The F8H Glycosyltransferase is a Functional Paralog of FRA8 Involved in Glucuronoxylan Biosynthesis in Arabidopsis
2009
Lee, Chanhui | Teng, Quincy | Huang, Wenlin | Zhong, Ruiqin | Ye, Zheng-Hua
The FRAGILE FIBER8 (FRA8) gene was previously shown to be required for the biosynthesis of the reducing end tetrasaccharide sequence of glucuronoxylan (GX) in Arabidopsis thaliana. Here, we demonstrate that F8H, a close homolog of FRA8, is a functional paralog of FRA8 involved in GX biosynthesis. The F8H gene is preferentially expressed in xylem cells, in which the secondary walls contain an abundant amount of GX, and the F8H protein is targeted to the Golgi where GX is synthesized. Overexpression of F8H in the fra8 mutant completely complemented the fra8 mutant phenotypes including the secondary wall thickness of fibers and vessels, vessel morphology, GX content and the abundance of the reducing end tetrasaccharide sequence of GX, indicating that F8H shares the same biochemical function as FRA8. Although the f8h mutant alone did not show any detectable cell wall defects, the f8h/fra8 double mutant exhibits an additional reduction in cell wall xylose level, a more severe deformation of vessels and an extreme retardation in plant growth compared with the fra8 mutant. Together, our findings suggest that F8H and FRA8 are functional paralogs and that they function redundantly in GX biosynthesis during secondary wall formation in the xylem.
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