Structural basis of NSP1-NSP2 heterodimerization and its regulatory mechanism in legume nodulation

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ID: 316506
2026
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Abstract
Abstract Legumes establish symbiotic relationships with rhizobia, leading to the development of nitrogen-fixing root nodules. Two GRAS transcription factors, Nodulation Signaling Pathway 1 (NSP1) and NSP2, are essential for Nod factor-induced transcription and subsequent nodulation in legumes. However, the structural basis of their interaction and functional mechanism remains poorly understood. Here, we report the crystal structure of the Medicago truncatula NSP1-NSP2 complex at 2.4 Å resolution. The structure reveals that NSP1 and NSP2 assemble into a heterodimer with a small, triangular interface exclusively composed of their leucine heptad repeat I (LHRI) motifs. This direct interaction is essential for nodulation, as NSP2 facilitates NSP1-DNA binding. Furthermore, we identified an HCCC-type zinc finger in NSP1 that modulates nodulation by influencing its DNA-binding activity. Together, our findings provide structural insights into NSP1-NSP2 heterodimerization and elucidate the regulatory mechanism underlying legume nodulation, offering a theoretical foundation for rationally engineering NSP1 and NSP2 to optimize plant-microbe relationships for agricultural applications.
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openalex_W7164082050 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Lihao Wan, Chunmei He, Chongyu Xue, Huangqi Chen, Xiakun Mao, Yaqi Peng, Xingming Lian, Xuelu Wang, Shutong Xu
Journal The Plant cell
Year 2026
DOI
10.1093/plcell/koag161
URL
https://doi.org/10.1093/plcell/koag161
Keywords Keywords not found

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