Modulation of abscisic acid signaling in vivo by an engineered receptor-insensitive protein phosphatase type 2C allele.

Détails

ID Serval
serval:BIB_700B285CFEFF
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Modulation of abscisic acid signaling in vivo by an engineered receptor-insensitive protein phosphatase type 2C allele.
Périodique
Plant physiology
Auteur⸱e⸱s
Dupeux F., Antoni R., Betz K., Santiago J., Gonzalez-Guzman M., Rodriguez L., Rubio S., Park S.Y., Cutler S.R., Rodriguez P.L., Márquez J.A.
ISSN
1532-2548 (Electronic)
ISSN-L
0032-0889
Statut éditorial
Publié
Date de publication
05/2011
Peer-reviewed
Oui
Volume
156
Numéro
1
Pages
106-116
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
The plant hormone abscisic acid (ABA) plays a crucial role in the control of the stress response and the regulation of plant growth and development. ABA binding to PYRABACTIN RESISTANCE1 (PYR1)/PYR1-LIKE (PYL)/REGULATORY COMPONENTS OF ABA RECEPTORS intracellular receptors leads to inhibition of key negative regulators of ABA signaling, i.e. clade A protein phosphatases type 2C (PP2Cs) such as ABA-INSENSITIVE1 and HYPERSENSITIVE TO ABA1 (HAB1), causing the activation of the ABA signaling pathway. To gain further understanding on the mechanism of hormone perception, PP2C inhibition, and its implications for ABA signaling, we have performed a structural and functional analysis of the PYR1-ABA-HAB1 complex. Based on structural data, we generated a gain-of-function mutation in a critical residue of the phosphatase, hab1(W385A), which abolished ABA-dependent receptor-mediated PP2C inhibition without impairing basal PP2C activity. As a result, hab1(W385A) caused constitutive inactivation of the protein kinase OST1 even in the presence of ABA and PYR/PYL proteins, in contrast to the receptor-sensitive HAB1, and therefore hab1(W385A) qualifies as a hypermorphic mutation. Expression of hab1(W385A) in Arabidopsis (Arabidopsis thaliana) plants leads to a strong, dominant ABA insensitivity, which demonstrates that this conserved tryptophan residue can be targeted for the generation of dominant clade A PP2C alleles. Moreover, our data highlight the critical role of molecular interactions mediated by tryptophan-385 equivalent residues for clade A PP2C function in vivo and the mechanism of ABA perception and signaling.
Mots-clé
Abscisic Acid/pharmacology, Arabidopsis/drug effects, Arabidopsis/enzymology, Arabidopsis/genetics, Arabidopsis/physiology, Arabidopsis Proteins/genetics, Arabidopsis Proteins/metabolism, Crystallography, X-Ray, Gene Expression Regulation, Plant, Germination, Membrane Transport Proteins/genetics, Membrane Transport Proteins/metabolism, Models, Molecular, Multiprotein Complexes, Mutation, Phosphoprotein Phosphatases/genetics, Phosphoprotein Phosphatases/metabolism, Plant Growth Regulators/pharmacology, Plants, Genetically Modified, Protein Kinases/genetics, Protein Kinases/metabolism, Protein Phosphatase 2C, Seedlings/drug effects, Seedlings/enzymology, Seedlings/genetics, Seedlings/physiology, Seeds/drug effects, Seeds/enzymology, Seeds/genetics, Seeds/physiology, Signal Transduction/drug effects, Tryptophan, Two-Hybrid System Techniques
Pubmed
Web of science
Open Access
Oui
Création de la notice
10/01/2019 18:23
Dernière modification de la notice
21/08/2019 6:35
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