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Review
. 2021 May 28;10(6):1087.
doi: 10.3390/plants10061087.

An Update on Crop ABA Receptors

Rafael Ruiz-Partida  1 , Sttefany M Rosario  1   2 , Jorge Lozano-Juste  1
Affiliations
Review

An Update on Crop ABA Receptors

Rafael Ruiz-Partida et al. Plants (Basel). .

Abstract

The hormone abscisic acid (ABA) orchestrates the plant stress response and regulates sophisticated metabolic and physiological mechanisms essential for survival in a changing environment. Plant ABA receptors were described more than 10 years ago, and a considerable amount of information is available for the model plant Arabidopsis thaliana. Unfortunately, this knowledge is still very limited in crops that hold the key to feeding a growing population. In this review, we summarize genomic, genetic and structural data obtained in crop ABA receptors. We also provide an update on ABA perception in major food crops, highlighting specific and common features of crop ABA receptors.

Keywords: ABA; PYR/PYL; crop; drought; phylogenetic; receptor; structure.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
ABA receptors in different crops. Cladograms (A) and circular phylogenetic tree (B) of PYR/PYLs in eudicot and monocot food crops. Receptors are grouped in three different subfamilies: subfamily I (purple), subfamily II (green) and subfamily III (red). Cladograms and the circular phylogenetic tree were built with the maximum likelihood method. The phylogenetic tree was built using 1000 bootstraps in MEGA. Numbers indicate bootstrap values.
Figure 2
Figure 2
Gene expression of the ABA receptors in different crops. The expression levels of the different genes are represented with increasing purple intensities as indicated in the legend. Expression data were extracted from the references indicated in the text [39,41,42,45,46,49,74].
Figure 3
Figure 3
Conformational states of a crop ABA receptor. Superimposition of the CsPYL1 crystal structures corresponding to the apo (PDB ID: 5MMQ), ABA-bound (PDB ID: 5MMX) and ternary complex (PDB ID: 5MN0) forms. The highly conserved latch and gate are highlighted in solid colors.
Figure 4
Figure 4
Arabidopsis and crop ABA-receptors adopt a similar latch-closed/gate-closed conformation upon PP2C binding. Structural alignment of PYL:ABA:PP2C ternary complexes from Arabidopsis thaliana (PDB ID: 3KDJ), Citrus sinensis (PDB ID: 5MN0) and Oryza sativa (PDB ID: 4OIC and 5GWP). The bottom panel shows a zoomed-in view of the PP2C tryptophan-lock highlighted in solid colors, similar to the gate and the latch loops.
Figure 5
Figure 5
The latch-closed/gate-open ABA-bound intermediate. (A) Structural alignment of a latch-closed/gate-open ABA-bound conformation of citrus PYL1 (CsPYL1) (PDB ID: 5MMX), tomato PYL1 (SlPYL1) (PDB ID: 5MOB) and PYR1 from turfgrass (FePYR1) (PDB ID: 5UJV). Latch and gate are highlighted in solid colors. (B) Superimposition of the latch-closed/gate-open and latch-closed/gate-closed ABA-bound molecules from FePYR1 crystal structure (PDB ID: 5UJV). Latch and gate are highlighted in solid colors.
Figure 6
Figure 6
Model of the molecular mechanism for ABA perception. CsPYL1 crystal structures of the apo (PDB ID: 5MMQ), ABA-bound (PDB ID: 5MMX) and ternary complex (PDB ID: 5MN0) forms were used to elaborate this model. Conformational equilibriums of the apo and the ABA-bound forms are represented by horizontal arrows.
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