9LUM

Cryo-EM structure of Arabidopsis thaliana RGA in complex with GID1A

9LUM の概要

• エントリーDOI: 10.2210/pdb9lum/pdb
• EMDBエントリー: 63398
• 分子名称: DELLA protein RGA, Gibberellin receptor GID1A, GIBBERELLIN A3, ... (4 entities in total)
• 機能のキーワード: gibberellin, della motif, gras domain, plant growth, hormone
• 由来する生物種: Arabidopsis thaliana (thale cress); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103268.42

構造登録者

Islam, S.,Park, K.,Kwon, E.,Kim, D.Y. (登録日: 2025-02-09, 公開日: 2025-07-09, 最終更新日: 2025-07-23)

主引用文献

Islam, S.,Park, K.,Xia, J.,Kwon, E.,Kim, D.Y.
Structural insights into gibberellin-mediated DELLA protein degradation.
Mol Plant, 18:1210-1221, 2025

PubMed Abstract: 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.

PubMed: 40542507
DOI: 10.1016/j.molp.2025.06.010

実験手法

ELECTRON MICROSCOPY (2.66 Å)