Correlation between expression and activity of ADP glucose pyrophosphorylase and starch synthase and their role in starch accumulation during grain filling under drought stress in rice.
AGPL
AGPS
AGPase
Drought
Rice
SS
Starch synthase
Journal
Plant physiology and biochemistry : PPB
ISSN: 1873-2690
Titre abrégé: Plant Physiol Biochem
Pays: France
ID NLM: 9882449
Informations de publication
Date de publication:
Dec 2020
Dec 2020
Historique:
received:
14
08
2020
accepted:
20
10
2020
pubmed:
2
11
2020
medline:
28
1
2021
entrez:
1
11
2020
Statut:
ppublish
Résumé
ADP glucose pyrophosphorylase (AGPase, EC 2.7.7.27) and starch synthase (SS, EC 2.4.1.21) are key regulatory enzymes involved in the starch biosynthesis. Comprehensive analysis of transcription levels of ADP-glucose pyrophosphorylase and starch synthase genes was performed in leaves, roots, and developing grains of drought susceptible (IR64) and drought-tolerant (N22) cultivars under applied water deficit stress (WDS). AGPase and SS genes are differentially regulated in leaves, roots, and grains under the drought stress. The expression pattern of SS and AGPase genes was correlated with the activity of both AGPase, SS, and starch content of developing grains under the drought. Drought stress reduced transitory starch in leaves and enhanced storage starch in developing grains. An increase in the activity of AGPase in developing grains was due to induced expression of ADP glucose pyrophosphorylase large subunit 3 (AGPL3) in N22 and both ADP glucose pyrophosphorylase small subunit 2 (AGPS2) & ADP glucose pyrophosphorylase large subunit 3 (AGPL3) in IR64 and a positive correlation was established with starch content. Similarly, an increase in the SS activity in developing grains was due to induced expression of soluble starch synthase (SSIIB, SSIVA, and SSIVB) in N22 and SSIVB in IR64.
Identifiants
pubmed: 33130401
pii: S0981-9428(20)30520-9
doi: 10.1016/j.plaphy.2020.10.018
pii:
doi:
Substances chimiques
Plant Proteins
0
Starch
9005-25-8
Starch Synthase
EC 2.4.1.21
Glucose-1-Phosphate Adenylyltransferase
EC 2.7.7.27
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
239-243Informations de copyright
Copyright © 2020. Published by Elsevier Masson SAS.