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Cell cycle-dependent O-GlcNAc modification of tobacco histones and their interaction with the tobacco lectin

The Nicotiana tabacum agglutinin or Nictaba is a nucleocytoplasmic lectin that is expressed in tobacco after the plants have been exposed to jasmonate treatment or insect herbivory. Nictaba specifically recognizes GlcNAc residues. Recently, it was shown that Nictaba is interacting in vitro with the...

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Bibliographic Details
Published in:Plant physiology and biochemistry 2014-10, Vol.83, p.151-158
Main Authors: Delporte, Annelies, De Zaeytijd, Jeroen, De Storme, Nico, Azmi, Abdelkrim, Geelen, Danny, Smagghe, Guy, Guisez, Yves, Van Damme, Els J.M.
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Language:English
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Summary:The Nicotiana tabacum agglutinin or Nictaba is a nucleocytoplasmic lectin that is expressed in tobacco after the plants have been exposed to jasmonate treatment or insect herbivory. Nictaba specifically recognizes GlcNAc residues. Recently, it was shown that Nictaba is interacting in vitro with the core histone proteins from calf thymus. Assuming that plant histones – similar to their animal counterparts – undergo O-GlcNAcylation, this interaction presumably occurs through binding of the lectin to the O-GlcNAc modification present on the histones. Hereupon, the question was raised whether this modification also occurs in plants and if it is cell cycle dependent. To this end, histones were purified from tobacco BY-2 suspension cells and the presence of O-GlcNAc modifications was checked. Concomitantly, O-GlcNAcylation of histone proteins was studied. Our data show that similar to animal histones plant histones are modified by O-GlcNAc in a cell cycle-dependent fashion. In addition, the interaction between Nictaba and tobacco histones was confirmed using lectin chromatography and far Western blot analysis. Collectively these findings suggest that Nictaba can act as a modulator of gene transcription through its interaction with core histones. •Histones were purified from tobacco BY-2 cells.•O-GlcNAc modification of plant histones was shown to be cell cycle dependent.•Interaction between plant histones and tobacco lectin was proven.
ISSN:0981-9428
1873-2690
DOI:10.1016/j.plaphy.2014.07.021