Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding. / Broghammer, Angelique; Krusell, Lene; Blaise, Mickaël; Sauer, Jørgen; Sullivan, John T; Maolanon, Nicolai Nareth; Vinther, Maria; Lorentzen, Andrea Maria; Madsen, Esben B; Jensen, Knud J; Roepstorff, Peter; Thirup, Søren Skou; Ronson, Clive W; Thygesen, Mikkel B; Stougaard, Jens.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 109, Nr. 34, 21.08.2012, s. 13859-13864.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Broghammer, A, Krusell, L, Blaise, M, Sauer, J, Sullivan, JT, Maolanon, NN, Vinther, M, Lorentzen, AM, Madsen, EB, Jensen, KJ, Roepstorff, P, Thirup, SS, Ronson, CW, Thygesen, MB & Stougaard, J 2012, 'Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding', Proceedings of the National Academy of Sciences of the United States of America, bind 109, nr. 34, s. 13859-13864. https://doi.org/10.1073/pnas.1205171109

APA

Broghammer, A., Krusell, L., Blaise, M., Sauer, J., Sullivan, J. T., Maolanon, N. N., Vinther, M., Lorentzen, A. M., Madsen, E. B., Jensen, K. J., Roepstorff, P., Thirup, S. S., Ronson, C. W., Thygesen, M. B., & Stougaard, J. (2012). Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding. Proceedings of the National Academy of Sciences of the United States of America, 109(34), 13859-13864. https://doi.org/10.1073/pnas.1205171109

CBE

Broghammer A, Krusell L, Blaise M, Sauer J, Sullivan JT, Maolanon NN, Vinther M, Lorentzen AM, Madsen EB, Jensen KJ, Roepstorff P, Thirup SS, Ronson CW, Thygesen MB, Stougaard J. 2012. Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding. Proceedings of the National Academy of Sciences of the United States of America. 109(34):13859-13864. https://doi.org/10.1073/pnas.1205171109

MLA

Broghammer, Angelique o.a.. "Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding". Proceedings of the National Academy of Sciences of the United States of America. 2012, 109(34). 13859-13864. https://doi.org/10.1073/pnas.1205171109

Vancouver

Broghammer A, Krusell L, Blaise M, Sauer J, Sullivan JT, Maolanon NN o.a. Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding. Proceedings of the National Academy of Sciences of the United States of America. 2012 aug 21;109(34):13859-13864. https://doi.org/10.1073/pnas.1205171109

Author

Broghammer, Angelique ; Krusell, Lene ; Blaise, Mickaël ; Sauer, Jørgen ; Sullivan, John T ; Maolanon, Nicolai Nareth ; Vinther, Maria ; Lorentzen, Andrea Maria ; Madsen, Esben B ; Jensen, Knud J ; Roepstorff, Peter ; Thirup, Søren Skou ; Ronson, Clive W ; Thygesen, Mikkel B ; Stougaard, Jens. / Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding. I: Proceedings of the National Academy of Sciences of the United States of America. 2012 ; Bind 109, Nr. 34. s. 13859-13864.

Bibtex

@article{4790762798bc44a2b7bf2ee6c7b69a40,
title = "Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding",
abstract = "Lipochitin oligosaccharides called Nod factors function as primary rhizobial signal molecules triggering legumes to develop new plant organs: root nodules that host the bacteria as nitrogen-fixing bacteroids. Here, we show that the Lotus japonicus Nod factor receptor 5 (NFR5) and Nod factor receptor 1 (NFR1) bind Nod factor directly at high-affinity binding sites. Both receptor proteins were posttranslationally processed when expressed as fusion proteins and extracted from purified membrane fractions of Nicotiana benthamiana or Arabidopsis thaliana. The N-terminal signal peptides were cleaved, and NFR1 protein retained its in vitro kinase activity. Processing of NFR5 protein was characterized by determining the N-glycosylation patterns of the ectodomain. Two different glycan structures with identical composition, Man(3)XylFucGlcNAc(4), were identified by mass spectrometry and located at amino acid positions N68 and N198. Receptor-ligand interaction was measured by using ligands that were labeled or immobilized by application of chemoselective chemistry at the anomeric center. High-affinity ligand binding was demonstrated with both solid-phase and free solution techniques. The K(d) values obtained for Nod factor binding were in the nanomolar range and comparable to the concentration range sufficient for biological activity. Structure-dependent ligand specificity was shown by using chitin oligosaccharides. Taken together, our results suggest that ligand recognition through direct ligand binding is a key step in the receptor-mediated activation mechanism leading to root nodule development in legumes.",
keywords = "Amino Acid Motifs, Binding Sites, Fabaceae, Kinetics, Ligands, Mass Spectrometry, Models, Biological, Mucoproteins, Oligosaccharides, Phosphorylation, Plant Proteins, Plants, Polysaccharides, Protein Binding, Rhizobium, Symbiosis",
author = "Angelique Broghammer and Lene Krusell and Micka{\"e}l Blaise and J{\o}rgen Sauer and Sullivan, {John T} and Maolanon, {Nicolai Nareth} and Maria Vinther and Lorentzen, {Andrea Maria} and Madsen, {Esben B} and Jensen, {Knud J} and Peter Roepstorff and Thirup, {S{\o}ren Skou} and Ronson, {Clive W} and Thygesen, {Mikkel B} and Jens Stougaard",
year = "2012",
month = aug,
day = "21",
doi = "10.1073/pnas.1205171109",
language = "English",
volume = "109",
pages = "13859--13864",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "34",

}

RIS

TY - JOUR

T1 - Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding

AU - Broghammer, Angelique

AU - Krusell, Lene

AU - Blaise, Mickaël

AU - Sauer, Jørgen

AU - Sullivan, John T

AU - Maolanon, Nicolai Nareth

AU - Vinther, Maria

AU - Lorentzen, Andrea Maria

AU - Madsen, Esben B

AU - Jensen, Knud J

AU - Roepstorff, Peter

AU - Thirup, Søren Skou

AU - Ronson, Clive W

AU - Thygesen, Mikkel B

AU - Stougaard, Jens

PY - 2012/8/21

Y1 - 2012/8/21

N2 - Lipochitin oligosaccharides called Nod factors function as primary rhizobial signal molecules triggering legumes to develop new plant organs: root nodules that host the bacteria as nitrogen-fixing bacteroids. Here, we show that the Lotus japonicus Nod factor receptor 5 (NFR5) and Nod factor receptor 1 (NFR1) bind Nod factor directly at high-affinity binding sites. Both receptor proteins were posttranslationally processed when expressed as fusion proteins and extracted from purified membrane fractions of Nicotiana benthamiana or Arabidopsis thaliana. The N-terminal signal peptides were cleaved, and NFR1 protein retained its in vitro kinase activity. Processing of NFR5 protein was characterized by determining the N-glycosylation patterns of the ectodomain. Two different glycan structures with identical composition, Man(3)XylFucGlcNAc(4), were identified by mass spectrometry and located at amino acid positions N68 and N198. Receptor-ligand interaction was measured by using ligands that were labeled or immobilized by application of chemoselective chemistry at the anomeric center. High-affinity ligand binding was demonstrated with both solid-phase and free solution techniques. The K(d) values obtained for Nod factor binding were in the nanomolar range and comparable to the concentration range sufficient for biological activity. Structure-dependent ligand specificity was shown by using chitin oligosaccharides. Taken together, our results suggest that ligand recognition through direct ligand binding is a key step in the receptor-mediated activation mechanism leading to root nodule development in legumes.

AB - Lipochitin oligosaccharides called Nod factors function as primary rhizobial signal molecules triggering legumes to develop new plant organs: root nodules that host the bacteria as nitrogen-fixing bacteroids. Here, we show that the Lotus japonicus Nod factor receptor 5 (NFR5) and Nod factor receptor 1 (NFR1) bind Nod factor directly at high-affinity binding sites. Both receptor proteins were posttranslationally processed when expressed as fusion proteins and extracted from purified membrane fractions of Nicotiana benthamiana or Arabidopsis thaliana. The N-terminal signal peptides were cleaved, and NFR1 protein retained its in vitro kinase activity. Processing of NFR5 protein was characterized by determining the N-glycosylation patterns of the ectodomain. Two different glycan structures with identical composition, Man(3)XylFucGlcNAc(4), were identified by mass spectrometry and located at amino acid positions N68 and N198. Receptor-ligand interaction was measured by using ligands that were labeled or immobilized by application of chemoselective chemistry at the anomeric center. High-affinity ligand binding was demonstrated with both solid-phase and free solution techniques. The K(d) values obtained for Nod factor binding were in the nanomolar range and comparable to the concentration range sufficient for biological activity. Structure-dependent ligand specificity was shown by using chitin oligosaccharides. Taken together, our results suggest that ligand recognition through direct ligand binding is a key step in the receptor-mediated activation mechanism leading to root nodule development in legumes.

KW - Amino Acid Motifs

KW - Binding Sites

KW - Fabaceae

KW - Kinetics

KW - Ligands

KW - Mass Spectrometry

KW - Models, Biological

KW - Mucoproteins

KW - Oligosaccharides

KW - Phosphorylation

KW - Plant Proteins

KW - Plants

KW - Polysaccharides

KW - Protein Binding

KW - Rhizobium

KW - Symbiosis

U2 - 10.1073/pnas.1205171109

DO - 10.1073/pnas.1205171109

M3 - Journal article

C2 - 22859506

VL - 109

SP - 13859

EP - 13864

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 34

ER -