Dehydrin ERD14 activates glutathione transferase Phi9 in Arabidopsis thaliana under osmotic stress.
Active site titration
Chaperone
Enzyme activation
Hydrogen peroxide
Intrinsically disordered protein
Oxidative stress
Journal
Biochimica et biophysica acta. General subjects
ISSN: 1872-8006
Titre abrégé: Biochim Biophys Acta Gen Subj
Pays: Netherlands
ID NLM: 101731726
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
18
08
2019
revised:
12
12
2019
accepted:
18
12
2019
pubmed:
25
12
2019
medline:
29
8
2020
entrez:
25
12
2019
Statut:
ppublish
Résumé
Fully intrinsically disordered plant dehydrin ERD14 can protect enzymes via its chaperone-like activity, but it was not formally linked with enzymes of the plant redox system yet. This is of particular interest, as the level of H The proteomic mass-spectrometry analysis of stressed plants was performed to find the candidates affected by ERD14. With cross-linking, microscale thermophoresis, and active-site titration kinetics, the interaction and influence of ERD14 on the function of two target proteins: glutathione transferase Phi9 and catalase was examined. Under osmotic stress, redox enzymes, specifically the glutathione transferase Phi enzymes, are upregulated. Using microscale thermophoresis, we showed that ERD14 directly interacts with GSTF9 with a K We propose that fully intrinsically disordered dehydrin ERD14 might protect and even activate redox enzymes, helping plants to survive oxidative stress under dehydration conditions. ERD14 has a direct effect on the activity of redox enzymes.
Sections du résumé
BACKGROUND
Fully intrinsically disordered plant dehydrin ERD14 can protect enzymes via its chaperone-like activity, but it was not formally linked with enzymes of the plant redox system yet. This is of particular interest, as the level of H
METHODS
The proteomic mass-spectrometry analysis of stressed plants was performed to find the candidates affected by ERD14. With cross-linking, microscale thermophoresis, and active-site titration kinetics, the interaction and influence of ERD14 on the function of two target proteins: glutathione transferase Phi9 and catalase was examined.
RESULTS
Under osmotic stress, redox enzymes, specifically the glutathione transferase Phi enzymes, are upregulated. Using microscale thermophoresis, we showed that ERD14 directly interacts with GSTF9 with a K
CONCLUSIONS
We propose that fully intrinsically disordered dehydrin ERD14 might protect and even activate redox enzymes, helping plants to survive oxidative stress under dehydration conditions.
GENERAL SIGNIFICANCE
ERD14 has a direct effect on the activity of redox enzymes.
Identifiants
pubmed: 31870857
pii: S0304-4165(19)30295-8
doi: 10.1016/j.bbagen.2019.129506
pii:
doi:
Substances chimiques
Arabidopsis Proteins
0
ERD14 protein, Arabidopsis
0
Plant Proteins
0
dehydrin proteins, plant
134711-03-8
Hydrogen Peroxide
BBX060AN9V
GSTF9 protein, Arabidopsis
EC 2.5.1.18
Glutathione Transferase
EC 2.5.1.18
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
129506Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.