Characterization of arabidopsis CTP:3-deoxy-d-manno-2-octulosonate cytidylyltransferase (CMP-KDO synthetase), the enzyme that activates KDO during rhamnogalacturonan II biosynthesis

Masaru Kobayashi, Nagisa Kouzu, Akina Inami, Kiminori Toyooka, Yuki Konishi, Ken Matsuoka, Toru Matoh

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Abstract

In plant cells, boron (B) occurs predominantly as a borate ester associated with rhamnogalacturonan II (RG-II), but the function of this B-RG-II complex has yet to be investigated. 3-Deoxy-d-manno-2-octulosonic acid (KDO) is a specific component monosaccharide of RG-II. Mutant plants defective in KDO biosynthesis are expected to have altered RG-II structure, and would be useful for studying the physiological function of the B-RG-II complex. Here, we characterized Arabidopsis CTP:KDO cytidylyltransferase (CMP-KDO synthetase; CKS), the enzyme activating KDO as a nucleotide sugar prior to its incorporation into RG-II. Our analyses localized the Arabidopsis CKS protein to mitochondria. The Arabidopsis CKS gene occurs as a single-copy gene in the genome, and we could not obtain cks null mutants from T-DNA insertion lines. Analysis using +/cks heterozygotes in the quartet1 background demonstrated that the cks mutation rendered pollen infertile through the inhibition of pollen tube elongation. These results suggest that KDO is an indispensable component of RG-II, and that the complete B-RG-II complex is essential for the cell wall integrity of rapidly growing tissues.

Original languageEnglish
Pages (from-to)1832-1843
Number of pages12
JournalPlant and Cell Physiology
Volume52
Issue number10
DOIs
Publication statusPublished - Oct 1 2011

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All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

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