Maternal and zygotic expression of mRNA for S-adenosylmethionine decarboxylase and its relevance to the unique polyamine composition in Xenopus oocytes and embryos

Jun Shinga, Keiko Kashiwagi, Kosuke Tashiro, Kazuei Igarashi, Koichiro Shiokawa

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

From Xenopus tailbud cDNA library, we isolated the cDNA for S- adenosylmethionine decarboxylase (SAMDC), an enzyme which provides putrescine and spermidine with the aminopropyl group to form spermidine and spermine, respectively. The cDNA coded for 335 amino acids whose sequence had high homology (ca. 83%) to other vertebrate SAMDCs, preserving the sequence reportedly essential for enzyme activity, proenzyme processing, and putrescine stimulation of the enzyme activity. Northern blot analysis showed one major mRNA signal of ca. 3.5 kb, with a minor signal of ca. 2.0 kb which may probably be due to cross-hybridization. In oocytes the SAMDC mRNA occurred from singe I, and its amount peaked at stage II, then gradually decreased from stage III to VI. The decreased level of the mRNA was maintained during oocyte maturation, further decreased from the cleavage to early neurula stage, and then increased greatly due to the zygotic expression during late neurula stages (stage 21-25), reaching a plateau level at the late tailbud stage (stage 28). Enzyme assays showed that the changing level of the SAMDC mRNA was reflected in the level of the functional enzyme, suggesting strongly that the zygotic expression of the mRNA leads to a large increase in the amount of SAMDC, albeit in the pre-neurula embryo the amount of the enzyme is very small. We found that the relative composition of polyamines is the eukaryote-type (high-level spermine) at the beginning of oogenesis, but it changes to the prokaryote-type, or more appropriately Escherichia coli-type (high-level putrescine but background level spermine) during oocyte maturation, and remains E. coli-type throughout embryogenesis. We assume that the E. coli-type polyamine composition is a necessary factor for the normal embryogenic development in Xenopus and its maintenance, especially that in pre-neurula stages, can be explained by the low level of both SAMDC mRNA and SAMDC.

Original languageEnglish
Pages (from-to)31-40
Number of pages10
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Volume1308
Issue number1
DOIs
Publication statusPublished - Jul 31 1996
Externally publishedYes

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Adenosylmethionine Decarboxylase
Polyamines
Xenopus
Oocytes
Embryonic Structures
Mothers
Messenger RNA
Putrescine
Spermine
Chemical analysis
Escherichia coli
Enzymes
Spermidine
Enzyme activity
Complementary DNA
Oogenesis
Enzyme Precursors
Enzyme Assays
Eukaryota
Gene Library

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

Cite this

Maternal and zygotic expression of mRNA for S-adenosylmethionine decarboxylase and its relevance to the unique polyamine composition in Xenopus oocytes and embryos. / Shinga, Jun; Kashiwagi, Keiko; Tashiro, Kosuke; Igarashi, Kazuei; Shiokawa, Koichiro.

In: Biochimica et Biophysica Acta - Gene Structure and Expression, Vol. 1308, No. 1, 31.07.1996, p. 31-40.

Research output: Contribution to journalArticle

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abstract = "From Xenopus tailbud cDNA library, we isolated the cDNA for S- adenosylmethionine decarboxylase (SAMDC), an enzyme which provides putrescine and spermidine with the aminopropyl group to form spermidine and spermine, respectively. The cDNA coded for 335 amino acids whose sequence had high homology (ca. 83{\%}) to other vertebrate SAMDCs, preserving the sequence reportedly essential for enzyme activity, proenzyme processing, and putrescine stimulation of the enzyme activity. Northern blot analysis showed one major mRNA signal of ca. 3.5 kb, with a minor signal of ca. 2.0 kb which may probably be due to cross-hybridization. In oocytes the SAMDC mRNA occurred from singe I, and its amount peaked at stage II, then gradually decreased from stage III to VI. The decreased level of the mRNA was maintained during oocyte maturation, further decreased from the cleavage to early neurula stage, and then increased greatly due to the zygotic expression during late neurula stages (stage 21-25), reaching a plateau level at the late tailbud stage (stage 28). Enzyme assays showed that the changing level of the SAMDC mRNA was reflected in the level of the functional enzyme, suggesting strongly that the zygotic expression of the mRNA leads to a large increase in the amount of SAMDC, albeit in the pre-neurula embryo the amount of the enzyme is very small. We found that the relative composition of polyamines is the eukaryote-type (high-level spermine) at the beginning of oogenesis, but it changes to the prokaryote-type, or more appropriately Escherichia coli-type (high-level putrescine but background level spermine) during oocyte maturation, and remains E. coli-type throughout embryogenesis. We assume that the E. coli-type polyamine composition is a necessary factor for the normal embryogenic development in Xenopus and its maintenance, especially that in pre-neurula stages, can be explained by the low level of both SAMDC mRNA and SAMDC.",
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