Role of a receptor-like kinase K1 in pea Rhizobium symbiosis development

• Published in: Planta Vol. 248; no. 5; pp. 1101 - 1120
• Main Authors: Kirienko, Anna N., Porozov, Yuri B., Malkov, Nikita V., Akhtemova, Gulnara A., Le Signor, Christine, Thompson, Richard, Saffray, Christine, Dalmais, Marion, Bendahmane, Abdelhafid, Tikhonovich, Igor A., Dolgikh, Elena A.
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Science + Business Media 01.11.2018; Springer Berlin Heidelberg; Springer Nature B.V; Springer Verlag
• Subjects: Agriculture; Biomedical and Life Sciences; Blotting, Western; Complementation; Complex formation; Developmental stages; Ecology; Environmental Sciences; Forestry; Genetic Engineering - methods; Hybrid systems; K1 gene; Kinases; Life Sciences; Nicotiana - genetics; ORIGINAL ARTICLE; Phenotypes; Phenotyping; Pisum sativum; Pisum sativum - enzymology; Pisum sativum - microbiology; Pisum sativum - physiology; Plant Leaves - enzymology; Plant Leaves - metabolism; Plant Proteins - physiology; Plant Sciences; Plants, Genetically Modified; Protein Kinases - physiology; Proteins; Receptors; Reverse Transcriptase Polymerase Chain Reaction; Rhizobium leguminosarum - physiology; Symbiosis; Two-Hybrid System Techniques; Vegetal Biology; Yeast; Yeasts; Nod factor perception; LysM receptor-like kinases; symbiosis; L; Pea; Heterologous expression; Legume; Mutants; Pisum sativum L; Legume-Rhizobium symbiosis
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/s00425-018-2944-4

The ability of the crop legume Pisum sativum L. to perceive the Nod factor rhizobial signals may depend on several receptors that differ in ligand structure specificity. Identification of pea mutants defective in two types of LysM receptor-like kinases (LysM-RLKs), SYM10 and SYM37, featuring different phenotypic manifestations and impaired at various stages of symbiosis development, corresponds well to this assumption. There is evidence that one of the receptor proteins involved in symbiosis initiation, SYM10, has an inactive kinase domain. This implies the presence of an additional component in the receptor complex, together with SYM10, that remains unknown. Here, we describe a new LysM-RLK, K1, which may serve as an additional component of the receptor complex in pea. To verify the function of K1 in symbiosis, several P. sativum non-nodulating mutants in the k1 gene were identified using the TILLING approach. Phenotyping revealed the blocking of symbiosis development at an appropriately early stage, strongly suggesting the importance of LysM-RLK K1 for symbiosis initiation. Moreover, the analysis of pea mutants with weaker phenotypes provides evidence for the additional role of K1 in infection thread distribution in the cortex and rhizobia penetration. The interaction between K1 and SYM10 was detected using transient leaf expression in Nicotiana benthamiana and in the yeast two-hybrid system. Since the possibility of SYM10/SYM37 complex formation was also shown, we tested whether the SYM37 and K1 receptors are functionally interchangeable using a complementation test. The interaction between K1 and other receptors is discussed.