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Published on March 6, 2003; 10.1104/pp.102.014654

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Received September 17, 2002
Returned for revision October 27, 2002
Accepted December 27, 2002

Expression and Function of Cell Wall-Bound Cationic Peroxidase in Asparagus Somatic Embryogenesis

Hiroyuki Takeda , Toshihisa Kotake , Naoki Nakagawa , Naoki Sakurai *, and Donald J. Nevins

Faculty of Integrated Arts and Sciences, Hiroshima University, Kagamiyama, Higashihiroshima, 739-8521, Japan (H.T., T.K., N.N., N.S.); and Department of Vegetable Crops, University of California, Davis, California 95616 (D.J.N.)

* Corresponding author; email: nsakura{at}hiroshima-u.ac.jp.

Cultured asparagus (Asparagus officinalis L. cv Y6) cells induced to regenerate into whole plants through somatic embryogenesis secreted a 38-kD protein into cell walls. The full-length cDNA sequence of this protein (Asparagus officinalis peroxidase 1 [AoPOX1]) determined by reverse transcriptase-polymerase chain reaction showed similarity with plant peroxidases. AoPOX1 transcripts were particularly abundant during early somatic embryogenesis. To evaluate the in vivo function of AoPOX1 protein, purified recombinant AoPOX1 protein was reacted with a series of phenolic substrates. The AoPOX1 protein was effective in the metabolism of feruloyl (o-methoxyphenol)-substituted substrates, including coniferyl alcohol. The reaction product of coniferyl alcohol was fractionated and subjected to gas chromatography-mass spectrometry analysis and 1H-nuclear magnetic resonance analysis, indicating that the oxidation product of coniferyl alcohol in the presence of AoPOX1 was dehydrodiconiferyl alcohol. The concentration of dehydrodiconiferyl alcohol in the cultured medium of the somatic embryos was in the range of 10-8 M. Functions of the AoPOX1 protein in the cell differentiation are discussed.




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