In vivo interaction between the tobacco lectin and the core histone proteins.

Nictaba, a lectin accumulating in tobacco (Nicotiana tabacum) leaves treated with jasmonate, is considered to act as a signaling protein in the stress physiology of the plant. Immunolocalization studies revealed that Nictaba has a nucleocytoplasmic localization. In previous research, histones were identified as primary interaction partners for Nictaba. Here, the interaction between Nictaba and tobacco histones was scrutinized in vivo. Localization studies, performed in stably transformed Nicotiana benthamiana plants, confirmed the nucleocytoplasmic localization of the lectin and colocalization with the presumed binding partners in the nucleus. Furthermore, bimolecular fluorescence complementation (BiFC) assays confirmed the interaction in vivo. Since BiFC signals were also observed for a Nictaba mutant incapable of binding sugar moieties, this interaction may be mediated by alternative binding sites. The interaction of Nictaba with core histones possibly reflects a role of this stress inducible lectin in gene regulation or chromatin remodeling.