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Plant and Cell Physiology Advance Access published online on January 30, 2006
Plant and Cell Physiology, doi:10.1093/pcp/pcj016
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Plant and Cell Physiology 2006 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received December 13, 2005
Accepted January 22, 2006

Regular Paper

Isolation and Characterization of a Novel Peroxidase Gene ZPO-C of Which Expression and Function Are Closely Associated with Lignification During Tracheary Element Differentiation

Yasushi Sato 1 *, Taku Demura 2, Ken Yamawaki 1, Yukina Inoue 1, Seiichi Sato 1, Munetaka Sugiyama 3, and Hiroo Fukuda 4

1 Department of Biology, Faculty of Science, Ehime University, Matsuyama 790-8577, Japan
2 RIKEN Plant Science Center, 230-0045 Yokohama, Japan
3 Botanical Gardens, Graduate School of Science, The University of Tokyo, Tokyo 112-0001, Japan
4 Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan

* To whom correspondence should be addressed.
Yasushi Sato, E-mail: ysato{at}sci.ehime-u.ac.jp


  Abstract

In an attempt to elucidate the regulatory mechanism of vessel lignification, we isolated ZPO-C, a novel peroxidase gene of Zinnia elegans that is expressed specifically in differentiating tracheary elements (TEs). The ZPO-C transcript was shown to accumulate transiently at the time of secondary wall thickening of TEs in xylogenic culture of Zinnia cells. In situ hybridization indicated specific accumulation of the ZPO-C transcript in immature vessels in Zinnia seedlings. Immunohistochemical analysis using anti-ZPO-C antibody showed that the ZPO-C protein is abundant in TEs, especially at their secondary walls. For enzymatic characterization of ZPO-C, 6xHis-tagged ZPO-C was produced in tobacco cultured cells and purified. The ZPO-C:6xHis protein had a peroxidase activity preferring sinapyl alcohol as well as coniferyl alcohol as a substrate, with a narrow pH optimum around 5.25. The peroxidase activity required calcium ion and was elevated by increasing Ca2+ concentration in the range of 0 to 10 mM. An Arabidopsis homolog of ZPO-C, At5g51890 was examined for expression patterns with transgenic plants carrying a yellow fluorescent protein (YFP) gene under the control of the At5g51890 promoter. The YFP fluorescence localization demonstrated vessel-specific expression of At5g51890 in the Arabidopsis roots. Taken collectively, our results strongly suggest that ZPO-C and its homologues play an important role in lignification of secondary cell walls in differentiating TEs.

Keywords: Arabidopsis; Lignification; Peroxidase; Tracheary element differentiation; Zinnia elegans; ZPO-C.
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