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Lysm receptor-like kinase lyk9 of pisum sativum l. May regulate plant responses to chitooligosaccharides differing in structure. / Leppyanen, Irina V.; Pavlova, Olga A.; Vashurina, Maria A.; Bovin, Andrey D.; Dolgikh, Alexandra V.; Shtark, Oksana Y.; Sendersky, Igor V.; Dolgikh, Vyacheslav V.; Tikhonovich, Igor A.; Dolgikh, Elena A.

в: International Journal of Molecular Sciences, Том 22, № 2, 711, 12.01.2021, стр. 1-16.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

Leppyanen, IV, Pavlova, OA, Vashurina, MA, Bovin, AD, Dolgikh, AV, Shtark, OY, Sendersky, IV, Dolgikh, VV, Tikhonovich, IA & Dolgikh, EA 2021, 'Lysm receptor-like kinase lyk9 of pisum sativum l. May regulate plant responses to chitooligosaccharides differing in structure', International Journal of Molecular Sciences, Том. 22, № 2, 711, стр. 1-16. https://doi.org/10.3390/ijms22020711

APA

Leppyanen, I. V., Pavlova, O. A., Vashurina, M. A., Bovin, A. D., Dolgikh, A. V., Shtark, O. Y., Sendersky, I. V., Dolgikh, V. V., Tikhonovich, I. A., & Dolgikh, E. A. (2021). Lysm receptor-like kinase lyk9 of pisum sativum l. May regulate plant responses to chitooligosaccharides differing in structure. International Journal of Molecular Sciences, 22(2), 1-16. [711]. https://doi.org/10.3390/ijms22020711

Vancouver

Leppyanen IV, Pavlova OA, Vashurina MA, Bovin AD, Dolgikh AV, Shtark OY и пр. Lysm receptor-like kinase lyk9 of pisum sativum l. May regulate plant responses to chitooligosaccharides differing in structure. International Journal of Molecular Sciences. 2021 Янв. 12;22(2):1-16. 711. https://doi.org/10.3390/ijms22020711

Author

Leppyanen, Irina V. ; Pavlova, Olga A. ; Vashurina, Maria A. ; Bovin, Andrey D. ; Dolgikh, Alexandra V. ; Shtark, Oksana Y. ; Sendersky, Igor V. ; Dolgikh, Vyacheslav V. ; Tikhonovich, Igor A. ; Dolgikh, Elena A. / Lysm receptor-like kinase lyk9 of pisum sativum l. May regulate plant responses to chitooligosaccharides differing in structure. в: International Journal of Molecular Sciences. 2021 ; Том 22, № 2. стр. 1-16.

BibTeX

@article{6c894c7fde254ef3afc847506d4d75d7,
title = "Lysm receptor-like kinase lyk9 of pisum sativum l. May regulate plant responses to chitooligosaccharides differing in structure",
abstract = "This study focused on the interactions of pea (Pisum sativum L.) plants with phytopatho-genic 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 my-corrhizal (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-immunoprecip-itation 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–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.",
keywords = "AM symbiosis, Binding, Co-immunoprecipitation, Heterologous synthesis, Lyk9 mutants, Lysin-motif receptor-like kinase PsLYK9, Microscale thermophoresis, Phytopathogenic fungi, Pisum sativum L, lysin-motif receptor-like kinase PsLYK9, heterologous synthesis, binding, co-immunoprecipitation, lyk9 mutants, microscale thermophoresis, phytopathogenic fungi",
author = "Leppyanen, {Irina V.} and Pavlova, {Olga A.} and Vashurina, {Maria A.} and Bovin, {Andrey D.} and Dolgikh, {Alexandra V.} and Shtark, {Oksana Y.} and Sendersky, {Igor V.} and Dolgikh, {Vyacheslav V.} and Tikhonovich, {Igor A.} and Dolgikh, {Elena A.}",
note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",
year = "2021",
month = jan,
day = "12",
doi = "10.3390/ijms22020711",
language = "English",
volume = "22",
pages = "1--16",
journal = "International Journal of Molecular Sciences",
issn = "1422-0067",
publisher = "MDPI AG",
number = "2",

}

RIS

TY - JOUR

T1 - Lysm receptor-like kinase lyk9 of pisum sativum l. May regulate plant responses to chitooligosaccharides differing in structure

AU - Leppyanen, Irina V.

AU - Pavlova, Olga A.

AU - Vashurina, Maria A.

AU - Bovin, Andrey D.

AU - Dolgikh, Alexandra V.

AU - Shtark, Oksana Y.

AU - Sendersky, Igor V.

AU - Dolgikh, Vyacheslav V.

AU - Tikhonovich, Igor A.

AU - Dolgikh, Elena A.

N1 - Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

PY - 2021/1/12

Y1 - 2021/1/12

N2 - This study focused on the interactions of pea (Pisum sativum L.) plants with phytopatho-genic 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 my-corrhizal (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-immunoprecip-itation 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–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.

AB - This study focused on the interactions of pea (Pisum sativum L.) plants with phytopatho-genic 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 my-corrhizal (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-immunoprecip-itation 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–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.

KW - AM symbiosis

KW - Binding

KW - Co-immunoprecipitation

KW - Heterologous synthesis

KW - Lyk9 mutants

KW - Lysin-motif receptor-like kinase PsLYK9

KW - Microscale thermophoresis

KW - Phytopathogenic fungi

KW - Pisum sativum L

KW - lysin-motif receptor-like kinase PsLYK9

KW - heterologous synthesis

KW - binding

KW - co-immunoprecipitation

KW - lyk9 mutants

KW - microscale thermophoresis

KW - phytopathogenic fungi

UR - http://www.scopus.com/inward/record.url?scp=85099416318&partnerID=8YFLogxK

U2 - 10.3390/ijms22020711

DO - 10.3390/ijms22020711

M3 - Article

C2 - 33445801

AN - SCOPUS:85099416318

VL - 22

SP - 1

EP - 16

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 2

M1 - 711

ER -

ID: 75820898