The UGT72 gene family encodes proteins that glycosylate phenylpropanoids, and thus contribute to the synthesis of various phenolic substances. However, their functional role and evolutionary history in Pyrus spp. remains poorly understood. Here we explored the evolution, amplification, coding region structural variation, and functional divergence of the UGT72 gene family and its subfamilies. Further, we identified functional genes involved in arbutin synthesis and functionally validated the key genes. 15 UGT72 genes were identified in the complete genome sequence and classified into two subfamilies of Pyrus betulifolia. Significant expansion of the UGT72 gene family occurred after genome duplication in P. betulifolia. 53.33 % of all UGT72 family genes were found to have undergone expansion via WGD/segmental duplication. A noteworthy discovery was that the amplification of functional genes such as PbUGT72B1714 during polyploidization, combined with the loss of vital motifs and variations at important sites within these genes, significantly impacted the diversification of arbutin metabolism. These findings offer novel insights into how gene gains and losses caused by WGDs have contributed to metabolic diversification and evolutionary adaptation in Pyrus, as well as a groundwork for more detailed investigations into the mechanisms of arbutin metabolism.
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http://dx.doi.org/10.1016/j.ijbiomac.2024.139005 | DOI Listing |
Int J Biol Macromol
December 2024
Research Institute of Pomology, Chinese Academy of Agricultural Sciences, Xingcheng, Liaoning Province 125100, China. Electronic address:
The UGT72 gene family encodes proteins that glycosylate phenylpropanoids, and thus contribute to the synthesis of various phenolic substances. However, their functional role and evolutionary history in Pyrus spp. remains poorly understood.
View Article and Find Full Text PDFFront Plant Sci
June 2022
School of Traditional Chinese Medicine, Shenyang Pharmaceutical University, Shenyang, China.
is a popular herbal medicine with its noticeable antiviral properties, which are primarily due to its lignan glycosides such as lariciresinol-4--β-D-glucoside and lariciresinol-4,4'-bis--β-D-glucosides (also called clemastanin B). UDP-glucose-dependent glycosyltransferases are the key enzymes involved in the biosynthesis of these antiviral metabolites. In this study, we systematically characterized the UGT72 family gene IiUGT1 and two UGT71B family genes, IiUGT4 and IiUGT71B5a, with similar enzymatic functions.
View Article and Find Full Text PDFFood Chem X
March 2022
Laboratory of Microbial Interaction, School of Biotechnology, Presidency University, Kolkata, West Bengal, India.
Flavour of tea is mainly contributed by a group of polyphenols - flavonoids. However, the content of flavonoid fluctuates seasonally and is found to be higher in the first flush of tea, when compared to the second flush. This disparity in the flavonoid content, and hence taste, incurs heavy economic losses to the tea plantation industry each harvest season.
View Article and Find Full Text PDFTree Physiol
May 2022
Laboratory of Plant Biotechnology, Université libre de Bruxelles, 12 rue des Profs Jeener et Brachet, Gosselies 6041, Belgium.
Reactive species (RS) causing oxidative stress are unavoidable by-products of various plant metabolic processes, such as photosynthesis, respiration or photorespiration. In leaves, flavonoids scavenge RS produced during photosynthesis and protect plant cells against deleterious oxidative damages. Their biosynthesis and accumulation are therefore under tight regulation at the cellular level.
View Article and Find Full Text PDFInt J Mol Sci
July 2020
Laboratoire de Biotechnologie Végétale, Université libre de Bruxelles (ULB), Rue des Professeurs Jeener et Brachet 12, 6041 Gosselies, Belgium.
Monolignols are the building blocks for lignin polymerization in the apoplastic domain. Monolignol biosynthesis, transport, storage, glycosylation, and deglycosylation are the main biological processes partaking in their homeostasis. In , members of the uridine diphosphate-dependent glucosyltransferases UGT72E and UGT72B subfamilies have been demonstrated to glycosylate monolignols.
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