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OsSGT1 Is a Glucosyltransferase Gene Involved in the Glucose Conjugation of Phenolics in Rice

  • Qian Liu
  • Yu-ying Zhang
  • Lu Chen
  • Ting-ting Chen
  • Yan-jie Li
  • Bing-kai HouEmail author
Original Paper

Abstract

Phenolics are a class of plant secondary metabolites that play important roles in plant growth and environmental adaptation. Glucosylation of phenolics is one of the molecular mechanisms controlling phenolics homeostasis. However, the relevant glucosyltransferases are largely unknown. In this study, a putative family 1 glucosyltransferase gene OsSGT1 was cloned from rice due to its close homology with the previously reported phenolics-related glucosyltransferases UGT84A1-A4, and the phylogenetic relationship of OsSGT1 with homologs from other species was investigated. Recombinant OsSGT1 protein showed strong activity towards phenolics to form their glucose conjugates. This is the first identified natural phenolics-related glucosyltransferase in rice. In addition, the expression patterns of OsSGT1 in different tissues of rice indicated that OsSGT1 was predominantly expressed in the old leaves and dough grains, suggesting that OsSGT1 might be involved in the maturation process of rice by regulating phenolic metabolism, and thus deepened our understanding on the roles of phenolics in rice growth and environmental adaptation.

Keywords

Oriza stiva Glucosyltransferase Glycosylation Phenolics Enzyme activity Expression pattern 

Notes

Contributions

BKH and QL conceived and designed the research. QL, YYZ, and LC conducted the experiments. TTC and YJL contributed analytical tools and analyzed data. QL, TTC, and BKH wrote the manuscript. All authors read and approved the manuscript.

Funding Information

This study was financially supported by key R & D project of Shandong Province of China (no. 2018GNC110019).

Compliance with Ethical Standards

Conflict of Interest

The authors declare that they have no conflict of interest.

Supplementary material

11105_2019_1134_MOESM1_ESM.docx (157 kb)
Fig S1 HPLC analysis of reaction mixtures of different phenolics with heat-inactivated OsSGT1 as negative control. (a-e) denote sinapic acid, ferulic acid, caffeic acid, cinnamic acid and coumaric acid, respectively; 1 denotes the reactions with inactivated GST-OsSGT1. 2 denotes the authentic standards of phenolics. (DOCX 157 kb)

References

  1. Blomstedt C-K, O'Donnell N-H, Bjarnholt N, Neale A-D, Hamill J-D, Møller B-L, Gleadow R-M (2016) Metabolic consequences of knocking out UGT85B1, the gene encoding the glucosyltransferase required for synthesis of dhurrin in Sorghum bicolor (L. Moench). Plant Cell Physiol 57:373–386CrossRefGoogle Scholar
  2. Boerjan W, Ralph J, Baucher M (2003) Lignin biosynthesis. Annu Rev Plant Bio 54:519–546CrossRefGoogle Scholar
  3. Booij-James I-S, Dube S-K, Jansen M-A, Edelman M, Mattoo A-K (2000) Ultraviolet-B radiation impacts light-mediated turnover of the photosystem II reaction center heterodimer in Arabidopsis mutants altered in phenolic metabolism. Plant Physiol 124:1275–1284CrossRefGoogle Scholar
  4. Brazier-Hicks M, Gershater M, Dixon D, Edwards R (2018) Substrate specificity and safener inducibility of the plant UDP-glucose-dependent family 1 glycosyltransferase super-family. Plant Biotechnol J 16:337–348CrossRefGoogle Scholar
  5. Chong J, Baltz R, Fritig B, Saindrenan P (1999) An early salicylic acid-, pathogen- and elicitor-inducible tobacco glucosyltransferase: role in compartmentalization of phenolics and H2O2 metabolism. FEBS Lett 458:204–208CrossRefGoogle Scholar
  6. Dudareva N, Pichersky E, Gershenzon J (2004) Biochemistry of plant volatiles. Plant Physiol 135:1893–1902CrossRefGoogle Scholar
  7. Franke H, Grosche J, Illes P, Allgaier C (2002) 5,7-Dihydroxytryptamine—a selective marker of dopaminergic or serotonergic neurons. Naunyn Schmiedeberg's Arch Pharmacol 366:315–318CrossRefGoogle Scholar
  8. Grace S-C, Logan B-A (2000) Energy dissipation and radical scavenging by the plant phenylpropanoid pathway. Philos Trans R Soc Lond Ser B Biol Sci 355:1499–1510CrossRefGoogle Scholar
  9. Hou B-K, Lim E-K, Higgins G-S, Bowles D-J (2004) N-Glucosylation of cytokinins by glycosyltransferases of Arabidopsis thaliana. J Biol Chem 279:47822–47832CrossRefGoogle Scholar
  10. Langenbach C, Campe R, Schaffrath U, Goellner K, Conrath U (2013) UDP-glucosyltransferase UGT84A2/BRT1 is required for Arabidopsis nonhost resistance to the Asian soybean rust pathogen Phakopsora pachyrhizi. New Phytol 198:536–545CrossRefGoogle Scholar
  11. Lanot A, Hodge D, Jackson R-G, George G-L, Elias L, Lim E-K, Vaistij F-E, Bowles D-J (2006) The glucosyltransferase UGT72E2 is responsible for monolignol 4-O-glucoside production in Arabidopsis thaliana. Plant J 48:286–295CrossRefGoogle Scholar
  12. Lim E-K, Ashford D-A, Hou B-K, Jackson R-G, Bowles D-J (2004) Arabidopsis glycosyltransferases as biocatalysts in fermentation for region selective synthesis of diverse quercetin glucosides. Biotechnol Bioeng 87:623–631CrossRefGoogle Scholar
  13. Lin J-S, Huang X-X, Li Q, Cao Y, Bao Y, Meng X-F, Li Y-J, Fu C, Hou B-K (2016) UDP-glycosyltransferase 72B1 catalyzes the glucose conjugation of monolignols and is essential for the normal cell wall lignification in Arabidopsis thaliana. Plant J 88:26–42CrossRefGoogle Scholar
  14. Lunkenbein S, Bellido M, Aharoni A, Salentijn E-M, Kaldenhoff R, Coiner H-A, Muñoz-Blanco J, Schwab W (2006) Characterization of a UDP-glucose:cinnamate glucosyltransferase from strawberry. Plant Physiol 140:1047–1058CrossRefGoogle Scholar
  15. Mathew S, Abraham T-E (2004) Ferulic acid: an antioxidant found naturally in plant cell walls and feruloyl esterases involved in its release and their applications. Crit Rev Biotechnol 24:59–83CrossRefGoogle Scholar
  16. Meissner D, Albert A, Böttcher C, Strack D, Milkowski C (2008) The role of UDP-glucose:hydroxycinnamate glucosyltransferases in phenylpropanoid metabolism and the response to UV-B radiation in Arabidopsis thaliana. Planta 228:663–674CrossRefGoogle Scholar
  17. Messner B, Thulke O, Schäffner A-R (2003) Arabidopsis glucosyltransferases with activities toward both endogenous and xenobiotic substrates. Planta 217:138–146PubMedGoogle Scholar
  18. Nicholson R-L, Hammerschmidt R (1992) Phenolic compounds and their role in disease resistance. Annu Rev Phytopathol 30:369–389CrossRefGoogle Scholar
  19. Ross J, Li Y, Lim E, Bowles D-J (2001) Higher plant glycosyltransferases. Genome Biol 2(3004):1–6Google Scholar
  20. Schoch G, Goepfert S, Morant M, Hehn A, Meyer D, Ullmann P, Werck-Reichhart D (2001) CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J Biol Chem 276:36566–36574CrossRefGoogle Scholar
  21. Thorsøe K-S, Bak S, Olsen C-E, Imberty A, Breton C, Lindberg Møller B (2005) Determination of catalytic key amino acids and UDP sugar donor specificity of the cyanohydrin glycosyltransferase UGT85B1 from Sorghum bicolor. Plant Physiol 139:664–673CrossRefGoogle Scholar
  22. Yonekura-Sakakibara K, Fukushima A, Nakabayashi R, Hanada K, Matsuda F, Sugawara S, Inoue E, Kuromori T, Ito T, Shinozaki K, Wangwattana B, Yamazaki M, Saito K (2012) Two glycosyltransferases involved in anthocyanin modification delineated by transcriptome independent component analysis in Arabidopsis thaliana. Plant J 69:154–167CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Qian Liu
    • 1
  • Yu-ying Zhang
    • 1
  • Lu Chen
    • 1
  • Ting-ting Chen
    • 1
  • Yan-jie Li
    • 1
  • Bing-kai Hou
    • 1
    Email author
  1. 1.The Key Laboratory of Plant Development and Environment Adaptation Biology, Ministry of Education; School of Life ScienceShandong UniversityQingdaoChina

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