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JXB Advance Access originally published online on May 13, 2003
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Journal of Experimental Botany, Vol. 54, No. 388, pp. 1785-1787, July 1, 2003
© 2003 Oxford University Press

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

Received 10 December 2002; Accepted 24 March 2003

Keiichi Matsuura1, Isao Miyagawa1, Masaru Kobayashi1, Daisaku Ohta2 and Toru Matoh{dagger},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

* The nucleotide sequence reported in this paper has been submitted to DDBJ under accession number AB059683.
{dagger} To whom correspondence should be addressed. Fax: +81 75 753 6128. E-mail: matoh{at}kais.kyoto-u.ac.jp
Abbreviations: EST, expressed sequence tag; KDO, 3-deoxy-D-manno-oct-2-ulosonic acid; KDOS, KDO-8 phosphate synthase, RT, reverse transcription.

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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