Journal Article

Molecular Cloning of Plant Spermidine Synthases

Takashi Hashimoto, Katsutomo Tamaki, Ken-ichi Suzuki and Yasuyuki Yamada

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 39, issue 1, pages 73-79
Published in print January 1998 | ISSN: 0032-0781
Published online January 1998 | e-ISSN: 1471-9053 | DOI:
Molecular Cloning of Plant Spermidine Synthases

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry


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Four cDNAs for spermidine synthase (SPDS), which converts the diamine putrescine to the higher polyamine spermidine using decarboxylated S-adenosylmethionine as the co-factor, were isolated from Nicotiana sylvestris, Hyoscyamus niger, and Arabidopsis thaliana. When the N. sylvestris SPDS cDNA was expressed in a SPDS-deficient E. coli mutant, the recombinant protein showed high SPDS activity, but did not have any spermine synthase activity. The plant SPDSs have molecular masses of about 34 kDa, possess the co-factor binding motifs which have been proposed for S-adenosylmethionine, and are more homologous in amino acid sequence to tobacco putrescine N-methyltransferase (PMT) than to SPDSs from mammals and E. coli. The SPDS gene is expressed in root, stem, and leaf in N. sylvestris, whereas the PMT gene is expressed only in root. The potential evolution of plant SPDS and PMT, and their evolutionary relationships with animal SPDS are discussed.

Keywords: Arabidopsis thaliana; Hyoscyamus niger; Nicoiiana sylvestris; Polyamine; Spermidine synthase (EC

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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