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JXB Advance Access published online on May 13, 2003
Journal of Experimental Botany, doi:10.1093/jxb/erg181
© 2003 by Oxford University Press
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Received December 10, 2002; accepted March 24, 2003
© 2003 Society for Experimental Biology

GENE NOTE

Arabidopsis 3-deoxy-D-manno-oct-2-ulosonate-8-phosphate synthase: cDNA cloning and expression analyses

Keiichi Matsuura 1, Isao Miyagawa 1, Masaru Kobayashi 1, Daisaku Ohta 2, Toru Matoh 1*

1 Laboratory of Plant Nutrition, Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, 606-8502, Japan
2 Graduate School of Agriculture and Biosciences, Osaka Prefecture University, Sakai, 599-8531, Japan

* To whom correspondence should be addressed. E-mail: matoh{at}kais.kyoto-u.ac.jp.


  Abstract

The molecular characterization of two isoforms of 3-deoxy-D-manno-oct-2-ulosonate (KDO) -8-phosphate synthase (AtkdsA1 and AtkdsA2) from Arabidopsis is reported here. First, by isolating a full-length cDNA for AtkdsA1, it was confirmed that the deduced primary structures of AtkdsA1 and AtkdsA2 proteins were 93% identical. Functional expression and purification studies demonstrated the efficient catalytic activity of the AtkdsA1 enzyme to produce KDO-8-phosphate from phosphoenolpyruvate and D-arabinose-5-phosphate. RT-PCR and RNA-gel blot analysis revealed different expression profiles for both genes; the AtkdsA1 gene was predominantly expressed in the shoots, while the AtkdsA2 transcript accumulated to a higher level in the roots, implicating differential roles of these isoforms in planta.

Key words: Arabidopsis thaliana, 3-deoxy-D-manno-oct-2-ulosonate-8-phosphate, 3-deoxy-D-manno-oct-2-ulosonate-8-phosphate synthase, rhamnogalacturonan II.


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