Interaction of the tobacco lectin with histone proteins
- Author
- Dieter Schouppe (UGent) , Bart Ghesquière (UGent) , Gerben Menschaert (UGent) , Winnok De Vos (UGent) , Stéphanie Bourque, Geert Trooskens (UGent) , Paul Proost, Kris Gevaert (UGent) and Els Van Damme (UGent)
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- Abstract
- The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells. Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant. In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells. Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins. Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column. Elution of Nictaba-interacting histone proteins was achieved with 1 M N-acetylglucosamine (GlcNAc). Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc. Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
- Keywords
- EXPRESSION, BINDING, GLYCOPROTEINS, GENES, RESPONSES, STRESS, PLANT-LECTINS, N-ACETYLGLUCOSAMINE
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-1197590
- MLA
- Schouppe, Dieter, et al. “Interaction of the Tobacco Lectin with Histone Proteins.” PLANT PHYSIOLOGY, vol. 155, no. 3, 2011, pp. 1091–102, doi:10.1104/pp.110.170134.
- APA
- Schouppe, D., Ghesquière, B., Menschaert, G., De Vos, W., Bourque, S., Trooskens, G., … Van Damme, E. (2011). Interaction of the tobacco lectin with histone proteins. PLANT PHYSIOLOGY, 155(3), 1091–1102. https://doi.org/10.1104/pp.110.170134
- Chicago author-date
- Schouppe, Dieter, Bart Ghesquière, Gerben Menschaert, Winnok De Vos, Stéphanie Bourque, Geert Trooskens, Paul Proost, Kris Gevaert, and Els Van Damme. 2011. “Interaction of the Tobacco Lectin with Histone Proteins.” PLANT PHYSIOLOGY 155 (3): 1091–1102. https://doi.org/10.1104/pp.110.170134.
- Chicago author-date (all authors)
- Schouppe, Dieter, Bart Ghesquière, Gerben Menschaert, Winnok De Vos, Stéphanie Bourque, Geert Trooskens, Paul Proost, Kris Gevaert, and Els Van Damme. 2011. “Interaction of the Tobacco Lectin with Histone Proteins.” PLANT PHYSIOLOGY 155 (3): 1091–1102. doi:10.1104/pp.110.170134.
- Vancouver
- 1.Schouppe D, Ghesquière B, Menschaert G, De Vos W, Bourque S, Trooskens G, et al. Interaction of the tobacco lectin with histone proteins. PLANT PHYSIOLOGY. 2011;155(3):1091–102.
- IEEE
- [1]D. Schouppe et al., “Interaction of the tobacco lectin with histone proteins,” PLANT PHYSIOLOGY, vol. 155, no. 3, pp. 1091–1102, 2011.
@article{1197590, abstract = {{The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells. Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant. In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells. Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins. Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column. Elution of Nictaba-interacting histone proteins was achieved with 1 M N-acetylglucosamine (GlcNAc). Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc. Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.}}, author = {{Schouppe, Dieter and Ghesquière, Bart and Menschaert, Gerben and De Vos, Winnok and Bourque, Stéphanie and Trooskens, Geert and Proost, Paul and Gevaert, Kris and Van Damme, Els}}, issn = {{0032-0889}}, journal = {{PLANT PHYSIOLOGY}}, keywords = {{EXPRESSION,BINDING,GLYCOPROTEINS,GENES,RESPONSES,STRESS,PLANT-LECTINS,N-ACETYLGLUCOSAMINE}}, language = {{eng}}, number = {{3}}, pages = {{1091--1102}}, title = {{Interaction of the tobacco lectin with histone proteins}}, url = {{http://doi.org/10.1104/pp.110.170134}}, volume = {{155}}, year = {{2011}}, }
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