LysM Receptor-Like Kinase LYK9 of Pisum Sativum L. May Regulate Plant Responses to Chitooligosaccharides Differing in Structure
| Autor: | Oksana Y. Shtark, Vyacheslav V. Dolgikh, Maria A Vashurina, Andrey D. Bovin, Elena A. Dolgikh, Igor V Sendersky, Olga A. Pavlova, Igor A. Tikhonovich, Alexandra V Dolgikh, I. V. Leppyanen |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0106 biological sciences
0301 basic medicine Receptor complex binding Mutant heterologous synthesis 01 natural sciences Catalysis Pisum Inorganic Chemistry Cell wall lcsh:Chemistry Pisum sativum L 03 medical and health sciences Sativum Extracellular Physical and Theoretical Chemistry phytopathogenic fungi Molecular Biology Gene lcsh:QH301-705.5 Spectroscopy lyk9 mutants biology Chemistry Kinase Organic Chemistry fungi lysin-motif receptor-like kinase PsLYK9 food and beverages General Medicine co-immunoprecipitation biology.organism_classification microscale thermophoresis Computer Science Applications 030104 developmental biology Biochemistry lcsh:Biology (General) lcsh:QD1-999 AM symbiosis 010606 plant biology & botany |
| Zdroj: | International Journal of Molecular Sciences Volume 22 Issue 2 International Journal of Molecular Sciences, Vol 22, Iss 711, p 711 (2021) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms22020711 |
| Popis: | This study focused on the interactions of pea (Pisum sativum L.) plants with phytopathogenic and beneficial fungi. Here, we examined whether the lysin-motif (LysM) receptor-like kinase PsLYK9 is directly involved in the perception of long- and short-chain chitooligosaccharides (COs) released after hydrolysis of the cell walls of phytopathogenic fungi and identified in arbuscular mycorrhizal (AM) fungal exudates. The identification and analysis of pea mutants impaired in the lyk9 gene confirmed the involvement of PsLYK9 in symbiosis development with AM fungi. Additionally, PsLYK9 regulated the immune response and resistance to phytopathogenic fungi, suggesting its bifunctional role. The existence of co-receptors may provide explanations for the potential dual role of PsLYK9 in the regulation of interactions with pathogenic and AM fungi. Co-immunoprecipitation assay revealed that PsLYK9 and two proposed co-receptors, PsLYR4 and PsLYR3, can form complexes. Analysis of binding capacity showed that PsLYK9 and PsLYR4, synthesized as extracellular domains in insect cells, were able to bind the deacetylated (DA) oligomers CO5-DA&ndash CO8-DA. Our results suggest that the receptor complex consisting of PsLYK9 and PsLYR4 can trigger a signal pathway that stimulates the immune response in peas. However, PsLYR3 seems not to be involved in the perception of CO4-5, as a possible co-receptor of PsLYK9. |
| Databáze: | OpenAIRE |
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