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Crystallization and initial X-ray data of abscisic acid receptor PYL3 in the presence of (-)-ABA.

ABSTRACT: Abscisic acid (ABA) modulates many complicated developmental processes and responses to environmental stimuli. Recently, several (+)-ABA signalling mechanisms by the RCAR/PYR1/PYL family of proteins (PYLs) have been proposed. However, the mechanism of the recognition and binding of the unnatural ligand (-)-ABA by PYLs has not yet been elucidated. In the present study, the expression, purification and crystallization of PYL3 in complex with (-)-ABA are reported. Diffraction data were refined to 2.65 Å resolution for this complex in space group P65. These findings will help to explain the stereospecificity of PYLs for (-)-ABA and to explore the selective ABA agonists.

SUBMITTER: Zhang X

PROVIDER: S-EPMC3660896 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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Crystallization and initial X-ray data of abscisic acid receptor PYL3 in the presence of (-)-ABA.

Zhang Xingliang X Zhang Qi Q Wang Guoqiang G

Acta crystallographica. Section F, Structural biology and crystallization communications 20130430 Pt 5

Abscisic acid (ABA) modulates many complicated developmental processes and responses to environmental stimuli. Recently, several (+)-ABA signalling mechanisms by the RCAR/PYR1/PYL family of proteins (PYLs) have been proposed. However, the mechanism of the recognition and binding of the unnatural ligand (-)-ABA by PYLs has not yet been elucidated. In the present study, the expression, purification and crystallization of PYL3 in complex with (-)-ABA are reported. Diffraction data were refined to 2 ...[more]

PMID: 23695572

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Project description:Abscisic acid (ABA)¹ is a plant hormone that controls many aspects of plant growth, including seed germination, stomatal aperture size, and cellular drought response. ABA interacts with a unique family of 14 receptor proteins. This interaction leads to the activation of a family of protein kinases, SnRK2s, which in turn phosphorylate substrates involved in many cellular processes. The family of receptors appears functionally redundant. To observe a measurable phenotype, four of the fourteen receptors have to be mutated to create a multilocus loss-of-function quadruple receptor (QR) mutant, which is much less sensitive to ABA than wild-type (WT) plants. Given these phenotypes, we asked whether or not a difference in ABA response between the WT and QR backgrounds would manifest on a phosphorylation level as well. We tested WT and QR mutant ABA response using isotope-assisted quantitative phosphoproteomics to determine what ABA-induced phosphorylation changes occur in WT plants within 5 min of ABA treatment and how that phosphorylation pattern is altered in the QR mutant. We found multiple ABA-induced phosphorylation changes that occur within 5 min of treatment, including three SnRK2 autophosphorylation events and phosphorylation on SnRK2 substrates. The majority of robust ABA-dependent phosphorylation changes observed were partially diminished in the QR mutant, whereas many smaller ABA-dependent phosphorylation changes observed in the WT were not responsive to ABA in the mutant. A single phosphorylation event was increased in response to ABA treatment in both the WT and QR mutant. A portion of the discovery data was validated using selected reaction monitoring-based targeted measurements on a triple quadrupole mass spectrometer. These data suggest that different subsets of phosphorylation events depend upon different subsets of the ABA receptor family to occur. Altogether, these data expand our understanding of the model by which the family of ABA receptors directs rapid phosphoproteomic changes.

Dataset Information

Crystallization and initial X-ray data of abscisic acid receptor PYL3 in the presence of (-)-ABA.

Publications

Crystallization and initial X-ray data of abscisic acid receptor PYL3 in the presence of (-)-ABA.

Similar Datasets

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