Comparative analysis of Arabidopsis UGT74 glucosyltransferases reveals a special role of UGT74C1 in glucosinolate biosynthesis. (13th June 2014)
- Record Type:
- Journal Article
- Title:
- Comparative analysis of Arabidopsis UGT74 glucosyltransferases reveals a special role of UGT74C1 in glucosinolate biosynthesis. (13th June 2014)
- Main Title:
- Comparative analysis of Arabidopsis UGT74 glucosyltransferases reveals a special role of UGT74C1 in glucosinolate biosynthesis
- Authors:
- Grubb, C. Douglas
Zipp, Brandon J.
Kopycki, Jakub
Schubert, Melvin
Quint, Marcel
Lim, Eng‐Kiat
Bowles, Dianna J.
Pedras, M. Soledade C.
Abel, Steffen - Abstract:
- <abstract abstract-type="main" id="tpj12541-abs-0001"> <title>Summary</title> <p>The study of glucosinolates and their regulation has provided a powerful framework for the exploration of fundamental questions about the function, evolution, and ecological significance of plant natural products, but uncertainties about their metabolism remain. Previous work has identified one thiohydroximate <italic>S</italic>‐glucosyltransferase, UGT74B1, with an important role in the core pathway, but also made clear that this enzyme functions redundantly and cannot be the sole UDP‐glucose dependent glucosyltransferase (UGT) in glucosinolate synthesis. Here, we present the results of a nearly comprehensive <italic>in vitro</italic> activity screen of recombinant Arabidopsis Family 1 UGTs, which implicate other members of the UGT74 clade as candidate glucosinolate biosynthetic enzymes. Systematic genetic analysis of this clade indicates that UGT74C1 plays a special role in the synthesis of aliphatic glucosinolates, a conclusion strongly supported by phylogenetic and gene expression analyses. Finally, the ability of <italic>UGT74C1</italic> to complement phenotypes and chemotypes of the <italic>ugt74b1‐2</italic> knockout mutant and to express thiohydroximate UGT activity <italic>in planta</italic> provides conclusive evidence for UGT74C1 being an accessory enzyme in glucosinolate biosynthesis with a potential function during plant adaptation to environmental challenge.</p> </abstract>
- Is Part Of:
- Plant journal. Volume 79:Number 1(2014:Jul.)
- Journal:
- Plant journal
- Issue:
- Volume 79:Number 1(2014:Jul.)
- Issue Display:
- Volume 79, Issue 1 (2014)
- Year:
- 2014
- Volume:
- 79
- Issue:
- 1
- Issue Sort Value:
- 2014-0079-0001-0000
- Page Start:
- 92
- Page End:
- 105
- Publication Date:
- 2014-06-13
- Subjects:
- Plant molecular biology -- Periodicals
Plant cells and tissues -- Periodicals
Botany -- Periodicals
580 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-313X ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/tpj.12541 ↗
- Languages:
- English
- ISSNs:
- 0960-7412
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6519.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3081.xml