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-Structure paper
| タイトル | Structural insights into gibberellin-mediated DELLA protein degradation. |
|---|---|
| ジャーナル・号・ページ | Mol Plant, Vol. 18, Issue 7, Page 1210-1221, Year 2025 |
| 掲載日 | 2025年7月7日 |
著者 | Soyaab Islam / Kunwoong Park / Jing Xia / Eunju Kwon / Dong Young Kim / ![]() |
| PubMed 要旨 | Gibberellin promotes plant growth by downregulating DELLA proteins, which act as growth repressors. In the presence of gibberellin, the gibberellin receptor GID1 binds DELLA proteins, triggering ...Gibberellin promotes plant growth by downregulating DELLA proteins, which act as growth repressors. In the presence of gibberellin, the gibberellin receptor GID1 binds DELLA proteins, triggering their degradation through polyubiquitination by the SCF ubiquitin E3 ligase. Despite extensive studies, the molecular mechanisms by which DELLA proteins assemble with SCF to regulate plant growth remain poorly understood. Here, we present two cryo-electron microscopy structures of the Arabidopsis thaliana DELLA protein RGA in complex with GID1A and GID1A-SLY1-ASK2, respectively. Structural analyses revealed that RGA interacts with GID1A and SLY1 through nonoverlapping binding surfaces, stabilizing the proteins. This suggests that the SCF-RGA-GID1A complex assembles through a stepwise stabilization process induced by gibberellin. Furthermore, structural comparison with GRAS proteins indicates that RGA does not interact with IDD-family transcription factors when bound to SLY1, suggesting that DELLA protein binding to GID1/SLY1 and to transcription factors is mutually exclusive. These findings provide new insights into the gibberellin-mediated regulation of transcription factor activity by DELLA proteins. |
リンク | Mol Plant / PubMed:40542507 |
| 手法 | EM (単粒子) |
| 解像度 | 2.66 - 3.07 Å |
| 構造データ | EMDB-63398, PDB-9lum: EMDB-63399, PDB-9lun: EMDB-63400, PDB-9luo: EMDB-63401, PDB-9lup: |
| 化合物 | ![]() ChemComp-GA3: ![]() ChemComp-HOH: |
| 由来 |
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キーワード | HORMONE / Gibberellin / DELLA motif / GRAS domain / Plant growth |
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