The function of UDP-glycosyltransferases in plants and their possible use in crop protection.
Agriculture
Agrotechnology
Crop engineering
Glycosylation
Glycosyltransferases
Stress response
Journal
Biotechnology advances
ISSN: 1873-1899
Titre abrégé: Biotechnol Adv
Pays: England
ID NLM: 8403708
Informations de publication
Date de publication:
10 2023
10 2023
Historique:
received:
13
02
2023
revised:
18
05
2023
accepted:
18
05
2023
medline:
14
8
2023
pubmed:
3
6
2023
entrez:
2
6
2023
Statut:
ppublish
Résumé
Glycosyltransferases catalyse the transfer of a glycosyl moiety from a donor to an acceptor. Members of this enzyme class are ubiquitous throughout all kingdoms of life and are involved in the biosynthesis of countless types of glycosides. Family 1 glycosyltransferases, also referred to as uridine diphosphate-dependent glycosyltransferases (UGTs), glycosylate small molecules such as secondary metabolites and xenobiotics. In plants, UGTs are recognised for their multiple functionalities ranging from roles in growth regulation and development, in protection against pathogens and abiotic stresses and in adaptation to changing environments. In this study, we review UGT-mediated glycosylation of phytohormones, endogenous secondary metabolites, and xenobiotics and contextualise the role this chemical modification plays in the response to biotic and abiotic stresses and plant fitness. Here, the potential advantages and drawbacks of altering the expression patterns of specific UGTs along with the heterologous expression of UGTs across plant species to improve stress tolerance in plants are discussed. We conclude that UGT-based genetic modification of plants could potentially enhance agricultural efficiency and take part in controlling the biological activity of xenobiotics in bioremediation strategies. However, more knowledge of the intricate interplay between UGTs in plants is needed to unlock the full potential of UGTs in crop resistance.
Identifiants
pubmed: 37268151
pii: S0734-9750(23)00089-7
doi: 10.1016/j.biotechadv.2023.108182
pii:
doi:
Substances chimiques
Glycosyltransferases
EC 2.4.-
Uridine Diphosphate
58-98-0
Xenobiotics
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
108182Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare no competing interests.