Broaden the sugar donor selectivity of blackberry glycosyltransferase UGT78H2 through residual substitutions

Chen, Qing; Liu, Xunju; Hu, Yun; Wang, Yan; Sun, Bo; Chen, Tao; Luo, Yunbo; Zhang, Yong; Li, Mengyao; Liu, Zejing; Wang, Xiaorong; Tang, Haoru

doi:10.1016/j.ijbiomac.2020.10.184

Cited by 18 publications

(13 citation statements)

References 44 publications

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“…However, whether it can glycosylate other anthocyanidins or flavonols and participate in processes other than blotch formation in petals remains to be determined. UGT78H2 glycosylated quercetin exclusively using UDP-glucuronic acid and UDP-galactose, but not UDP-glucose [ 31 ]. In this study, we determined that PhUGT78A22 transferred glucose to glycosylated anthocyanins with UDP-glucose as the sugar donate, which was different from the results of Chen et al [ 31 ].…”

Section: Discussionmentioning

confidence: 99%

“…UGT78H2 glycosylated quercetin exclusively using UDP-glucuronic acid and UDP-galactose, but not UDP-glucose [ 31 ]. In this study, we determined that PhUGT78A22 transferred glucose to glycosylated anthocyanins with UDP-glucose as the sugar donate, which was different from the results of Chen et al [ 31 ]. This may be due to the differences of species resulting in functional diversification of group F UGTs so as to ensure the accurate modification of corresponding substrates.…”

Section: Discussionmentioning

confidence: 99%

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PhUGT78A22, a novel glycosyltransferase in Paeonia ‘He Xie’, can catalyze the transfer of glucose to glucosylated anthocyanins during petal blotch formation

Kong

Liu

et al. 2022

BMC Plant Biol

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Background Flower color patterns play an important role in the evolution and subsequent diversification of flowers by attracting animal pollinators. This interaction can drive the diversity observed in angiosperms today in many plant families such as Liliaceae, Paeoniaceae, and Orchidaceae, and increased their ornamental values. However, the molecular mechanism underlying the differential distribution of anthocyanins within petals remains unclear in Paeonia. Results In this study, we used an intersectional hybrid between the section Moutan and Paeonia, hereafter named Paeonia ‘He Xie’, which has purple flowers with dark purple blotches. After Ultra-high performance liquid chromatography-diode array detector (UPLC-DAD) analysis of blotched and non-blotched parts of petals, we found the anthocyanin content in the blotched part was always higher than that in the non-blotched part. Four kinds of anthocyanins, namely cyanidin-3-O-glucoside (Cy3G), cyanidin-3,5-O-glucoside (Cy3G5G), peonidin-3-O-glucoside (Pn3G), and peonidin-3,5-O-glucoside (Pn3G5G) were detected in the blotched parts, while only Cy3G5G and Pn3G5G were detected in the non-blotched parts. This suggests that glucosyltransferases may play a vital role in the four kinds of glucosylated anthocyanins in the blotched parts. Moreover, 2433 differentially expressed genes (DEGs) were obtained from transcriptome analysis of blotched and non-blotched parts, and a key UDP-glycosyltransferase named PhUGT78A22 was identified, which could use Cy3G and Pn3G as substrates to produce Cy3G5G and Pn3G5G, respectively, in vitro. Furthermore, silencing of PhUGT78A22 reduced the content of anthocyanidin 3,5-O-diglucoside in P. ‘He Xie’. Conclusions A UDP-glycosyltransferase, PhUGT78A22, was identified in P. ‘He Xie’, and the molecular mechanism underlying differential distribution of anthocyanins within petals was elucidated. This study provides new insights on the biosynthesis of different kinds of anthocyanins within colorful petals, and helps to explain petal blotch formation, which will facilitate the cultivar breeding with respect to increasing ornamental value. Additionally, it provides a reference for understanding the molecular mechanisms responsible for precise regulation of anthocyanin biosynthesis and distribution patterns.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

PhUGT78A22, a novel glycosyltransferase in Paeonia ‘He Xie’, can catalyze the transfer of glucose to glucosylated anthocyanins during petal blotch formation

Kong

Liu

et al. 2022

BMC Plant Biol

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“…Based on the model of UGT78D2 complex, two residues, His154 and Phe378, in proximity to quercetin were mutated into any other residue while quercetin was docked to the protein using Rosetta . Reasonable structures were chosen from 5000 poses according to the interface energy and the referable catalytic mechanism of UGTs …”

Section: Methodsmentioning

confidence: 99%

Three Glycosyltransferase Mutants in a One-Pot Multi-enzyme System with Enhanced Efficiency for Biosynthesis of Quercetin-3,4′-O-diglucoside

Tao

Shao

et al. 2023

J. Agric. Food Chem.

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Quercetin-3,4′-O-diglucoside (Q3,4′G), among the major dietary flavonoids, is superior to quercetin aglycone or quercetin monoglucoside in solubility. However, its low content in nature makes it hard to be prepared in large quantities by traditional extraction methods. In the present study, the F378S mutant of UGT78D2 (78D2_F378S) derived from Arabidopsis thaliana with improved regioselectivity and the V371A mutant of UGT73G1 (73G1_V371A) derived from Allium cepa were adopted to realize a two-step continuous glycosylation of quercetin to produce Q3,4′G. The mutation S31D was introduced to the sucrose synthase from Micractinium conductrix with enhanced activity, which was responsible for regenerating UDP-glucose by coupling with 78D2_F378S and 73G1_V371A. Using the aforementioned enzymes, prepared from the three-enzyme co-expression strain, 4.4 ± 0.03 g/L (7.0 ± 0.05 mM, yield 21.2%) Q3,4′G was produced from 10 g/L quercetin after reaction for 24 h at 45 °C.

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“…This experimental setup was successfully applied to confirm in planta the activity of UGT92G6 detected in vitro with caffeic acid [115]. Chen and colleagues evidenced the activity of UGT78H2 extracted from transiently modified tobacco leaves towards quercetin [116].…”

Section: Challenges and Perspectives In Ugt Researchmentioning

confidence: 96%

UGT72, a Major Glycosyltransferase Family for Flavonoid and Monolignol Homeostasis in Plants

Speeckaert

Jaziri

Baucher

et al. 2022

Biology

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Plants have developed the capacity to produce a diversified range of specialized metabolites. The glycosylation of those metabolites potentially decreases their toxicity while increasing their stability and their solubility, modifying their transport and their storage. The UGT, forming the largest glycosyltransferase superfamily in plants, combine enzymes that glycosylate mainly hormones and phenylpropanoids by using UDP-sugar as a sugar donor. Particularly, members of the UGT72 family have been shown to glycosylate the monolignols and the flavonoids, thereby being involved in their homeostasis. First, we explore primitive UGTs in algae and liverworts that are related to the angiosperm UGT72 family and their role in flavonoid homeostasis. Second, we describe the role of several UGT72s glycosylating monolignols, some of which have been associated with lignification. In addition, the role of other UGT72 members that glycosylate flavonoids and are involved in the development and/or stress response is depicted. Finally, the importance to explore the subcellular localization of UGTs to study their roles in planta is discussed.

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Broaden the sugar donor selectivity of blackberry glycosyltransferase UGT78H2 through residual substitutions

Cited by 18 publications

References 44 publications

PhUGT78A22, a novel glycosyltransferase in Paeonia ‘He Xie’, can catalyze the transfer of glucose to glucosylated anthocyanins during petal blotch formation

PhUGT78A22, a novel glycosyltransferase in Paeonia ‘He Xie’, can catalyze the transfer of glucose to glucosylated anthocyanins during petal blotch formation

Three Glycosyltransferase Mutants in a One-Pot Multi-enzyme System with Enhanced Efficiency for Biosynthesis of Quercetin-3,4′-O-diglucoside

UGT72, a Major Glycosyltransferase Family for Flavonoid and Monolignol Homeostasis in Plants

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