Alteration of gibberellin response in transgenic tobacco plants which express a human Lewis fucosyltransferase.

In plants, Lewisa type N-glycans may be involved in cell-to-cell communication and recognition. N-glycoproteins harboring Lewisa glycotopes are mainly found in plasma membranes and cell walls. Some can be also involved in cell wall synthesis or the loosening process, and subsequently in cell elongation. In order to determine the potential role(s) of the alpha4-fucosylation during vegetative development, transgenic tobacco plants overexpressing a human Lewis fucosyltransferase (hFUT3), which transfers a fucose residue in a alpha(1,4)-linkage on complex glycans, have been developed. The heterologous enzyme hFUT3 was strongly expressed and fully functional in transgenic tobacco. Transgenic plants showed a delay in growth linked to a reduction of internode length. Furthermore, transgenic seedling roots were significantly shorter than wild-type roots and the length of their epidermis cells was reduced. Strikingly, root growth was completely and specifically restored following gibberellin treatment. Etiolated hypocotyls of hFUT3 overexpressors were also more sensitive to exogenous gibberellin. Furthermore, paclobutrazol, an inhibitor of gibberellin synthesis, induced a similar effect on control and transgenic dark-grown hypocotyls suggesting that gibberellin biosynthesis was probably not altered in seedlings overexpressing hFUT3. Thus, alpha4-fucosylation could act as a possible modulator of conformation and/or functioning of N-glycoproteins involved in the gibberellin-dependent elongation process.