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References

  • Almrud, J.J., Oliveira, M.A., Kern, A.D., Grishin, N.V., Phillips, M.A., Hackert, M.L. (2000) Crystal structure of human ornithine decarboxylase at 2.1 Å resolution: structural insights to antizyme binding. J. Mol. Biol. 295, 716.DOI: 10.1006/jmbi.1999.3331
  • Ariyanayagam, M.R. & Fairlamb, A.H. (1997) Diamine auxotrophy may be a universal feature of Trypanosoma cruzi epimastigotes. Mol. Biochem. Parasitol. 84, 111121.
  • Auvinen, M., Paasinen, A., Andersson, L.C., Holtta, E. (1992) Ornithine decarboxylase is critical for cell transformation. Nature, 360, 355358.
  • Bailey, A., Mueller, E., Bowyer, P. (2000) Ornithine decarboxylase of Stagonospora (Septoria) nodorum is required for virulence toward wheat. J. Biol. Chem. 275, 1424214247.
  • Bell, E. & Malmberg, R.L. (1990) Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing. Mol. Gen. Genet. 224, 431436.
  • Bello-Fernandez, C., Packham, G., Cleveland, J.L. (1993) The ornithine decarboxylase gene is a transcriptional target of c-Myc. Proc. Natl Acad. Sci. USA, 90, 78047808.
  • Birecka, H., Bitonti, A.J., McCann, P.P. (1985) Activities of arginine and ornithine decarboxylases in various plant species. Plant Physiol. 79, 515519.
  • Borrell, A., Cuiliañez-Macià, F.A., Altabella, T., Besford, R.T., Flores, D., Tiburcio, A.F. (1995) Arginine decarboxylase is localized in chloroplasts. Plant Physiol. 109, 771776.
  • Borrell, A., Besford, R.T., Altabella, T., Masgrau, C., Tiburcio, A.F. (1996) Regulation of arginine decarboxylase by spermine in osmotically-stressed oat leaves. Physiol. Plant. 98, 105110.
  • Burtin, D. & Michael, A.J. (1997) Overexpression of arginine decarboxylase in transgenic plants. Biochem. J. 325, 331337.
  • Chang, K.W., Lee, S.H., Hwang, S.B., Park, K.Y. (2000) Characterization and translational regulation of the arginine decarboxylase gene in carnation (Dianthus caryophyllus L.). Plant J. 24, 4556.DOI: 10.1046/j.0960-7412.2000.00854.x
  • Cohen, S. (1998) A Guide to the Polyamines. Oxford: Oxford University Press.
  • Coleman, C.S., Stanley, B.A., Pegg, A.E. (1993) Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors. J. Biol. Chem. 268, 2457224579.
  • Coleman, C.S., Stanley, B.A., Visanath, R., Pegg, A.E. (1994) Rapid exchange of subunits of mammalian ornithine decarboxylase. J. Biol. Chem. 269, 31553158.
  • Davidson, N.E., Hahm, H.A., McCloskey, D.E., Woster, P.M., Casero, R.A. (1999) Clinical aspects of cell death in breast cancer: the polyamine pathway as a new target for treatment. Endocr. Relat. Cancer, 6, 6973.
  • Elbe, R. (1992) A simple and efficient procedure for transformation of yeasts. Biotechniques, 13, 1820.
  • Feirer, R.P., Hocking, K.L., Woods, P.J. (1997) Involvement of arginine decarboxylase in the response of Arabidopsis thaliana to osmotic stress. J. Plant Physiol. 153, 733738.
  • Franceschetti, M., Hanfrey, C., Scaramagli, S., Torrigiani, P., Bagni, N., Burtin, D., Michael, A.J. (2001) Characterisation of monocot and dicot plant S-adenosylmethionine decarboxylase gene families including identification in the mRNA of a highly conserved pair of upstream overlapping open reading frames. Biochem. J. 353, 403409.DOI: 10.1042/0264-6021:3530403
  • Galloway, G.L., Malmberg, R.L., Price, R.A. (1998) Phylogenetic utility of the nuclear gene arginine decarboxylase: an example from Brassicaceae. Mol. Biol. Evol. 15, 13121320.
  • Grishin, N.V., Phillips, M.A., Goldsmith, E.J. (1995) Modeling of the spatial structure of eukaryotic ornithine decarboxylase. Protein Sci. 4, 12911304.
  • Grishin, N.V., Osterman, A.L., Brooks, H.B., Phillips, M.A., Goldsmith, E.J. (1999) X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with α-difluoromethylornithine. Biochemistry, 38, 1517415184.DOI: 10.1021/bi9915115
  • Hanzawa, Y., Takahashi, T., Michael, A.J., Burtin, D., Long, D., Pineiro, M., Coupland, G., Komeda, Y. (2000) ACAULIS5, an Arabidopsis gene required for stem elongation, encodes a spermine synthase. EMBO J. 19, 42484256.
  • Hunter, K.J., Le Quesne, S.A., Fairlamb, A.H. (1994) Identification and biosynthesis of N1,N9-bis(glutathionyl) aminopropylcadaverine (homotrypanothione) in Trypanosoma cruzi. Eur. J. Biochem. 226, 10191027.
  • Igarashi, K. & Kashiwagi, K. (2000) Polyamines: mysterious modulators of cellular functions. Biochem. Biophys. Res. Commun. 271, 559564.
  • Ivanov, I.P., Gesteland, R.F., Atkins, J.F. (2000) Antizyme expression: a subversion of triplet decoding, which is remarkably conserved by evolution, is a sensor for an autoregulatory circuit. Nucl. Acids Res. 28, 31853196.
  • Kern, A.D., Oliveira, M.A., Coffino, P., Hackert, M.L. (1999) Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure, 7, 567581.
  • Kinch, L.N., Scott, J.R., Ullman, B., Phillips, M.A. (1998) Cloning and characterization of the Trypanosoma cruzi S-adenosylmethionine decarboxylase. Mol. Biochem. Parasitol. 101, 111.
  • Klein, R.D., Geary, T.G., Gibson, A.S., et al. (1999) Reconstitution of a bacterial/plant polyamine biosynthetic pathway in Saccharomyces cerevisiae. Microbiology, 145, 301307.
  • Le Quesne, S.A. & Fairlamb, A.H. (1996) Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes. Biochem. J. 316, 481486.
  • Li, X. & Coffino, P. (1993) Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein. Mol. Cell. Biol. 13, 23772383.
  • Malmberg, R.L. & Cellino, M.L. (1994) Arginine decarboxylase of oats is activated by enzymatic cleavage into two polypeptides. J. Biol. Chem. 269, 27032706.
  • Malmberg, R.L., Smith, K.E., Bell, E., Cellino, M.L. (1992) Arginine decarboxylase of oats is clipped from a precursor into two polypeptides found in the soluble enzyme. Plant Physiol. 100, 146152.
  • Marton, L.J. & Morris, D.R. (1987) Inhibition of Polyamine Biosynthesis. Biological Significance and Basis for New Therapies (McCann, P.P., Pegg, A.E. and Sjoerdsma, A., eds), pp. 79105. New York: Academic Press, Inc.
  • Michael, A.J., Furze, J.M., Rhodes, M.J., Burtin, D. (1996) Molecular cloning and functional identification of a plant ornithine decarboxylase cDNA. Biochem. J. 314, 241248.
  • Mize, G.J., Ruan, H., Low, J.J., Morris, D.R. (1998) The inhibitory upstream open reading frame from mammalian S-adenosylmethionine decarboxylase mRNA has a strict sequence specificity in critical positions. J. Biol. Chem. 273, 3250032505.
  • Osterman, A.L., Grishin, N.V., Kinch, L.N., Phillips, M.A. (1994) Formation of functional cross-species heterodimers of ornithine decarboxylase. Biochemistry, 33, 1366213667.
  • Osterman, A.L., Kinch, L.N., Grishin, N.V., Phillips, M.A. (1995a) Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis. J. Biol. Chem. 270, 1179711802.
  • Osterman, A.L., Lueder, D.V., Quick, M., Myers, D., Canagarajah, B.J., Phillips, M.A. (1995b) Domain organization and a protease-sensitive loop in eukaryotic ornithine decarboxylase. Biochemistry, 34, 1343113436.
  • Osterman, A.L., Brooks, H.B., Rizo, J., Phillips, M.A. (1997) Role of Arg-277 in the binding of the pyridoxal-5′-phosphate to Trypanosoma brucei ornithine decarboxylase. Biochemistry, 36, 45584567.DOI: 10.1021/bi962916h
  • Osterman, A.L., Brooks, H.B., Jackson, L., Abbott, J.J., Phillips, M.A. (1999) Lysine-69 plays a key role in catalysis by ornithine decarboxylase through acceleration of the Schiff base formation, decarboxylation, and product release steps. Biochemistry, 38, 1181411826.DOI: 10.1021/bi9906221
  • Packham, G. & Cleveland, J.L. (1994) Ornithine decarboxylase is a mediator of c-Myc-induced apoptosis. Mol. Cell. Biol. 14, 57415747.
  • Pegg, A.E. (1988) Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy. Cancer Res. 48, 759774.
  • Pérez-Amador, M.A., Carbonell, J., Granell, A. (1995) Expression of arginine decarboxylase is induced during early fruit development and in young tissues of Pisum sativum (L.). Plant Mol. Biol. 28, 9971009.
  • Persson, K., Åslund, L., Grahn, B., Hanke, J., Heby, O. (1998) Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: characterization of the gene and the encoded enzyme. Biochem. J. 333, 527537.
  • Pollard, K.J., Samuels, M.L., Crowley, K.A., Hansen, J.C., Peterson, C.L. (1999) Functional interactions between GCN5 and polyamines: a new role for core histone acetylation. EMBO J. 18, 56225633.
  • Poulin, R., Lu, L., Ackermann, B., Bey, P., Pegg, A.E. (1992) Mechanism of the irreversible inactivation of mouse ornithine decarboxylase by α-difluoromethylornithine. J. Biol. Chem. 267, 150158.
  • Pyronnet, S., Pradayrol, L., Sonenberg, N. (2000) A cell cycle-dependent internal ribosome entry site. Mol. Cell, 5, 607616.
  • Raney, A., Baron, A.C., Mize, G.J., Law, G.L., Morris, D.R. (2000) In vitro translation of the upstream open reading frame in the mammalian mRNA encoding S-adenosylmethionine decarboxylase. J. Biol. Chem. 275, 2444424450.
  • Sandmeier, E., Hale, T.I., Christen, P. (1994) Multiple evolutionary origin of pyridoxal-5′-phosphate-dependent amino acid decarboxylases. Eur. J. Biochem. 221, 9971002.
  • Soyka, S. & Heyer, A.G. (1999) Arabidopsis knockout mutation of ADC2 gene reveals inducibility by osmotic stress. FEBS Lett. 458, 219223.
  • Tobias, K.E. & Kahana, C. (1993) Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants. Biochemistry, 32, 58425847.
  • Tobias, K.E., Mamroud-Kidron, E., Kahana, C. (1993) Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers. Eur. J. Biochem. 218, 245250.
  • Tsirka, S. & Coffino, P. (1992) Dominant negative mutants of ornithine decarboxylase. J. Biol. Chem. 267, 2305723062.
  • Watson, M.B. & Malmberg, R.L. (1996) Regulation of Arabidopsis thaliana (L.) Heynh arginine decarboxylase by potassium deficiency stress. Plant Physiol. 111, 10771083.
  • Watson, M.B., Emory, K.K., Piatak, R.M., Malmberg, R.L. (1998) Arginine decarboxylase (polyamine synthesis) mutants of Arabidopsis thaliana exhibit altered root growth. Plant J. 13, 231239.