β-Amyrin Synthase1 Controls the Accumulation of the Major Saponins Present in Pea (Pisum sativum).
DDMP saponin
Pea
Seed quality
TILLING
β-Amyrin synthase
Journal
Plant & cell physiology
ISSN: 1471-9053
Titre abrégé: Plant Cell Physiol
Pays: Japan
ID NLM: 9430925
Informations de publication
Date de publication:
01 Oct 2021
01 Oct 2021
Historique:
revised:
02
04
2021
received:
12
01
2021
accepted:
06
04
2021
pubmed:
8
4
2021
medline:
15
10
2021
entrez:
7
4
2021
Statut:
ppublish
Résumé
The use of pulses as ingredients for the production of food products rich in plant proteins is increasing. However, protein fractions prepared from pea or other pulses contain significant amounts of saponins, glycosylated triterpenes that can impart an undesirable bitter taste when used as an ingredient in foodstuffs. In this article, we describe the identification and characterization of a gene involved in saponin biosynthesis during pea seed development, by screening mutants obtained from two Pisum sativum TILLING (Targeting Induced Local Lesions IN Genomes) populations in two different genetic backgrounds. The mutations studied are located in a gene designated PsBAS1 (β-amyrin synthase1), which is highly expressed in maturing pea seeds and which encodes a protein previously shown to correspond to an active β-amyrin synthase. The first allele is a nonsense mutation, while the second mutation is located in a splice site and gives rise to a mis-spliced transcript encoding a truncated, nonfunctional protein. The homozygous mutant seeds accumulated virtually no saponin without affecting the seed nutritional or physiological quality. Interestingly, BAS1 appears to control saponin accumulation in all other tissues of the plant examined. These lines represent a first step in the development of pea varieties lacking bitterness off-flavors in their seeds. Our work also shows that TILLING populations in different genetic backgrounds represent valuable genetic resources for both crop improvement and functional genomics.
Identifiants
pubmed: 33826728
pii: 6214505
doi: 10.1093/pcp/pcab049
doi:
Substances chimiques
Plant Proteins
0
Saponins
0
Intramolecular Transferases
EC 5.4.-
2,3-oxidosqualene-beta-amyrin-cyclase
EC 5.4.99.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
784-797Subventions
Organisme : European Funds for Regional Development
ID : FEDER-FSE Bourgogne 2014/2020
Organisme : French Inter-Ministerial Unique Funds
Organisme : Region of Burgundy (France)
ID : AAP FUI 18
Organisme : Investment for the Future program PeaMUST
ID : ANR-11-BTBR-0002
Commentaires et corrections
Type : CommentIn
Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.