DELLA proteins are common components of symbiotic rhizobial and mycorrhizal signalling pathways

Legumes form symbiotic associations with either nitrogen-fixing bacteria or arbuscular mycorrhizal fungi. Formation of these two symbioses is regulated by a common set of signalling components that act downstream of recognition of rhizobia or mycorrhizae by host plants. Central to these pathways is...

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Veröffentlicht in:Nature communications 2016-08, Vol.7 (1), p.12433-12433, Article 12433
Hauptverfasser: Jin, Yue, Liu, Huan, Luo, Dexian, Yu, Nan, Dong, Wentao, Wang, Chao, Zhang, Xiaowei, Dai, Huiling, Yang, Jun, Wang, Ertao
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Sprache:eng
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Zusammenfassung:Legumes form symbiotic associations with either nitrogen-fixing bacteria or arbuscular mycorrhizal fungi. Formation of these two symbioses is regulated by a common set of signalling components that act downstream of recognition of rhizobia or mycorrhizae by host plants. Central to these pathways is the calcium and calmodulin-dependent protein kinase (CCaMK)–IPD3 complex which initiates nodule organogenesis following calcium oscillations in the host nucleus. However, downstream signalling events are not fully understood. Here we show that Medicago truncatula DELLA proteins, which are the central regulators of gibberellic acid signalling, positively regulate rhizobial symbiosis. Rhizobia colonization is impaired in della mutants and we provide evidence that DELLAs can promote CCaMK–IPD3 complex formation and increase the phosphorylation state of IPD3. DELLAs can also interact with NSP2–NSP1 and enhance the expression of Nod-factor-inducible genes in protoplasts. We show that DELLA is able to bridge a protein complex containing IPD3 and NSP2. Our results suggest a transcriptional framework for regulation of root nodule symbiosis. Symbiotic associations between legumes and nitrogen-fixing bacteria are regulated by a CCaMK-IPD3 protein complex which promotes nodule initiation. Here, Jin et al . propose that DELLA proteins positively regulate nodulation by enhancing phosphorylation of IPD3 and acting as a positive regulator of transcription.
ISSN:2041-1723
2041-1723
DOI:10.1038/ncomms12433