Structure and regulation of mammalian s-adenosylmethionine decarboxylase

Antti Pajunen, Anne Crozat, Olli A. Jänne, Ritva Ihalainen, Päivi H. Laitinen, Bruce Stanley, Rentala Madhubala, Anthony Pegg

Research output: Contribution to journalArticle

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Abstract

In order to understand the structure and regulation of S-adenosylmethionine decarboxylase, cDNA clones encoding this enzyme have been isolated from rat prostate and human fibroblast cDNA libraries. The authenticity of the cDNAs was verified by: (a) transfecting the Chinese hamster ovary cells with the human cDNA in the pcD vector which resulted in a transient 10-20- fold increase in S-adenosylmethionine decarboxylase activity in recipient cells; and (b) translating the mRNA formed by transcription of the cDNA insert in a reticulocyte lysate and recording an increase in S-adenosylmethionine decarboxylase activity. The amino acid sequences deduced from thec DNAs indicate that the human proenzyme for this protein contains 334 amino acids and has am olecular weight of 38,331 whereas the rat proenzyme contains 333 amino acid residues. The human and rat enzymes are very similar having only 11 amino acid differences and the cDNAs are also closely related showing over 90% homology in the 1617-nucleotide overlap which was sequenced. A further indication of the highly conserved nature of mammalian S-adenosylmethionine decarboxylases is that thea mino acid sequences deduced from theh uman and the rat cDNAs contained peptide sequences identical to those previously reported for the purifiedb ovine enzyme. In vitro transcription/translation experiments showed that the proenzyme is converted to two polypeptides of molecular weights about 32,000 and 6,000 in a processing reaction which generates the prosthetic pyruvate group and that the final enzyme contains both polypeptides. Two forms of S-adenosylmethionine decarboxylase mRNA (2.1 and about 3.4- 3.6 kilobases) are present in human and rodent tissues and may originate from the utilization of two different polyadenylation signals. Southern blots of rat genomic DNA indicated that the S-adenosylmethionine decarboxylase gene belongs to a multigene family. Depletion of cellular polyamines by inhibitors of ornithine decarboxylase or the aminopropyltransferases led to an increase in the content of S-adenosylmethionine decarboxylase protein and mRNA, but the elevation in the mRNA was not sufficient to account for all of the change in the enzyme level, particularly in cells in which spermine was depleted.

Original languageEnglish (US)
Pages (from-to)17040-17049
Number of pages10
JournalJournal of Biological Chemistry
Volume263
Issue number32
DOIs
StatePublished - Jan 1 1988

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Adenosylmethionine Decarboxylase
Complementary DNA
Rats
Enzyme Precursors
Enzymes
Amino Acids
Messenger RNA
Transcription
Peptides
Spermidine Synthase
Camellia
Polyadenylation
Spermine
Reticulocytes
DNA
Polyamines
Fibroblasts
Multigene Family
Southern Blotting
Cricetulus

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Pajunen, Antti ; Crozat, Anne ; Jänne, Olli A. ; Ihalainen, Ritva ; Laitinen, Päivi H. ; Stanley, Bruce ; Madhubala, Rentala ; Pegg, Anthony. / Structure and regulation of mammalian s-adenosylmethionine decarboxylase. In: Journal of Biological Chemistry. 1988 ; Vol. 263, No. 32. pp. 17040-17049.
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abstract = "In order to understand the structure and regulation of S-adenosylmethionine decarboxylase, cDNA clones encoding this enzyme have been isolated from rat prostate and human fibroblast cDNA libraries. The authenticity of the cDNAs was verified by: (a) transfecting the Chinese hamster ovary cells with the human cDNA in the pcD vector which resulted in a transient 10-20- fold increase in S-adenosylmethionine decarboxylase activity in recipient cells; and (b) translating the mRNA formed by transcription of the cDNA insert in a reticulocyte lysate and recording an increase in S-adenosylmethionine decarboxylase activity. The amino acid sequences deduced from thec DNAs indicate that the human proenzyme for this protein contains 334 amino acids and has am olecular weight of 38,331 whereas the rat proenzyme contains 333 amino acid residues. The human and rat enzymes are very similar having only 11 amino acid differences and the cDNAs are also closely related showing over 90{\%} homology in the 1617-nucleotide overlap which was sequenced. A further indication of the highly conserved nature of mammalian S-adenosylmethionine decarboxylases is that thea mino acid sequences deduced from theh uman and the rat cDNAs contained peptide sequences identical to those previously reported for the purifiedb ovine enzyme. In vitro transcription/translation experiments showed that the proenzyme is converted to two polypeptides of molecular weights about 32,000 and 6,000 in a processing reaction which generates the prosthetic pyruvate group and that the final enzyme contains both polypeptides. Two forms of S-adenosylmethionine decarboxylase mRNA (2.1 and about 3.4- 3.6 kilobases) are present in human and rodent tissues and may originate from the utilization of two different polyadenylation signals. Southern blots of rat genomic DNA indicated that the S-adenosylmethionine decarboxylase gene belongs to a multigene family. Depletion of cellular polyamines by inhibitors of ornithine decarboxylase or the aminopropyltransferases led to an increase in the content of S-adenosylmethionine decarboxylase protein and mRNA, but the elevation in the mRNA was not sufficient to account for all of the change in the enzyme level, particularly in cells in which spermine was depleted.",
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Pajunen, A, Crozat, A, Jänne, OA, Ihalainen, R, Laitinen, PH, Stanley, B, Madhubala, R & Pegg, A 1988, 'Structure and regulation of mammalian s-adenosylmethionine decarboxylase', Journal of Biological Chemistry, vol. 263, no. 32, pp. 17040-17049. https://doi.org/10.111/J.0021-9258

Structure and regulation of mammalian s-adenosylmethionine decarboxylase. / Pajunen, Antti; Crozat, Anne; Jänne, Olli A.; Ihalainen, Ritva; Laitinen, Päivi H.; Stanley, Bruce; Madhubala, Rentala; Pegg, Anthony.

In: Journal of Biological Chemistry, Vol. 263, No. 32, 01.01.1988, p. 17040-17049.

Research output: Contribution to journalArticle

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AB - In order to understand the structure and regulation of S-adenosylmethionine decarboxylase, cDNA clones encoding this enzyme have been isolated from rat prostate and human fibroblast cDNA libraries. The authenticity of the cDNAs was verified by: (a) transfecting the Chinese hamster ovary cells with the human cDNA in the pcD vector which resulted in a transient 10-20- fold increase in S-adenosylmethionine decarboxylase activity in recipient cells; and (b) translating the mRNA formed by transcription of the cDNA insert in a reticulocyte lysate and recording an increase in S-adenosylmethionine decarboxylase activity. The amino acid sequences deduced from thec DNAs indicate that the human proenzyme for this protein contains 334 amino acids and has am olecular weight of 38,331 whereas the rat proenzyme contains 333 amino acid residues. The human and rat enzymes are very similar having only 11 amino acid differences and the cDNAs are also closely related showing over 90% homology in the 1617-nucleotide overlap which was sequenced. A further indication of the highly conserved nature of mammalian S-adenosylmethionine decarboxylases is that thea mino acid sequences deduced from theh uman and the rat cDNAs contained peptide sequences identical to those previously reported for the purifiedb ovine enzyme. In vitro transcription/translation experiments showed that the proenzyme is converted to two polypeptides of molecular weights about 32,000 and 6,000 in a processing reaction which generates the prosthetic pyruvate group and that the final enzyme contains both polypeptides. Two forms of S-adenosylmethionine decarboxylase mRNA (2.1 and about 3.4- 3.6 kilobases) are present in human and rodent tissues and may originate from the utilization of two different polyadenylation signals. Southern blots of rat genomic DNA indicated that the S-adenosylmethionine decarboxylase gene belongs to a multigene family. Depletion of cellular polyamines by inhibitors of ornithine decarboxylase or the aminopropyltransferases led to an increase in the content of S-adenosylmethionine decarboxylase protein and mRNA, but the elevation in the mRNA was not sufficient to account for all of the change in the enzyme level, particularly in cells in which spermine was depleted.

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Pajunen A, Crozat A, Jänne OA, Ihalainen R, Laitinen PH, Stanley B et al. Structure and regulation of mammalian s-adenosylmethionine decarboxylase. Journal of Biological Chemistry. 1988 Jan 1;263(32):17040-17049. https://doi.org/10.111/J.0021-9258