Characterization of IRX10 and IRX10-like reveals an essential role in glucuronoxylan biosynthesis in Arabidopsis

Characterization of IRX10 and IRX10-like reveals an essential role in glucuronoxylan biosynthesis in Arabidopsis
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DOI:
10.1111/j.1365-313x.2008.03729.x
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发表时间:
2009-02-01
期刊:
影响因子:
7.2
通讯作者:
Turner, Simon R.
Turner, Simon R.
中科院分区:
生物学1区
文献类型:
--
作者:
Brown, David M.;Zhang, Zhinong;Turner, Simon R.

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木聚糖是拟南芥次生细胞壁中的主要半纤维素多糖,需要许多糖基转移酶 (GT) 来催化聚合物中发现的各种糖苷键的形成。在这项研究中,我们鉴定了 IRX10 和 IRX10 样 (IRX10-L),这两个编码糖基转移酶家族 47 (GT47) 成员的高度同源基因。 IRX10 中的 T-DNA 插入产生了轻微的不规则木质部 (irx) 表型,与次生细胞壁合成中的微小缺陷一致,而 IRX10-L 中含有突变的植物没有显示任何变化。然而,irx10 irx10-L 双突变体植物表现出更严重的 irx 和全植物表型,表明这两个基因之间存在相当大的功能冗余。对 irx10 irx10-L 双突变体的详细生化分析显示,次生细胞壁中的木聚糖大量减少,这与木聚糖生物合成的特定缺陷一致。此外,irx10 irx10-L突变体保留了拟南芥木聚糖还原端发现的独特寡糖,但β(1,4)木糖基转移酶活性严重降低。这些特征与 irx9 和 irx14 的特征相似,这两种突变体被认为在木聚糖链伸长方面存在缺陷,并且表明 IRX10 和 IRX10-L 在木聚糖主链的伸长中也发挥着作用。
Xylan, the major hemicellulosic polysaccharide in Arabidopsis secondary cell walls, requires a number of glycosyltransferases (GT) to catalyse formation of the various glycosidic linkages found in the polymer. In this study, we characterized IRX10 and IRX10-like (IRX10-L), two highly homologous genes encoding members of the glycosyltransferase family 47 (GT47). T-DNA insertions in IRX10 gave a mild irregular xylem (irx) phenotype consistent with a minor defect in secondary cell-wall synthesis, whereas plants containing mutations in IRX10-L showed no change. However, irx10 irx10-L double mutant plants showed a much more severe irx and whole-plant phenotype, suggesting considerable functional redundancy between these two genes. Detailed biochemical analysis of the irx10 irx10-L double mutant showed a large reduction of xylan in the secondary cell walls, consistent with a specific defect in xylan biosynthesis. Furthermore, the irx10 irx10-L mutant retains the unique oligosaccharide found at the reducing end of Arabidopsis xylan, but shows a severe reduction in beta(1,4) xylosyltransferase activity. These characteristics are similar to those of irx9 and irx14, mutants that are believed to be defective in xylan chain elongation, and suggests that IRX10 and IRX10-L also play a role in elongation of the xylan backbone.