Caenorhabditis elegans S-adenosylmethionine decarboxylase is highly stimulated by putrescine but exhibits a low specificity for activator binding

Biological Chemistry

Volumn 384, Issue 1, 2003, Pages 83-91

  Ndjonka, Dieudonne ^a   Da'dara, Akram ^b   Walter, Rolf D ^a   Lüersen, Kai ^a  

^a BERNHARD NOCHT INSTITUTE FOR TROPICAL MEDICINE   (Germany)

^b HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

Nematodes; Polyamines; Putrescine; Spermidine

Indexed keywords

ADENOSYLMETHIONINE DECARBOXYLASE; AMINO ACID; ARGININE; GLUTAMIC ACID; LYSINE; MUTANT PROTEIN; POLYAMINE; PUTRESCINE; SERINE; SPERMIDINE; SPERMINE; THREONINE;

BINDING AFFINITY; CAENORHABDITIS ELEGANS; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; MAMMAL; NEMATODE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYAMINE SYNTHESIS; PRIORITY JOURNAL; PROTEIN PROCESSING; REVIEW; SITE DIRECTED MUTAGENESIS;

ADENOSYLMETHIONINE DECARBOXYLASE; AMINO ACID SEQUENCE; ANIMALS; BLOTTING, WESTERN; CAENORHABDITIS ELEGANS; CATALYSIS; CONSERVED SEQUENCE; ENZYME ACTIVATORS; HUMANS; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PUTRESCINE; RECOMBINANT PROTEINS; SPERMIDINE; SPERMINE; STIMULATION, CHEMICAL; SUBSTRATE SPECIFICITY;

CAENORHABDITIS; CAENORHABDITIS ELEGANS; MAMMALIA; NEMATODA;

EID: 0037228657     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.009     Document Type: Review

References (48)

1. Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
2. Da'dara, A. A. and Walter, R. D. (1998). Molecular and biochemical characterization of S-adenosylmethionine decarboxylase from the free-living nematode Caenorhabditis elegans. Biochem. J. 336, 545-550.
3. Dezeure, F., Gerhart, F. and Seiler, N. (1989). Activation of rat liver S-adenosylmethionine decarboxylase by putrescine and 2-substituted 1,4-butanediamines. Int. J. Biochem. 21, 889-899.
4. Ekstrom, J. L., Mathews, II, Stanley, B. A., Pegg, A. E. and Ealick, S. E. (1999). The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 Å resolution reveals a novel fold. Struct. Fold Des. 7, 583-595.
5. Ekstrom, J. L., Tolbert, W. D., Xiong, H., Pegg, A. E. and Ealick, S. E. (2001). 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, 9495-9504.
6. Granato, M., Schnabel, H. and Schnabel, R. (1994). pha-1, a selectable marker for gene transfer in C. elegans. Nucleic Acids Res. 22, 1762-1763.
7. Gupta, S., Shukla, O. P. and Walter, R. D. (1987). Putrescine-activated S-adenosylmethionine decarboxylase from Acanthamoeba culbertsoni. Mol. Biochem. Parasitol. 23, 247-252.
8. Hafner, E. W., Tabor, C. W. and Tabor, H. (1979). Mutants of Escherichia coli that do not contain 1,4-diaminobutane (putrescine) or spermidine. J. Biol. Chem. 254, 12419-12426.
9. Hamana, K., Hamana, H. and Shinozawa, T. (1995) Alterations in polyamine levels of nematode, leech and planaria during regeneration, temperature and osmotic stresses. Comp. Biochem. Physiol. 111B, 91-97.
10. Hart, D., Winther, M. and Stevens, L. (1978). Polyamine distribution and S-adenosylmethionine decarboxylase activity in filamentous fungi. FEMS Microbiol. Lett. 3, 173-175.
11. Hoyt, M. A., Williams-Abbott, L. J., Pitkin, J. W. and Davis, R. H. (2000). Cloning and expression of the S-adenosylmethionine decarboxylase gene of Neurospora crassa and processing of its product. Mol. Gen. Genet. 263, 664-673.
12. Hugo, E. R. and Byers, T. J. (1993). S-adenosyl-L-methionine decarboxylase of Acanthamoeba castellanii (Neff): purification and properties. Biochem. J. 295, 203-209.
13. Jansen, G., Hazendonk, E., Thijssen, K. L. and Plasterk, R. H. (1997). Reverse genetics by chemical mutagenesis in Caenorhabditis elegans. Nature Genet. 17, 119-121.
14. Jones, D., Dixon, D. K., Graham, R. W. and Candido, E. P. (1989). Differential regulation of closely related members of the hsp 16 gene family in Caenorhabditis elegans. DNA. 8, 481-490.
15. Kameji, T. and Pegg, A. E. (1987). Effect of putrescine on the synthesis of S-adenosylmethionine decarboxylase. Biochem. J. 243, 285-288.
16. Kinch, L. N., Scott, J. R., Ullman, B. and Phillips, M. A. (1999). Cloning and kinetic characterization of the Trypanosoma cruzi S-adenosylmethionine decarboxylase. Mol. Biochem. Parasitol. 101, 1-11.
17. Lu, S. C. (2000). S-Adenosylmethionine. Int. J. Biochem. Cell. Biol. 32, 391-395.
18. Macrae, M., Kramer, D. L. and Coffino, P. (1998). Developmental effect of polyamine depletion in C. elegans . Biochem. J. 333, 309-315.
19. Mamont, P. S. and Danzin, C. (1981). In vitro and in vivo regulation of S-adenosylmethionine decarboxylase by polyamines. Adv. Polyamine Res. 3, 123-135.
20. Mello, C. and Fire, A. (1995). DNA transformation. Methods Cell. Biol. 48, 451-482.
21. Pegg, A. E. (1986). Recent advances in the biochemistry of polyamines in eukaryotes. Biochem. J. 234, 249-262.
22. Pegg, A. E. and Jacobs, G. (1983). Comparison of inhibitors of S-adenosylmethionine decarboxylase from different species. Biochem. J. 213, 495-502.
23. Pegg, A. E. and Williams-Ashman, H. G. (1968). Stimulation of the decarboxylation of S-adenosylmethionine by putrescine in mammalian tissues. Biochem. Biophys. Res. Commun. 30, 76-82.
24. Pegg, A. E. and Williams-Ashman, H. G. (1969). On the role of S-adenosyl-L-methionine in the biosynthesis of spermidine by rat prostate. J. Biol. Chem. 244, 682-693.
25. Persson, K., Aslund, L., Grahn, B., Hanke, J. and Heby, O. (1998). Trypanosoma cruzi has not lost its S-adenosylmethionine decarboxylase: characterization of the gene and the encoded enzyme. Biochem. J. 333, 527-537.
26. Porta, R., Esposito, C. and Pietra, G. D. (1977). S-adenosylmethionine decarboxylase from human placenta. Int. J. Biochem. 8, 347-352.
27. Pösö, H., Sinervirta, R., Himberg, J. J. and Jänne, J. (1975a). Putrescine-insensitive S-adenosyl-L-methionine decarboxylase from Tetrahymena pyriformis. Acta Chem. Scand. B. 29, 932-936.
28. Pösö, H., Sinervirta, R. and Jänne, J. (1975b). S-adenosylmethionine decarboxylase from baker's yeast. Biochem. J. 151, 67-73.
29. Sakai, T., Hori, C., Kano, K. and Oka, T. (1979). Purification and characterization of S-adenosyl-L-methionine decarboxylase from mouse mammary gland and liver. Biochemistry 18, 5541-5548.
30. Sambrook, J., Fritsch, E. F. and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press).
31. Schägger, H. and von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
32. Schröder, G. and Schröder, J. (1995). cDNAs for S-adenosyl-L-methionine decarboxylase from Catharanthus roseus, heterologous expression, identification of the proenzyme-processing site, evidence for the presence of both subunits in the active enzyme, and a conserved region in the 5?′ mRNA leader. Eur. J. Biochem. 228, 74-78.
33. Stanley, B. A. (1995). S-Adenosylmethionine decarboxylase regulation and processing. In: Polyamines. Regulation and Molecular Interaction, R.A. Casero, ed. (Austin, USA: R.G. Landes Co.), pp. 27-75.
34. Stanley, B. A. and Pegg, A. E. (1991). Amino acid residues necessary for putrescine stimulation of human S-adenosylmethionine decarboxylase proenzyme processing and catalytic activity. J. Biol. Chem. 266, 18502-18506.
35. Stanley, B. A. and Shantz, L. M. (1994). S-adenosylmethionine decarboxylase structure-function relationships. Biochem. Soc. Trans. 22, 863-869.
36. Stanley, B. A., Pegg, A. E. and Holm, I. (1989). Site of pyruvate formation and processing of mammalian S-adenosylmethionine decarboxylase proenzyme. J. Biol. Chem. 264, 21073-21079.
37. Stanley, B. A., Shantz, L. M. and Pegg, A. E. (1994). Expression of mammalian S-adenosylmethionine decarboxylase in Escherichia coli. Determination of sites for putrescine activation of activity and processing. J. Biol. Chem. 269, 7901-7907.
38. Sulston, J. and Hodgkin, J. (1988). Methods. In: The Nematode Caenorhabditis elegans, W. B. Wood, ed. (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press), pp. 587-606.
39. Suresh, M. R. and Adiga, P. R. (1977). Putrescine-sensitive (artifactual) and insensitive (biosynthetic) S-adenosyl-L-methionine decarboxylase activities of Lathyrus sativus seedlings. Eur. J. Biochem. 79, 511-518.
40. Tabor, C. W. and Tabor, H. (1984). Polyamines. Annu. Rev. Biochem. 53, 749-790.
41. Tekwani, B. L., Bacchi, C. J. and Pegg, A. E. (1992). Putrescine activated S-adenosylmethionine decarboxylase from Trypanosoma brucei brucei. Mol. Cell. Biochem. 117, 53-61.
42. Tolbert, W. D., Ekstrom, J. L., Mathews, I.I., Secrist 3rd, J. A., Kapoor, P., Pegg, A. E. and Ealick, S. E. (2001). The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase. Biochemistry 40, 9484-9494.
43. Wrenger, C., Lüersen, K., Krause, T, Müller, S. and Walter, R. D. (2001). 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, 29651-29656.
44. Xiong, H. and Pegg, A. E. (1999). Mechanistic studies of the processing of human S-adenosylmethionine decarboxylase proenzyme. Isolation of an ester intermediate. J. Biol. Chem. 274, 35059-35066.
45. Xiong, H., Stanley, B. A., Tekwani, B. L. and Pegg, A. E. (1997). Processing of mammalian and plant S-adenosylmethionine decarboxylase proenzymes. J. Biol. Chem. 272, 28342-28348.
46. Xiong, H., Stanley, B. A. and Pegg, A. E. (1999). Role of cysteine-82 in the catalytic mechanism of human S-adenosylmethionine decarboxylase. Biochemistry. 38, 2462-2470.
47. Yang, Y. G. and Cho, Y. D. (1991). Purification of S-adenosylmethionine decarboxylase from soybean. Biochem. Biophys. Res. Commun. 181, 1181-1186.
48. Zappia, V., Carteni-Farina, M. and Delia Pietra, G. (1972). S-adenosylmethionine decarboxylase from human prostate. Activation by putrescine. Biochem. J. 129, 703-709.