ABI5 modulates seed germination via feedback regulation of the expression of the PYR/PYL/RCAR ABA receptor genes

2020 ◽  
Vol 228 (2) ◽  
pp. 596-608 ◽  
Author(s):  
Hongyun Zhao ◽  
Kaili Nie ◽  
Huapeng Zhou ◽  
Xiaojing Yan ◽  
Qidi Zhan ◽  
...  
Cell Reports ◽  
2021 ◽  
Vol 35 (11) ◽  
pp. 109263
Author(s):  
Pablo Albertos ◽  
Kiyoshi Tatematsu ◽  
Isabel Mateos ◽  
Inmaculada Sánchez-Vicente ◽  
Alejandro Fernández-Arbaizar ◽  
...  

PLoS Genetics ◽  
2021 ◽  
Vol 17 (12) ◽  
pp. e1009955
Author(s):  
Bo Zhao ◽  
Likai Wang ◽  
Zhengyao Shao ◽  
Kevin Chin ◽  
Daveraj Chakravarty ◽  
...  

Histone acetylation is involved in the regulation of seed germination. The transcription factor ABI5 plays an essential role in ABA- inhibited seed germination. However, the molecular mechanism of how ABI5 and histone acetylation coordinate to regulate gene expression during seed germination is still ambiguous. Here, we show that ENAP1 interacts with ABI5 and they co-bind to ABA responsive genes including ABI5 itself. The hypersensitivity to ABA of ENAP1ox seeds germination is recovered by the abi5 null mutation. ABA enhances H3K9Ac enrichment in the promoter regions as well as the transcription of target genes co-bound by ENAP1 and ABI5, which requires both ENAP1 and ABI5. ABI5 gene is directly regulated by ENAP1 and ABI5. In the enap1 deficient mutant, H3K9Ac enrichment and the binding activity of ABI5 in its own promoter region, along with ABI5 transcription and protein levels are all reduced; while in the abi5-1 mutant, the H3K9Ac enrichment and ENAP1 binding activity in ABI5 promoter are decreased, suggesting that ENAP1 and ABI5 function together to regulate ABI5- mediated positive feedback regulation. Overall, our research reveals a new molecular mechanism by which ENAP1 regulates H3K9 acetylation and mediates the positive feedback regulation of ABI5 to inhibit seed germination.


2021 ◽  
Vol 118 (38) ◽  
pp. e2108281118
Author(s):  
Aditya S. Vaidya ◽  
Francis C. Peterson ◽  
James Eckhardt ◽  
Zenan Xing ◽  
Sang-Youl Park ◽  
...  

Abscisic acid (ABA) is a key plant hormone that mediates both plant biotic and abiotic stress responses and many other developmental processes. ABA receptor antagonists are useful for dissecting and manipulating ABA’s physiological roles in vivo. We set out to design antagonists that block receptor–PP2C interactions by modifying the agonist opabactin (OP), a synthetically accessible, high-affinity scaffold. Click chemistry was used to create an ∼4,000-member library of C4-diversified opabactin derivatives that were screened for receptor antagonism in vitro. This revealed a peptidotriazole motif shared among hits, which we optimized to yield antabactin (ANT), a pan-receptor antagonist. An X-ray crystal structure of an ANT–PYL10 complex (1.86 Å) reveals that ANT’s peptidotriazole headgroup is positioned to sterically block receptor–PP2C interactions in the 4′ tunnel and stabilizes a noncanonical closed-gate receptor conformer that partially opens to accommodate ANT binding. To facilitate binding-affinity studies using fluorescence polarization, we synthesized TAMRA–ANT. Equilibrium dissociation constants for TAMRA–ANT binding to Arabidopsis receptors range from ∼400 to 1,700 pM. ANT displays improved activity in vivo and disrupts ABA-mediated processes in multiple species. ANT is able to accelerate seed germination in Arabidopsis, tomato, and barley, suggesting that it could be useful as a germination stimulant in species where endogenous ABA signaling limits seed germination. Thus, click-based diversification of a synthetic agonist scaffold allowed us to rapidly develop a high-affinity probe of ABA–receptor function for dissecting and manipulating ABA signaling.


1991 ◽  
Vol 83 (1) ◽  
pp. 34-40 ◽  
Author(s):  
Yohji Esashi ◽  
Shinichi Matsuyama ◽  
Hiroki Ashino ◽  
Maria Ogasawara ◽  
Ryo Hasegawa

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