고
    • Expression of mammalian S-adenosylmethionine decarboxylase in E. coli. Determination of sites for putrescine activation of activity and processing
    • Stanley B.A., Shantz L.M., and Pegg A.E. Expression of mammalian S-adenosylmethionine decarboxylase in E. coli. Determination of sites for putrescine activation of activity and processing. J Biol Chem 269 (1994) 7901-7907
    • (1994) J Biol Chem , vol.269 , pp. 7901-7907
    • Stanley, B.A.1    Shantz, L.M.2    Pegg, A.E.3
  • 26
    • 0034193939 scopus 로고    scopus 로고
    • Polyamine content and metabolism in Arabidopsis thaliana and effect of spermidine on plant development
    • Tassoni A., van-Buuren M., Franceschetti M., Fornalè S., and Bagni N. Polyamine content and metabolism in Arabidopsis thaliana and effect of spermidine on plant development. Plant Physiol Biochem 38 (2000) 383-393
    • (2000) Plant Physiol Biochem , vol.38 , pp. 383-393
    • Tassoni, A.1    van-Buuren, M.2    Franceschetti, M.3    Fornalè, S.4    Bagni, N.5
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J., Higgins D., and Gibson T. CLUSTAL W: improving the sensitivity of progressive multiple sequence through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.1    Higgins, D.2    Gibson, T.3
  • 29
    • 28944447254 scopus 로고    scopus 로고
    • Novel properties of malarian S-adenosylmethionine decarboxylase as revealed by structural modeling
    • Wells G., Birkholtz L., Joubert F., Walter R., and Louw A. Novel properties of malarian S-adenosylmethionine decarboxylase as revealed by structural modeling. J Mol Graph Model 24 (2006) 307-318
    • (2006) J Mol Graph Model , vol.24 , pp. 307-318
    • Wells, G.1    Birkholtz, L.2    Joubert, F.3    Walter, R.4    Louw, A.5
  • 30
    • 0035839493 scopus 로고    scopus 로고
    • The Plasmodium falciparum bifunctional ornithine decarboxylase, S-adenosyl-l-methionine decarboxylase, enables a well balanced polyamine synthesis without domain-domain interaction
    • Wrenger C., Luersen K., Krause T., Muller S., and Walter R.D. The Plasmodium falciparum bifunctional ornithine decarboxylase, S-adenosyl-l-methionine decarboxylase, enables a well balanced polyamine synthesis without domain-domain interaction. J Biol Chem 276 (2001) 29651-29656
    • (2001) J Biol Chem , vol.276 , pp. 29651-29656
    • Wrenger, C.1    Luersen, K.2    Krause, T.3    Muller, S.4    Walter, R.D.5
  • 31
    • 0030695934 scopus 로고    scopus 로고
    • Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes
    • Xiong H., Stanley B.A., Tekwani B.L., and Pegg A.E. Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes. J Biol Chem 272 (1997) 28342-28348
    • (1997) J Biol Chem , vol.272 , pp. 28342-28348
    • Xiong, H.1    Stanley, B.A.2    Tekwani, B.L.3    Pegg, A.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.