Structures of D14 and D14L in the strigolactone and karrikin signaling pathways

Strigolactones (SLs) are plant hormones that inhibit shoot branching. DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14‐LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derive...

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Veröffentlicht in:Genes to cells : devoted to molecular & cellular mechanisms 2013-02, Vol.18 (2), p.147-160
Hauptverfasser: Kagiyama, Megumi, Hirano, Yoshinori, Mori, Tomoyuki, Kim, Sun‐Yong, Kyozuka, Junko, Seto, Yoshiya, Yamaguchi, Shinjiro, Hakoshima, Toshio
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container_issue 2
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container_title Genes to cells : devoted to molecular & cellular mechanisms
container_volume 18
creator Kagiyama, Megumi
Hirano, Yoshinori
Mori, Tomoyuki
Kim, Sun‐Yong
Kyozuka, Junko
Seto, Yoshiya
Yamaguchi, Shinjiro
Hakoshima, Toshio
description Strigolactones (SLs) are plant hormones that inhibit shoot branching. DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14‐LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derived from burnt vegetation as smoke stimulants of seed germination. We provide the first evidence for direct binding of the bioactive SL analogue GR24 to D14. Isothermal titration calorimetry measurements show a D14–GR24 binding affinity in the sub‐micromolar range. Similarly, bioactive KAR1 directly binds D14L in the micromolar range. The crystal structure of rice D14 shows a compact α‐/β‐fold hydrolase domain forming a deep ligand‐binding pocket capable of accommodating GR24. Insertion of four α‐helices between β6 strand and αD helix forms the helical cap of the pocket, although the pocket is open to the solvent. The pocket contains the conserved catalytic triad Ser‐His‐Asp aligned with the oxyanion hole, suggesting hydrolase activity. Although these structural characteristics are conserved in D14L, the D14L pocket is smaller than that of D14. The KAR‐insensitive mutation kai2‐1 is located at the prominent long β6‐αD1 loop, which is characteristic in D14 and D14L, but not in related α‐/β‐fold hydrolases.
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DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14‐LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derived from burnt vegetation as smoke stimulants of seed germination. We provide the first evidence for direct binding of the bioactive SL analogue GR24 to D14. Isothermal titration calorimetry measurements show a D14–GR24 binding affinity in the sub‐micromolar range. Similarly, bioactive KAR1 directly binds D14L in the micromolar range. The crystal structure of rice D14 shows a compact α‐/β‐fold hydrolase domain forming a deep ligand‐binding pocket capable of accommodating GR24. Insertion of four α‐helices between β6 strand and αD helix forms the helical cap of the pocket, although the pocket is open to the solvent. The pocket contains the conserved catalytic triad Ser‐His‐Asp aligned with the oxyanion hole, suggesting hydrolase activity. 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subjects Amino Acid Sequence
Catalytic Domain
Crystal structure
Enzymes
Furans - metabolism
Models, Molecular
Molecular Sequence Data
Mutation
Oryza - genetics
Oryza - metabolism
Oryza sativa
Plant Growth Regulators - chemistry
Plant Growth Regulators - metabolism
Plant Proteins - chemistry
Plant Proteins - metabolism
Protein Binding
Protein Conformation
Protein Stability
Pyrans - metabolism
Sequence Alignment
Signal Transduction
title Structures of D14 and D14L in the strigolactone and karrikin signaling pathways
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