Detoxification of monoterpenes by a family of plant glycosyltransferases. (November 2022)
- Record Type:
- Journal Article
- Title:
- Detoxification of monoterpenes by a family of plant glycosyltransferases. (November 2022)
- Main Title:
- Detoxification of monoterpenes by a family of plant glycosyltransferases
- Authors:
- Karlova, Rumyana
Busscher, Jeroen
Schempp, Florence M.
Buchhaupt, Markus
van Dijk, Aalt D.J.
Beekwilder, Jules - Abstract:
- Abstract: Plant monoterpenes are challenging compounds, since they often act as solvents, and thus have both phytotoxic and antimicrobial properties. In this study an approach is developed to identify and characterize enzymes that can detoxify monoterpenoids, and thus would protect both plants and microbial production systems from these compounds. Plants respond to the presence of monoterpenes by expressing glycosyltransferases (UGTs), which conjugate the monoterpenoids into glycosides. By identifying these enzymes in a transcriptomics approach using Mentha × piperita, a family of UGTs was identified which is active on cyclic monoterpenoids such as menthol, and on acyclic monoterpenoids such as geranic acid. Other members of this family, from tomato, were also shown to be active on these monoterpenoids. In vitro and in vivo activity of different UGTs were tested with different substrates. We found that some glycosyltransferases significantly affect the toxicity of selected monoterpenoids in Escherichia coli, suggesting that glycosyltransferases can protect cells from monoterpenoid toxicity. Graphical abstract: A new clade of glucosyltransferases with members from mint and tomato is able to detoxify monoterpene alcohols. Image 1 Highlights: A glycosyltransferase clade glycosylates monoterpenoids menthol and geranic acid. Members from Mentha x piperita and from Solanum lycopersicum were characterized. Toxicity of monoterpenoids in bacterial growth assays is mitigated byAbstract: Plant monoterpenes are challenging compounds, since they often act as solvents, and thus have both phytotoxic and antimicrobial properties. In this study an approach is developed to identify and characterize enzymes that can detoxify monoterpenoids, and thus would protect both plants and microbial production systems from these compounds. Plants respond to the presence of monoterpenes by expressing glycosyltransferases (UGTs), which conjugate the monoterpenoids into glycosides. By identifying these enzymes in a transcriptomics approach using Mentha × piperita, a family of UGTs was identified which is active on cyclic monoterpenoids such as menthol, and on acyclic monoterpenoids such as geranic acid. Other members of this family, from tomato, were also shown to be active on these monoterpenoids. In vitro and in vivo activity of different UGTs were tested with different substrates. We found that some glycosyltransferases significantly affect the toxicity of selected monoterpenoids in Escherichia coli, suggesting that glycosyltransferases can protect cells from monoterpenoid toxicity. Graphical abstract: A new clade of glucosyltransferases with members from mint and tomato is able to detoxify monoterpene alcohols. Image 1 Highlights: A glycosyltransferase clade glycosylates monoterpenoids menthol and geranic acid. Members from Mentha x piperita and from Solanum lycopersicum were characterized. Toxicity of monoterpenoids in bacterial growth assays is mitigated by these enzymes. This suggests their involvement in detoxification of monoterpenoids in plants. … (more)
- Is Part Of:
- Phytochemistry. Volume 203(2022)
- Journal:
- Phytochemistry
- Issue:
- Volume 203(2022)
- Issue Display:
- Volume 203, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 203
- Issue:
- 2022
- Issue Sort Value:
- 2022-0203-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-11
- Subjects:
- Mentha × piperita L -- Lamiaceae -- Solanum lycopersicum L. Solanaceae -- Monoterpene -- Glycosyltransferase -- Menthol -- Geranic acid
Botanical chemistry -- Periodicals
Biochemistry -- Periodicals
Botany -- Periodicals
Chimie végétale -- Périodiques
572.2 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00319422 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.phytochem.2022.113371 ↗
- Languages:
- English
- ISSNs:
- 0031-9422
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6489.800000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 23976.xml