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-Structure paper
タイトル | Conformational Dynamics of the D53-D3-D14 Complex in Strigolactone Signaling. |
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ジャーナル・号・ページ | Plant Cell Physiol, Vol. 64, Issue 9, Page 1046-1056, Year 2023 |
掲載日 | 2023年9月15日 |
著者 | Simiao Liu / Jia Wang / Bin Song / Xinqi Gong / Huihui Liu / Qingliang Hu / Junhui Zhang / Qianqian Li / Jie Zheng / Hongwei Wang / H Eric Xu / Jiayang Li / Bing Wang / |
PubMed 要旨 | Strigolactones (SLs) play fundamental roles in regulating plant architecture, which is a major factor determining crop yield. The perception and signal transduction of SLs require the formation of a ...Strigolactones (SLs) play fundamental roles in regulating plant architecture, which is a major factor determining crop yield. The perception and signal transduction of SLs require the formation of a complex containing the receptor DWARF14 (D14), an F-box protein D3 and a transcriptional regulator D53 in an SL-dependent manner. Structural and biochemical analyses of D14 and its orthologs DAD2 and AtD14, D3 and the complexes of ASK1-D3-AtD14 and D3CTH-D14 have made great contributions to understanding the mechanisms of SL perception. However, structural analyses of D53 and the D53-D3-D14 holo-complex are challenging, and the biochemical mechanism underlying the complex assembly remains poorly understood. Here, we found that apo-D53 was rather flexible and reconstituted the holo-complex containing D53, S-phase kinase-associated protein 1 (SKP1), D3 and D14 with rac-GR24. The cryo-electron microscopy (cryo-EM) structure of SKP1-D3-D14 in the presence of D53 was analyzed and superimposed on the crystal structure of ASK1-D3-AtD14 without D53. No large conformational rearrangement was observed, but a 9Å rotation appeared between D14 and AtD14. Using hydrogen-deuterium exchange monitored by mass spectrometry, we analyzed dynamic motifs of D14, D3 and D53 in the D53-SKP1-D3-D14 complex assembly process and further identified two potential interfaces in D53 that are located in the N and D2 domains, respectively. Together, our results uncovered the dynamic conformational changes and built a model of the holo-complex D53-SKP1-D3-D14, offering valuable information for the biochemical and genetic mechanisms of SL perception and signal transduction. |
リンク | Plant Cell Physiol / PubMed:37384578 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 7.09 Å |
構造データ | EMDB-35402, PDB-8if6: |
由来 |
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キーワード | PLANT PROTEIN / D14 D3 D53 SL |