Abstract

UDP-glucose dehydrogenase (UGD; EC1.1.1.22) is a NAD+-dependent enzyme that catalyzes the two-fold oxidation of UDP-glucose (UDP-Glc) to produce UDP-glucuronic acid and plays an important role in plant cell wall synthesis. A total of 42 UGD genes from four Gossypium genomes including G. hirsutum, G. arboretum, G. barbadense, and G. raimondii were identified and found that the UGD gene family has conservative evolution patterns in gene structure and protein domain. The growth of fibers can be effectively promoted after adding the UDP-Glc to the medium, and the GhUGD gene expression enhanced. In addition, the transgenic Arabidopsis lines over-expressing GH_D12G1806 had longer root lengths and higher gene expression level than the wild-type plants of Columbia-0. These results indicated that UGD may play important roles in cotton fiber development and has a guiding significance for dissecting fiber development mechanism.

Highlights

  • Cotton fiber is the most important textile raw material

  • Each subgroup of Gossypium UDP-glucose dehydrogenase (UGD) consists of six members including one from A genome (G. arboreum; Du et al, 2018; see text footnote 3), one from D genome (G. raimondii; Paterson et al, 2012; see text footnote 5), two from G. hirsutum, and two from G. barbadense

  • There is one subgroup in UGD-I that has four UGDs, in which there is no UGD from G. arboreum and G. raimondii identified

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Summary

Introduction

Cotton fiber is the most important textile raw material. Its primary cell wall components, including pectin, hemicellulose, and cellulose, are mainly derived from a common biochemical precursor, UDP-glucuronic acid (UDP-GlcA; Hofte and Voxeur, 2017), which is responsible for the derivation of about 50% of the cell wall biomass (Zablackis et al, 1995). Plants have evolved two independent pathways for the synthesis of UDP-GlcA. One pathway consists of conversion of UDP-glucose (UDP-Glc) to UDP-GalA catalyzed by UDP-glucose dehydrogenase (UGD, which belongs to the family of NAD+-linked oxidoreductase; EC 1.1.1.22; Tenhaken and Thulke, 1996). The other is the more complex myo-inositol pathway, in which cleavage of inositol into D-GlcA catalyzed. D-GlcA is activated to UDP-GlcA (Loewus et al, 1962; Seitz et al, 2000; Ute et al, 2004; Kanter et al, 2005; Pieslinger et al, 2010). Further analysis revealed that an alternative pathway to UDP-GlcA via UDP-Glc is compensatorily up-regulated in these mutants (Endres and Tenhaken, 2011)

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