A conserved juxtamembrane motif in plant NFR5 receptors is essential for root nodule symbiosis.
Autor: | Hansen SB; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Luu TB; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Gysel K; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Lironi D; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Krönauer C; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Rübsam H; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Jensen IB; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Tsitsikli M; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Birkefeldt TG; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Trgovcevic A; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Stougaard J; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Radutoiu S; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark., Andersen KR; Department of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus C, Denmark. |
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Jazyk: | angličtina |
Zdroj: | Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Nov 12; Vol. 121 (46), pp. e2405671121. Date of Electronic Publication: 2024 Nov 04. |
DOI: | 10.1073/pnas.2405671121 |
Abstrakt: | Establishment of root nodule symbiosis is initiated by the perception of bacterial Nod factor ligands by the plant LysM receptor kinases NFR1 and NFR5. Receptor signaling initiating the symbiotic pathway depends on the kinase activity of NFR1, while the signaling mechanism of the catalytically inactive NFR5 pseudokinase is unknown. Here, we present the crystal structure of the signaling-competent Lotus japonicus NFR5 intracellular domain, comprising the juxtamembrane region and pseudokinase domain. The juxtamembrane region is structurally well defined and forms two α-helices, αA and αA', which contain an exposed hydrophobic motif. We demonstrate that this "juxtamembrane motif" promotes NFR5-NFR5 and NFR1-NFR5 interactions and is essential for symbiotic signaling. Conservation analysis reveals that the juxtamembrane motif is present throughout NFR5-type receptors and is required for symbiosis signaling from barley RLK10, suggesting a conserved and broader function for this motif in plant-microbe symbioses. Competing Interests: Competing interests statement:Some findings from this article are considered for a patent application. |
Databáze: | MEDLINE |
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