Ghent University Academic Bibliography

Advanced

Interaction of the tobacco lectin with histone proteins

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 (2011) PLANT PHYSIOLOGY. 155(3). p.1091-1102
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
EXPRESSION, BINDING, GLYCOPROTEINS, GENES, RESPONSES, STRESS, PLANT-LECTINS, N-ACETYLGLUCOSAMINE
journal title
PLANT PHYSIOLOGY
Plant Physiol.
volume
155
issue
3
pages
1091 - 1102
Web of Science type
Article
Web of Science id
000287843800005
JCR category
PLANT SCIENCES
JCR impact factor
6.535 (2011)
JCR rank
7/189 (2011)
JCR quartile
1 (2011)
ISSN
0032-0889
DOI
10.1104/pp.110.170134
project
Center for nano- and biophotonics (NB-Photonics)
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1197590
handle
http://hdl.handle.net/1854/LU-1197590
date created
2011-03-28 10:18:14
date last changed
2013-02-27 09:02:08
@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 Ghesqui{\`e}re, Bart and Menschaert, Gerben and De Vos, Winnok and Bourque, St{\'e}phanie and Trooskens, Geert and Proost, Paul and Gevaert, Kris and Van Damme, Els},
  issn         = {0032-0889},
  journal      = {PLANT PHYSIOLOGY},
  keyword      = {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://dx.doi.org/10.1104/pp.110.170134},
  volume       = {155},
  year         = {2011},
}

Chicago
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.
APA
Schouppe, D., Ghesquière, B., Menschaert, G., De Vos, W., Bourque, S., Trooskens, G., Proost, P., et al. (2011). Interaction of the tobacco lectin with histone proteins. PLANT PHYSIOLOGY, 155(3), 1091–1102.
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.
MLA
Schouppe, Dieter, Bart Ghesquière, Gerben Menschaert, et al. “Interaction of the Tobacco Lectin with Histone Proteins.” PLANT PHYSIOLOGY 155.3 (2011): 1091–1102. Print.