Crystal structures of two phytohormone signal-transducing α/β hydrolases: karrikin-signaling KAI2 and strigolactone-signaling DWARF14

Zhao, Lihua; Zhou, Xuemei; Wu, Zhongshan; Yi, Wei; Xu, Yong; Li, Suling; Xu, Tianyuan; Liu, Yue; Chen, Runze; Kovach, Amanda; Kang, Yangyong; Li, Hou; He, Yuanzheng; Xie, Cen; Song, Wanling; Zhong, Dafang; Xu, Yechun; Wang, Yonghong; Li, Jiayang; Zhang, Chenghai; Melcher, Karsten; Xu, Hongjiao

doi:10.1038/cr.2013.19

Cited by 223 publications

(239 citation statements)

References 12 publications

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“…While the free D-ring of GR24 is biologically inactive and does not bind to D14, GR24 hydrolysis proceeds through formation of a covalently bound D-ring-derived reaction intermediate [24]. Since the radiolabel is localized to the D-ring, the SPA signal could be due to binding of either intact GR24 or the hydrolysis intermediate or product.…”

Section: Recombinant D14 Binds Gr24 or The Gr24 D-ring With µM Affinitymentioning

confidence: 99%

“…We and others have previously solved the crystal structures of apo-D14 (51-318) [24][25][26][27] and the complex of D14 covalently bound to the GR24 hydrolysis intermediate [24] or bound to the free, hydrolyzed D-ring [26]. In order to trap the complex of D14 with intact GR24, we co-crystallized the complex at a high molar ratio of GR24 to D14 and extensively screened crystallization conditions.…”

Section: Crystal Structure Of the Complex Formed Between D14 And Gr24mentioning

confidence: 99%

“…It can hydrolyze the synthetic SL GR24, albeit with an extremely low turnover rate of only about one molecule GR24 for every one molecule of D14 every three minutes [24] or less [25], and this hydrolysis has been proposed to be required for SL signaling [3,26]. Several groups reported high-resolution crystal structures of apo-D14 and its orthologs [24][25][26][27] and of KAI2 in apo- [23,24,27,28] and karrikin-bound [23] states. In contrast, attempts to co-crystallize D14 in complex with GR24 only yielded structures of D14 covalently bound to a GR24 hydrolysis intermediate [24] or weakly bound to the butenolide ring (D ring) hydrolysis product [26].…”

Section: Introductionmentioning

confidence: 99%

“…Several groups reported high-resolution crystal structures of apo-D14 and its orthologs [24][25][26][27] and of KAI2 in apo- [23,24,27,28] and karrikin-bound [23] states. In contrast, attempts to co-crystallize D14 in complex with GR24 only yielded structures of D14 covalently bound to a GR24 hydrolysis intermediate [24] or weakly bound to the butenolide ring (D ring) hydrolysis product [26]. Similarly, all attempts to crystallize a D14/SL/D3 complex have failed.…”

Section: Introductionmentioning

confidence: 99%

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Destabilization of strigolactone receptor DWARF14 by binding of ligand and E3-ligase signaling effector DWARF3

et al. 2015

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Strigolactones (SLs) are endogenous hormones and exuded signaling molecules in plant responses to low levels of mineral nutrients. Key mediators of the SL signaling pathway in rice include the α/β-fold hydrolase DWARF 14 (D14) and the F-box component DWARF 3 (D3) of the ubiquitin ligase SCF D3 that mediate ligand-dependent degradation of downstream signaling repressors. One perplexing feature is that D14 not only functions as the SL receptor but is also an active enzyme that slowly hydrolyzes diverse natural and synthetic SLs including GR24, preventing the crystallization of a binary complex of D14 with an intact SL as well as the ternary D14/SL/D3 complex. Here we overcome these barriers to derive a structural model of D14 bound to intact GR24 and identify the interface that is required for GR24-mediated D14-D3 interaction. The mode of GR24-mediated signaling, including ligand recognition, hydrolysis by D14, and ligand-mediated D14-D3 interaction, is conserved in structurally diverse SLs. More importantly, D14 is destabilized upon the binding of ligands and D3, thus revealing an unusual mechanism of SL recognition and signaling, in which the hormone, the receptor, and the downstream effectors are systematically destabilized during the signal transduction process.

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Section: Recombinant D14 Binds Gr24 or The Gr24 D-ring With µM Affinitymentioning

confidence: 99%

Section: Crystal Structure Of the Complex Formed Between D14 And Gr24mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Destabilization of strigolactone receptor DWARF14 by binding of ligand and E3-ligase signaling effector DWARF3

et al. 2015

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“…S5a,b) and, therefore, a substrate and a reactive water molecule could access to the cavity even in the crystal. D-OH may be produced via the reported intermediate, 2,4,4-trihydroxy-3-methyl-3-butenal 41 from the soaked ( À )-ent-2 0 -epi-GR7 (3) by an in-crystal activity of D14. This product is located at a site far from the catalytic triad residues and is surrounded by Val194, Ser270 and several aromatic residues, such as Phe186, Trp205, Tyr209 and Phe245 (Fig.…”

Section: D14 Forms a Complex With D-oh To Mediate Slr1 Interactionmentioning

confidence: 99%

Molecular mechanism of strigolactone perception by DWARF14

et al. 2013

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Strigolactones (SLs) are phytohormones that inhibit shoot branching and function in the rhizospheric communication with symbiotic fungi and parasitic weeds. An a/b-hydrolase protein, DWARF14 (D14), has been recognized to be an essential component of plant SL signalling, although its precise function remains unknown. Here we present the SL-dependent interaction of D14 with a gibberellin signalling repressor SLR1 and a possible mechanism of phytohormone perception in D14-mediated SL signalling. D14 functions as a cleavage enzyme of SLs, and the cleavage reaction induces the interaction with SLR1. The crystal structure of D14 shows that 5-hydroxy-3-methylbutenolide (D-OH), which is a reaction product of SLs, is trapped in the catalytic cavity of D14 to form an altered surface. The D14 residues recognizing D-OH are critical for the SL-dependent D14 À SLR1 interaction. These results provide new insight into crosstalk between gibberellin and SL signalling pathways.

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Strigolactone: Pflanzenhormone mit vielversprechenden Eigenschaften

et al. 2019

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Vor einigen Jahren, und damit fast 80 Jahre nach der Entdeckung des ersten Pflanzenhormons Auxin, wurde eine neue Klasse von Pflanzenhormonen – die Strigolactone – entdeckt. Diese Moleküle zeigen eine einzigartige biologische Aktivität in zahlreichen wichtigen biologischen Prozessen der Pflanzen, aber auch außerhalb von Pflanzen, nämlich in der Rhizosphäre, einer Erdschicht, die die Wurzeln umgibt und von Lebewesen wimmelt. Die Nutzung dieser erstaunlichen biologischen Aktivität ist nicht ohne Herausforderungen: Die Biosynthese von Strigolactonen ist kompliziert, und es ist schwierig, die erwünschte Aktivität zu konzipieren. Dieser Kurzaufsatz beschreibt den heutigen Stand der Wissenschaft im Bereich der Strigolactone und diskutiert, wie funktionelle Analoga entwickelt werden können, die möglicherweise zu einer nachhaltigen Landwirtschaft beitragen.

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Crystal structures of two phytohormone signal-transducing α/β hydrolases: karrikin-signaling KAI2 and strigolactone-signaling DWARF14

Cited by 223 publications

References 12 publications

Destabilization of strigolactone receptor DWARF14 by binding of ligand and E3-ligase signaling effector DWARF3

Destabilization of strigolactone receptor DWARF14 by binding of ligand and E3-ligase signaling effector DWARF3

Molecular mechanism of strigolactone perception by DWARF14

Strigolactone: Pflanzenhormone mit vielversprechenden Eigenschaften

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