Next Article in Journal
Electrospun Water-Borne Polyurethane Nanofibrous Membrane as a Barrier for Preventing Postoperative Peritendinous Adhesion
Next Article in Special Issue
Biochemical and Anatomical Investigation of Sesbania herbacea (Mill.) McVaugh Nodules Grown under Flooded and Non-Flooded Conditions
Previous Article in Journal
Kidney Lipidomics by Mass Spectrometry Imaging: A Focus on the Glomerulus
Previous Article in Special Issue
Classical Soybean (Glycine max (L.) Merr) Symbionts, Sinorhizobium fredii USDA191 and Bradyrhizobium diazoefficiens USDA110, Reveal Contrasting Symbiotic Phenotype on Pigeon Pea (Cajanus cajan (L.) Millsp)
Open AccessArticle

Structural Variations in LysM Domains of LysM-RLK PsK1 May Result in a Different Effect on Pea–Rhizobial Symbiosis Development

1
All-Russia Research Institute for Agricultural Microbiology, Podbelsky chausse 3, Pushkin, 196608 St. Petersburg, Russia
2
Agroécologie, AgroSup Dijon, INRA, Univ. Bourgogne Franche-Comté, 21000 Dijon, France
3
IPS2, UMR9213/UMR1403, CNRS, INRA, UPSud, UPD, SPS, 91405 Orsay, France
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(7), 1624; https://doi.org/10.3390/ijms20071624
Received: 27 February 2019 / Revised: 18 March 2019 / Accepted: 19 March 2019 / Published: 1 April 2019
(This article belongs to the Special Issue Biological Nitrogen Fixation)
Lysin-motif receptor-like kinase PsK1 is involved in symbiosis initiation and the maintenance of infection thread (IT) growth and bacterial release in pea. We verified PsK1 specificity in relation to the Nod factor structure using k1 and rhizobial mutants. Inoculation with nodO and nodE nodO mutants significantly reduced root hair deformations, curling, and the number of ITs in k1-1 and k1-2 mutants. These results indicated that PsK1 function may depend on Nod factor structures. PsK1 with replacement in kinase domain and PsSYM10 co-production in Nicotiana benthamiana leaves did not induce a hypersensitive response (HR) because of the impossibility of signal transduction into the cell. Replacement of P169S in LysM3 domain of PsK1 disturbed the extracellular domain (ECD) interaction with PsSYM10′s ECD in Y2H system and reduced HR during the co-production of full-length PsK1 and PsSYM0 in N. benthamiana. Lastly, we explored the role of PsK1 in symbiosis with arbuscular mycorrhizal (AM) fungi; no significant differences between wild-type plants and k1 mutants were found, suggesting a specific role of PsK1 in legume–rhizobial symbiosis. However, increased sensitivity to a highly aggressive Fusarium culmorum strain was found in k1 mutants compared with the wild type, which requires the further study of the role of PsK1 in immune response regulation. View Full-Text
Keywords: legume–Rhizobium symbiosis; LysM receptor-like kinases; Nod factor perception; bacterial mutants; arbuscular mycorrhizal fungi; Fusarium culmorum fungi; pea Pisum sativum L. legume–Rhizobium symbiosis; LysM receptor-like kinases; Nod factor perception; bacterial mutants; arbuscular mycorrhizal fungi; Fusarium culmorum fungi; pea Pisum sativum L.
Show Figures

Figure 1

MDPI and ACS Style

Kirienko, A.N.; Vishnevskaya, N.A.; Kitaeva, A.B.; Shtark, O.Y.; Kozyulina, P.Y.; Thompson, R.; Dalmais, M.; Bendahmane, A.; Tikhonovich, I.A.; Dolgikh, E.A. Structural Variations in LysM Domains of LysM-RLK PsK1 May Result in a Different Effect on Pea–Rhizobial Symbiosis Development. Int. J. Mol. Sci. 2019, 20, 1624.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop