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Interaction of the Tobacco Lectin with Histone Proteins

Dieter Schouppe, Bart Ghesquière, Gerben Menschaert, Winnok H. De vos, Stéphane Bourque, Geert Trooskens, Paul Proost, Kris Gevaert and Els J.M. Van Damme
Plant Physiology
Vol. 155, No. 3 (March 2011), pp. 1091-1102
Stable URL: http://www.jstor.org/stable/41434184
Page Count: 12
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Interaction of the Tobacco Lectin with Histone Proteins
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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 signalilng 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 column. Elution of Nictaba-interacting using affinity chromatography of purified calf thyms histone proteins on a Nictaba column. Elution of Nictaba-interacting histone proteins was acheived with 1 m N-acetylglucosamine (GIcNAc). Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GIcNac. 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-GicNAcylated proteins in the plant cell nucleus.

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